Fibrinogen and fibrin: An illustrated review

Since its discovery over 350 years ago, studies of fibrinogen have revealed remarkable characteristics. Its complex structure as a large (340 kDa) hexameric homodimer supports complex roles in hemostasis and homeostasis. Fibrinogen synthesis is regulated at the transcriptional and translational leve...

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Published inResearch and practice in thrombosis and haemostasis Vol. 3; no. 2; pp. 161 - 172
Main Authors Pieters, Marlien, Wolberg, Alisa S.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.04.2019
Elsevier Limited
John Wiley and Sons Inc
Subjects
factor XIII
fibrin
fibrinogen
fibrinolysis
Gene expression
hemostasis
Illustrated Review
infection
thrombosis
fibrinolysis
infection
thrombosis
fibrinogen
factor XIII
hemostasis
fibrin
Online AccessGet full text
ISSN2475-0379
2475-0379
DOI10.1002/rth2.12191

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Abstract Since its discovery over 350 years ago, studies of fibrinogen have revealed remarkable characteristics. Its complex structure as a large (340 kDa) hexameric homodimer supports complex roles in hemostasis and homeostasis. Fibrinogen synthesis is regulated at the transcriptional and translational levels, undergoing both constitutive (basal) secretion from liver, and inducible upregulation in response to inflammatory events. In addition, alternative splicing yields fibrinogen variants with unique properties and contributions to coagulation biochemistry. During coagulation, fibrinogen conversion to fibrin occurs via thrombin‐mediated proteolytic cleavage that produces intermediate protofibrils and then mature fibers that provide remarkable biochemical and mechanical stability to clots. Fibrin formation, structure, and stability are regulated by various genetic, biochemical, and environmental factors, allowing for dynamic kinetics of fibrin formation and structure. Interactions between fibrinogen and/or fibrin and plasma proteins and receptors on platelets, leukocytes, endothelial cells, and other cells enable complex functions in hemostasis, thrombosis, pregnancy, inflammation, infection, cancer, and other pathologies. Disorders in fibrinogen concentration and/or function increase risk of bleeding, thrombosis, and infection. This illustrated review covers fundamental aspects of fibrinogen and fibrin biology, biochemistry, biophysics, epidemiology, and clinical applications. Continued efforts to enhance our understanding of fibrinogen and fibrin in these processes are likely to advance treatment and prevention of many human diseases.
AbstractList Since its discovery over 350 years ago, studies of fibrinogen have revealed remarkable characteristics. Its complex structure as a large (340 kDa) hexameric homodimer supports complex roles in hemostasis and homeostasis. Fibrinogen synthesis is regulated at the transcriptional and translational levels, undergoing both constitutive (basal) secretion from liver, and inducible upregulation in response to inflammatory events. In addition, alternative splicing yields fibrinogen variants with unique properties and contributions to coagulation biochemistry. During coagulation, fibrinogen conversion to fibrin occurs via thrombin‐mediated proteolytic cleavage that produces intermediate protofibrils and then mature fibers that provide remarkable biochemical and mechanical stability to clots. Fibrin formation, structure, and stability are regulated by various genetic, biochemical, and environmental factors, allowing for dynamic kinetics of fibrin formation and structure. Interactions between fibrinogen and/or fibrin and plasma proteins and receptors on platelets, leukocytes, endothelial cells, and other cells enable complex functions in hemostasis, thrombosis, pregnancy, inflammation, infection, cancer, and other pathologies. Disorders in fibrinogen concentration and/or function increase risk of bleeding, thrombosis, and infection. This illustrated review covers fundamental aspects of fibrinogen and fibrin biology, biochemistry, biophysics, epidemiology, and clinical applications. Continued efforts to enhance our understanding of fibrinogen and fibrin in these processes are likely to advance treatment and prevention of many human diseases.
Since its discovery over 350 years ago, studies of fibrinogen have revealed remarkable characteristics. Its complex structure as a large (340 kDa) hexameric homodimer supports complex roles in hemostasis and homeostasis. Fibrinogen synthesis is regulated at the transcriptional and translational levels, undergoing both constitutive (basal) secretion from liver, and inducible upregulation in response to inflammatory events. In addition, alternative splicing yields fibrinogen variants with unique properties and contributions to coagulation biochemistry. During coagulation, fibrinogen conversion to fibrin occurs via thrombin-mediated proteolytic cleavage that produces intermediate protofibrils and then mature fibers that provide remarkable biochemical and mechanical stability to clots. Fibrin formation, structure, and stability are regulated by various genetic, biochemical, and environmental factors, allowing for dynamic kinetics of fibrin formation and structure. Interactions between fibrinogen and/or fibrin and plasma proteins and receptors on platelets, leukocytes, endothelial cells, and other cells enable complex functions in hemostasis, thrombosis, pregnancy, inflammation, infection, cancer, and other pathologies. Disorders in fibrinogen concentration and/or function increase risk of bleeding, thrombosis, and infection. This illustrated review covers fundamental aspects of fibrinogen and fibrin biology, biochemistry, biophysics, epidemiology, and clinical applications. Continued efforts to enhance our understanding of fibrinogen and fibrin in these processes are likely to advance treatment and prevention of many human diseases.Since its discovery over 350 years ago, studies of fibrinogen have revealed remarkable characteristics. Its complex structure as a large (340 kDa) hexameric homodimer supports complex roles in hemostasis and homeostasis. Fibrinogen synthesis is regulated at the transcriptional and translational levels, undergoing both constitutive (basal) secretion from liver, and inducible upregulation in response to inflammatory events. In addition, alternative splicing yields fibrinogen variants with unique properties and contributions to coagulation biochemistry. During coagulation, fibrinogen conversion to fibrin occurs via thrombin-mediated proteolytic cleavage that produces intermediate protofibrils and then mature fibers that provide remarkable biochemical and mechanical stability to clots. Fibrin formation, structure, and stability are regulated by various genetic, biochemical, and environmental factors, allowing for dynamic kinetics of fibrin formation and structure. Interactions between fibrinogen and/or fibrin and plasma proteins and receptors on platelets, leukocytes, endothelial cells, and other cells enable complex functions in hemostasis, thrombosis, pregnancy, inflammation, infection, cancer, and other pathologies. Disorders in fibrinogen concentration and/or function increase risk of bleeding, thrombosis, and infection. This illustrated review covers fundamental aspects of fibrinogen and fibrin biology, biochemistry, biophysics, epidemiology, and clinical applications. Continued efforts to enhance our understanding of fibrinogen and fibrin in these processes are likely to advance treatment and prevention of many human diseases.
Since its discovery over 350 years ago, studies of fibrinogen have revealed remarkable characteristics. Its complex structure as a large (340 kDa) hexameric homodimer supports complex roles in hemostasis and homeostasis. Fibrinogen synthesis is regulated at the transcriptional and translational levels, undergoing both constitutive (basal) secretion from liver, and inducible upregulation in response to inflammatory events. In addition, alternative splicing yields fibrinogen variants with unique properties and contributions to coagulation biochemistry. During coagulation, fibrinogen conversion to fibrin occurs via thrombin‐mediated proteolytic cleavage that produces intermediate protofibrils and then mature fibers that provide remarkable biochemical and mechanical stability to clots. Fibrin formation, structure, and stability are regulated by various genetic, biochemical, and environmental factors, allowing for dynamic kinetics of fibrin formation and structure. Interactions between fibrinogen and/or fibrin and plasma proteins and receptors on platelets, leukocytes, endothelial cells, and other cells enable complex functions in hemostasis, thrombosis, pregnancy, inflammation, infection, cancer, and other pathologies. Disorders in fibrinogen concentration and/or function increase risk of bleeding, thrombosis, and infection. This illustrated review covers fundamental aspects of fibrinogen and fibrin biology, biochemistry, biophysics, epidemiology, and clinical applications. Continued efforts to enhance our understanding of fibrinogen and fibrin in these processes are likely to advance treatment and prevention of many human diseases.
Since its discovery over 350 years ago, studies of fibrinogen have revealed remarkable characteristics. Its complex structure as a large (340  kD a) hexameric homodimer supports complex roles in hemostasis and homeostasis. Fibrinogen synthesis is regulated at the transcriptional and translational levels, undergoing both constitutive (basal) secretion from liver, and inducible upregulation in response to inflammatory events. In addition, alternative splicing yields fibrinogen variants with unique properties and contributions to coagulation biochemistry. During coagulation, fibrinogen conversion to fibrin occurs via thrombin‐mediated proteolytic cleavage that produces intermediate protofibrils and then mature fibers that provide remarkable biochemical and mechanical stability to clots. Fibrin formation, structure, and stability are regulated by various genetic, biochemical, and environmental factors, allowing for dynamic kinetics of fibrin formation and structure. Interactions between fibrinogen and/or fibrin and plasma proteins and receptors on platelets, leukocytes, endothelial cells, and other cells enable complex functions in hemostasis, thrombosis, pregnancy, inflammation, infection, cancer, and other pathologies. Disorders in fibrinogen concentration and/or function increase risk of bleeding, thrombosis, and infection. This illustrated review covers fundamental aspects of fibrinogen and fibrin biology, biochemistry, biophysics, epidemiology, and clinical applications. Continued efforts to enhance our understanding of fibrinogen and fibrin in these processes are likely to advance treatment and prevention of many human diseases.
Author Pieters, Marlien
Wolberg, Alisa S.
AuthorAffiliation 1 Center of Excellence for Nutrition North‐West University Potchefstroom South Africa
2 Department of Pathology and Laboratory Medicine University of North Carolina Chapel Hill North Carolina
AuthorAffiliation_xml – name: 2 Department of Pathology and Laboratory Medicine University of North Carolina Chapel Hill North Carolina
– name: 1 Center of Excellence for Nutrition North‐West University Potchefstroom South Africa
Author_xml – sequence: 1
  givenname: Marlien
  orcidid: 0000-0003-2849-6370
  surname: Pieters
  fullname: Pieters, Marlien
  organization: Center of Excellence for Nutrition, North‐West University, Potchefstroom, South Africa
– sequence: 2
  givenname: Alisa S.
  orcidid: 0000-0002-2845-2303
  surname: Wolberg
  fullname: Wolberg, Alisa S.
  email: alisa.wolberg@med.unc.edu
  organization: Department of Pathology and Laboratory Medicine, University of North Carolina, Chapel Hill, North Carolina
BackLink https://www.ncbi.nlm.nih.gov/pubmed/31011700$$D View this record in MEDLINE/PubMed
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Cites_doi 10.1160/TH13-10-0855
10.1038/s41598-017-06383-w
10.1091/mbc.1.12.883
10.1182/blood-2010-06-290338
10.1016/S0006-291X(88)80866-0
10.1016/j.bpj.2010.08.060
10.1055/s-0038-1648188
10.1016/j.matbio.2016.10.005
10.2174/187152508784871963
10.1172/JCI109671
10.1055/s-0029-1234141
10.1016/j.bpj.2011.11.4016
10.1111/j.1538-7836.2007.02504.x
10.1161/ATVBAHA.111.230631
10.1155/2017/2748340
10.1172/JCI75386
10.1371/journal.pone.0074682
10.1160/TH14-06-0514
10.1172/JCI98734
10.1182/blood-2012-09-306639
10.1182/blood.V79.6.1420.1420
10.1172/JCI20741
10.1002/rth2.12127
10.1055/s-0036-1572353
10.1111/jth.14248
10.1182/blood-2013-12-547182
10.1111/jth.14216
10.1101/gad.9.16.2020
10.1093/rheumatology/key089
10.1182/blood-2015-04-639849
10.1182/blood-2017-07-798306
10.1182/blood-2015-06-652214
10.1093/imammb/dqs029
10.1182/blood-2005-10-4168
10.1016/S0021-9258(19)38316-4
10.1111/j.1538-7836.2012.04717.x
10.1161/01.ATV.0000041037.06509.C2
10.1055/s-0037-1613195
10.1016/S0021-9258(19)44960-0
10.1182/blood-2009-05-217968
10.1093/eurheartj/ehy013
10.1017/S0025727300060385
10.1021/bi00313a033
10.1182/blood-2015-04-641654
10.1182/blood-2015-06-652263
10.1182/blood.V92.12.4721
10.1161/01.ATV.0000136649.83297.bf
10.1016/j.thromres.2014.08.018
10.1160/TH12-04-0273
10.1055/s-0037-1613368
10.1111/jth.12229
10.1161/01.CIR.92.7.1883
10.1021/bi802205g
10.1182/blood-2007-01-066837
10.1111/jth.13354
10.1371/journal.pone.0116350
10.2174/187152508784871981
10.1160/th14-02-0184
10.1111/j.1749-6632.2001.tb03535.x
10.1126/science.1127317
10.1016/j.actbio.2017.07.037
10.1073/pnas.0804865105
10.1074/jbc.273.42.27220
10.1016/j.thromres.2016.01.008
10.1161/01.ATV.20.5.1354
10.1182/blood-2005-05-2150
10.1016/j.blre.2006.11.001
10.1002/j.1460-2075.1996.tb00962.x
ContentType Journal Article
Copyright 2019 The Authors. Research and Practice in Thrombosis and Haemostasis published by Wiley Periodicals, Inc on behalf of International Society on Thrombosis and Haemostasis.
2019 The Authors. published by Wiley Periodicals, Inc on behalf of International Society on Thrombosis and Haemostasis.
2019. This work is published under http://creativecommons.org/licenses/by-nc-nd/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Copyright_xml – notice: 2019 The Authors. Research and Practice in Thrombosis and Haemostasis published by Wiley Periodicals, Inc on behalf of International Society on Thrombosis and Haemostasis.
– notice: 2019 The Authors. published by Wiley Periodicals, Inc on behalf of International Society on Thrombosis and Haemostasis.
– notice: 2019. This work is published under http://creativecommons.org/licenses/by-nc-nd/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
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DOI 10.1002/rth2.12191
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Issue 2
Keywords fibrinolysis
infection
thrombosis
fibrinogen
factor XIII
hemostasis
fibrin
Language English
License This is an open access article under the CC BY-NC-ND license.
http://creativecommons.org/licenses/by-nc-nd/4.0
Attribution-NonCommercial-NoDerivs
This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.
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Notes Funding information
M. Pieters is supported by funding from the South African Medical Research Council and the Academy of Medical Sciences UK (Newton Fund Advanced Fellowship Grant). A.S. Wolberg is supported by funding from the National Institutes of Health (R01HL126974)
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References Fish, Di Sanza, Neerman‐Arbez (bb0285) 2014; 123
Cho, Mosher (bb0115) 2006; 107
Cronje, Nienaber‐Rousseau, Zandberg (bb0210) 2017; 60–61
Collet, Moen, Veklich, Gorkun, Lord, Montalescot (bb0085) 2005; 106
Kotze, Ariens, de Lange, Pieters (bb0330) 2014; 134
Gulledge, McShea, Schwartz, Koch, Lord (bb0275) 2003; 23
Valnickova, Enghild (bb0110) 1998; 273
Alshehri, Hughes, Montague, Watson, Frampton, Bender (bb0230) 2015; 126
Sakharov, Rijken (bb0180) 1995; 92
Bannish, Keener, Fogelson (bb0175) 2014; 31
Espitia Jaimes, Fish, Neerman‐Arbez (bb0020) 2018; 16
Sakata, Aoki (bb0105) 1980; 65
Li, Sigley, Baker, Helms, Kinney, Pieters (bb0050) 2017; 2017
Kollman, Pandi, Sawaya, Riley, Doolittle (bb0015) 2009; 48
Smith, Bornikova, Noetzli, Guglielmone, Minoldo, Backos (bb0295) 2018; 2
Suh, Holmback, Jensen, Daugherty, Small, Simon (bb0260) 1995; 9
Weisel, Litvinov (bb0045) 2013; 121
Bucay, O'Brien, Wulfe, Superfine, Wolberg, Falvo (bb0170) 2015; 10
Longstaff, Thelwell, Williams, Silva, Szabo, Kolev (bb0165) 2011; 117
Undas, Ariens (bb0310) 2011; 31
Bannish, Chernysh, Keener, Fogelson, Weisel (bb0140) 2017; 7
Standeven, Uitte de Willige, Carter, Grant (bb0205) 2009; 35
Fish, Neerman‐Arbez (bb0025) 2012; 108
Collet, Park, Lesty, Soria, Soria, Montalescot (bb0145) 2000; 20
Holmback, Danton, Suh, Daugherty, Degen (bb0255) 1996; 15
Altieri, Agbanyo, Plescia, Ginsberg, Edgington, Plow (bb0240) 1990; 265
Forrester (bb0010) 1995; 39
Helms, Ariens, Uitte de Willige, Standeven, Guthold (bb0100) 2012; 102
Weisel, Litvinov (bb0160) 2008; 6
Folsom, Tang, George, Heckbert, MacLehose, Cushman (bb0335) 2016; 139
Veklich, Francis, White, Weisel (bb0150) 1998; 92
Li, Lucioni, Li, Bonin, Cho, Guthold (bb0195) 2017; 60
Vo, Swaroop, Liu, Norris, Shavit (bb0280) 2013; 8
Houser, Hudson, Ping, Superfine, Lord (bb0130) 2010; 99
Mosesson, Finlayson, Umfleet (bb0035) 1972; 247
Hoffman (bb0215) 2008; 6
Redman, Xia (bb0030) 2001; 936
Kunitada, FitzGerald, Fitzgerald (bb0190) 1992; 79
Aleman, Byrnes, Wang, Tran, Lam, Di Paola (bb0270) 2014; 124
Trezzini, Jungi, Kuhnert, Peterhans (bb0235) 1988; 156
Solomon, Groner, Ye, Pendrak (bb0300) 2015; 113
Macrae, Duval, Papareddy, Baker, Yuldasheva, Kearney (bb0060) 2018; 128
Hudson (bb0155) 2017; 2017
O'Brien, Falvo, Millard, Eastwood, Taylor, Superfine (bb0055) 2008; 105
Rijken, Abdul, Malfliet, Leebeek, Uitte de Willige (bb0095) 2016; 14
Bridge, Philippou, Ariens (bb0225) 2014; 112
Byrnes, Duval, Wang, Hansen, Ahn, Mooberry (bb0090) 2015; 126
Wolberg (bb0220) 2007; 21
Standeven, Carter, Grant, Weisel, Chernysh, Masova (bb0080) 2007; 110
Uitte de Willige, Standeven, Philippou, Ariens (bb0350) 2009; 114
Allan, Uitte de Willige, Abou‐Saleh, Connell, Ariens (bb0070) 2012; 1
Cieslik, Mrozinska, Broniatowska, Undas (bb0315) 2018; 131
Weisel (bb0125) 2007; 5
Casini, Undas, Palla, Thachil, de Moerloose (bb0290) 2018; 16
O'Toole, Loftus, Du, Glass, Ruggeri, Shattil (bb0245) 1990; 1
Macrae, Domingues, Casini, Ariens (bb0340) 2016; 42
Chung, Davie (bb0040) 1984; 23
Medved, Nieuwenhuizen (bb0135) 2003; 89
Ariens (bb0305) 2013; 11
Prasad, Gorkun, Raghu, Thornton, Mullins, Palumbo (bb0250) 2015; 126
Liu, Jawerth, Sparks, Falvo, Hantgan, Superfine (bb0120) 2006; 313
Flick, Du, Witte, Jirousková, Soloviev, Busuttil (bb0265) 2004; 113
Duval, Allan, Connell, Ridger, Philippou, Ariens (bb0075) 2014; 111
Celinska‐Lowenhoff, Zabczyk, Iwaniec, Plens, Musial, Undas (bb0325) 2018; 57
Scott, Ariens, Grant (bb0200) 2004; 24
Domingues, Macrae, Duval, McPherson, Bridge, Ajjan (bb0065) 2016; 127
Sumaya, Wallentin, James, Siegbahn, Gabrysch, Bertilsson (bb0320) 2018; 39
de Bosch, Mosesson, Ruiz‐Saez, Echenagucia, Rodriguez‐Lemoin (bb0345) 2002; 88
Blinc, Planinsic, Keber, Jarh, Lahajnar, Zidansĕk (bb0185) 1991; 65
2010; 99
2017; 7
2011; 117
1995; 39
2018; 128
1984; 23
2004; 24
2017; 60–61
2008; 105
2008; 6
2013; 121
2013; 8
1990; 265
2009; 114
2009; 48
2014; 134
1998; 273
2018; 131
2018; 39
2018; 2
2013; 11
2005; 106
2002; 88
2016; 42
1998; 92
2001; 936
2007; 5
2007; 21
2014; 123
2003; 89
2014; 124
1995; 9
1995; 92
2017; 60
2012; 102
2017; 2017
2015; 126
1980; 65
2000; 20
2015; 10
2011; 31
1992; 79
2016; 127
2014; 111
2006; 313
1996; 15
2016; 14
2012; 108
2014; 112
1990; 1
2009; 35
2012; 1
2004; 113
1991; 65
2015; 113
2007; 110
1988; 156
2016; 139
2006; 107
2018; 16
1972; 247
2014; 31
2003; 23
2018; 57
Weisel (10.1002/rth2.12191_bb0125) 2007; 5
Veklich (10.1002/rth2.12191_bb0150) 1998; 92
Mosesson (10.1002/rth2.12191_bb0035) 1972; 247
Longstaff (10.1002/rth2.12191_bb0165) 2011; 117
Suh (10.1002/rth2.12191_bb0260) 1995; 9
Byrnes (10.1002/rth2.12191_bb0090) 2015; 126
Blinc (10.1002/rth2.12191_bb0185) 1991; 65
Cronje (10.1002/rth2.12191_bb0210) 2017; 60–61
O'Toole (10.1002/rth2.12191_bb0245) 1990; 1
Kunitada (10.1002/rth2.12191_bb0190) 1992; 79
Collet (10.1002/rth2.12191_bb0145) 2000; 20
Sakharov (10.1002/rth2.12191_bb0180) 1995; 92
Vo (10.1002/rth2.12191_bb0280) 2013; 8
Li (10.1002/rth2.12191_bb0050) 2017; 2017
Redman (10.1002/rth2.12191_bb0030) 2001; 936
Cho (10.1002/rth2.12191_bb0115) 2006; 107
Chung (10.1002/rth2.12191_bb0040) 1984; 23
Medved (10.1002/rth2.12191_bb0135) 2003; 89
Collet (10.1002/rth2.12191_bb0085) 2005; 106
Bucay (10.1002/rth2.12191_bb0170) 2015; 10
Prasad (10.1002/rth2.12191_bb0250) 2015; 126
Kollman (10.1002/rth2.12191_bb0015) 2009; 48
Fish (10.1002/rth2.12191_bb0285) 2014; 123
Espitia Jaimes (10.1002/rth2.12191_bb0020) 2018; 16
Sakata (10.1002/rth2.12191_bb0105) 1980; 65
O'Brien (10.1002/rth2.12191_bb0055) 2008; 105
Hudson (10.1002/rth2.12191_bb0155) 2017; 2017
Bannish (10.1002/rth2.12191_bb0140) 2017; 7
Uitte de Willige (10.1002/rth2.12191_bb0350) 2009; 114
Celinska‐Lowenhoff (10.1002/rth2.12191_bb0325) 2018; 57
Flick (10.1002/rth2.12191_bb0265) 2004; 113
Wolberg (10.1002/rth2.12191_bb0220) 2007; 21
Undas (10.1002/rth2.12191_bb0310) 2011; 31
Alshehri (10.1002/rth2.12191_bb0230) 2015; 126
Scott (10.1002/rth2.12191_bb0200) 2004; 24
Casini (10.1002/rth2.12191_bb0290) 2018; 16
Rijken (10.1002/rth2.12191_bb0095) 2016; 14
Standeven (10.1002/rth2.12191_bb0080) 2007; 110
de Bosch (10.1002/rth2.12191_bb0345) 2002; 88
Sumaya (10.1002/rth2.12191_bb0320) 2018; 39
Li (10.1002/rth2.12191_bb0195) 2017; 60
Allan (10.1002/rth2.12191_bb0070) 2012; 1
Ariens (10.1002/rth2.12191_bb0305) 2013; 11
Smith (10.1002/rth2.12191_bb0295) 2018; 2
Holmback (10.1002/rth2.12191_bb0255) 1996; 15
Weisel (10.1002/rth2.12191_bb0045) 2013; 121
Cieslik (10.1002/rth2.12191_bb0315) 2018; 131
Valnickova (10.1002/rth2.12191_bb0110) 1998; 273
Liu (10.1002/rth2.12191_bb0120) 2006; 313
Fish (10.1002/rth2.12191_bb0025) 2012; 108
Macrae (10.1002/rth2.12191_bb0060) 2018; 128
Standeven (10.1002/rth2.12191_bb0205) 2009; 35
Aleman (10.1002/rth2.12191_bb0270) 2014; 124
Folsom (10.1002/rth2.12191_bb0335) 2016; 139
Weisel (10.1002/rth2.12191_bb0160) 2008; 6
Altieri (10.1002/rth2.12191_bb0240) 1990; 265
Gulledge (10.1002/rth2.12191_bb0275) 2003; 23
Domingues (10.1002/rth2.12191_bb0065) 2016; 127
Duval (10.1002/rth2.12191_bb0075) 2014; 111
Bridge (10.1002/rth2.12191_bb0225) 2014; 112
Macrae (10.1002/rth2.12191_bb0340) 2016; 42
Houser (10.1002/rth2.12191_bb0130) 2010; 99
Solomon (10.1002/rth2.12191_bb0300) 2015; 113
Helms (10.1002/rth2.12191_bb0100) 2012; 102
Hoffman (10.1002/rth2.12191_bb0215) 2008; 6
Trezzini (10.1002/rth2.12191_bb0235) 1988; 156
Forrester (10.1002/rth2.12191_bb0010) 1995; 39
Kotze (10.1002/rth2.12191_bb0330) 2014; 134
Bannish (10.1002/rth2.12191_bb0175) 2014; 31
References_xml – volume: 124
  start-page: 3590
  year: 2014
  end-page: 600
  ident: bb0270
  article-title: Factor XIII activity mediates red blood cell retention in venous thrombi
  publication-title: J Clin Invest
– volume: 107
  start-page: 3555
  year: 2006
  end-page: 63
  ident: bb0115
  article-title: Enhancement of thrombogenesis by plasma fibronectin cross‐linked to fibrin and assembled in platelet thrombi
  publication-title: Blood
– volume: 113
  start-page: 1596
  year: 2004
  end-page: 606
  ident: bb0265
  article-title: Leukocyte engagement of fibrin(ogen) via the integrin receptor alphaMbeta2/Mac‐1 is critical for host inflammatory response in vivo
  publication-title: J Clin Invest
– volume: 14
  start-page: 1453
  year: 2016
  end-page: 61
  ident: bb0095
  article-title: Compaction of fibrin clots reveals the antifibrinolytic effect of factor XIII
  publication-title: J Thromb Haemost
– volume: 102
  start-page: 168
  year: 2012
  end-page: 75
  ident: bb0100
  article-title: alpha‐alpha Cross‐links increase fibrin fiber elasticity and stiffness
  publication-title: Biophys J
– volume: 2
  start-page: 800
  year: 2018
  end-page: 11
  ident: bb0295
  article-title: Identification and characterization of novel mutations implicated in congenital fibrinogen disorders
  publication-title: Res Pract Thromb Haemost
– volume: 42
  start-page: 344
  year: 2016
  end-page: 55
  ident: bb0340
  article-title: The (patho)physiology of gibrinogen gamma’
  publication-title: Semin Thromb Hemost
– volume: 106
  start-page: 3824
  year: 2005
  end-page: 30
  ident: bb0085
  article-title: The alphaC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis
  publication-title: Blood
– volume: 273
  start-page: 27220
  year: 1998
  end-page: 4
  ident: bb0110
  article-title: Human procarboxypeptidase U, or thrombin‐activable fibrinolysis inhibitor, is a substrate for transglutaminases. Evidence for transglutaminase‐catalyzed cross‐linking to fibrin
  publication-title: J Biol Chem
– volume: 1
  start-page: 1072
  year: 2012
  end-page: 80
  ident: bb0070
  article-title: Evidence that fibrinogen gamma’ directly interferes with protofibril growth: implications for fibrin structure and clot stiffness
  publication-title: J Thromb Haemost
– volume: 108
  start-page: 419
  year: 2012
  end-page: 26
  ident: bb0025
  article-title: Fibrinogen gene regulation
  publication-title: Thromb Haemost
– volume: 79
  start-page: 1420
  year: 1992
  end-page: 7
  ident: bb0190
  article-title: Inhibition of clot lysis and decreased binding of tissue‐type plasminogen activator as a consequence of clot retraction
  publication-title: Blood
– volume: 15
  start-page: 5760
  year: 1996
  end-page: 57671
  ident: bb0255
  article-title: Impaired platelet aggregation and sustained bleeding in mice lacking the fibrinogen motif bound by integrin alpha IIb beta 3
  publication-title: EMBO J
– volume: 16
  start-page: 1887
  year: 2018
  end-page: 90
  ident: bb0290
  article-title: Diagnosis and classification of congenital fibrinogen disorders: communication from the SSC of the ISTH
  publication-title: J Thromb Haemost
– volume: 936
  start-page: 480
  year: 2001
  end-page: 95
  ident: bb0030
  article-title: Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion
  publication-title: Ann N Y Acad Sci
– volume: 23
  start-page: 4232
  year: 1984
  end-page: 6
  ident: bb0040
  article-title: Gamma and gamma’ chains of human fibrinogen are produced by alternative mRNA processing
  publication-title: Biochemistry
– volume: 31
  start-page: 17
  year: 2014
  end-page: 44
  ident: bb0175
  article-title: Modelling fibrinolysis: a 3D stochastic multiscale model
  publication-title: Math Med Biol
– volume: 156
  start-page: 477
  year: 1988
  end-page: 84
  ident: bb0235
  article-title: Fibrinogen association with human monocytes: evidence for constitutive expression of fibrinogen receptors and for involvement of Mac‐1 (CD18, CR3) in the binding
  publication-title: Biochem Biophys Res Commun
– volume: 23
  start-page: 130
  year: 2003
  end-page: 5
  ident: bb0275
  article-title: Effects of hyperfibrinogenemia on vasculature of C57BL/6 mice with and without atherogenic diet
  publication-title: Arterioscler Thromb Vasc Biol
– volume: 313
  start-page: 634
  year: 2006
  ident: bb0120
  article-title: Fibrin fibers have extraordinary extensibility and elasticity
  publication-title: Science
– volume: 123
  start-page: 2278
  year: 2014
  end-page: 81
  ident: bb0285
  article-title: Targeted mutation of zebrafish fga models human congenital afibrinogenemia
  publication-title: Blood
– volume: 6
  start-page: 161
  year: 2008
  end-page: 80
  ident: bb0160
  article-title: The biochemical and physical process of fibrinolysis and effects of clot structure and stability on the lysis rate
  publication-title: Cardiovasc Hematol Agents Med Chem
– volume: 39
  start-page: 477
  year: 1995
  end-page: 92
  ident: bb0010
  article-title: Malpighi's De polypo cordis: an annotated translation
  publication-title: Med Hist
– volume: 113
  start-page: 759
  year: 2015
  end-page: 71
  ident: bb0300
  article-title: Safety of fibrinogen concentrate: analysis of more than 27 years of pharmacovigilance data
  publication-title: Thromb Haemost
– volume: 110
  start-page: 902
  year: 2007
  end-page: 7
  ident: bb0080
  article-title: Functional analysis of fibrin {gamma}‐chain cross‐linking by activated factor XIII: determination of a cross‐linking pattern that maximizes clot stiffness
  publication-title: Blood
– volume: 121
  start-page: 1712
  year: 2013
  end-page: 9
  ident: bb0045
  article-title: Mechanisms of fibrin polymerization and clinical implications
  publication-title: Blood
– volume: 126
  start-page: 1940
  year: 2015
  end-page: 8
  ident: bb0090
  article-title: Factor XIIIa‐dependent retention of red blood cells in clots is mediated by fibrin alpha‐chain crosslinking
  publication-title: Blood
– volume: 127
  start-page: 487
  year: 2016
  end-page: 95
  ident: bb0065
  article-title: Thrombin and fibrinogen gamma’ impact clot structure by marked effects on intrafibrillar structure and protofibril packing
  publication-title: Blood
– volume: 111
  start-page: 842
  year: 2014
  end-page: 50
  ident: bb0075
  article-title: Roles of fibrin alpha‐ and gamma‐chain specific cross‐linking by FXIIIa in fibrin structure and function
  publication-title: Thromb Haemost
– volume: 112
  start-page: 901
  year: 2014
  end-page: 8
  ident: bb0225
  article-title: Clot properties and cardiovascular disease
  publication-title: Thromb Haemost
– volume: 65
  start-page: 290
  year: 1980
  end-page: 7
  ident: bb0105
  article-title: Cross‐linking of alpha 2‐plasmin inhibitor to fibrin by fibrin‐stabilizing factor
  publication-title: J Clin Invest
– volume: 16
  start-page: 2070
  year: 2018
  end-page: 82
  ident: bb0020
  article-title: Local chromatin interactions contribute to expression of the fibrinogen gene cluster
  publication-title: J Thromb Haemost
– volume: 7
  start-page: 6914
  year: 2017
  ident: bb0140
  article-title: Molecular and physical mechanisms of fibrinolysis and thrombolysis from mathematical modeling and experiments
  publication-title: Sci Rep
– volume: 57
  start-page: 1340
  year: 2018
  end-page: 9
  ident: bb0325
  article-title: Reduced plasma fibrin clot permeability is associated with recurrent thromboembolic events in patients with antiphospholipid syndrome
  publication-title: Rheumatology (Oxford)
– volume: 128
  start-page: 3356
  year: 2018
  end-page: 68
  ident: bb0060
  article-title: A fibrin biofilm covers blood clots and protects from microbial invasion
  publication-title: J Clin Invest
– volume: 9
  start-page: 2020
  year: 1995
  end-page: 33
  ident: bb0260
  article-title: Resolution of spontaneous bleeding events but failure of pregnancy in fibrinogen‐deficient mice
  publication-title: Genes Dev
– volume: 134
  start-page: 963
  year: 2014
  end-page: 9
  ident: bb0330
  article-title: CVD risk factors are related to plasma fibrin clot properties independent of total and or gamma’ fibrinogen concentration
  publication-title: Thromb Res
– volume: 10
  start-page: e0116350
  year: 2015
  ident: bb0170
  article-title: Physical determinants of fibrinolysis in single fibrin fibers
  publication-title: PLoS ONE
– volume: 24
  start-page: 1558
  year: 2004
  end-page: 66
  ident: bb0200
  article-title: Genetic and environmental determinants of fibrin structure and function: relevance to clinical disease
  publication-title: Arterioscler Thromb Vasc Biol
– volume: 88
  start-page: 253
  year: 2002
  end-page: 8
  ident: bb0345
  article-title: Inhibition of thrombin generation in plasma by fibrin formation (Antithrombin I)
  publication-title: Thromb Haemost
– volume: 89
  start-page: 409
  year: 2003
  end-page: 4019
  ident: bb0135
  article-title: Molecular mechanisms of initiation of fibrinolysis by fibrin
  publication-title: Thromb Haemost
– volume: 99
  start-page: 3038
  year: 2010
  end-page: 47
  ident: bb0130
  article-title: Evidence that alphaC region is origin of low modulus, high extensibility, and strain stiffening in fibrin fibers
  publication-title: Biophys J
– volume: 2017
  start-page: 6385628
  year: 2017
  ident: bb0050
  article-title: Nonuniform internal structure of fibrin fibers: protein density and bond density strongly decrease with increasing diameter
  publication-title: Biomed Res Int
– volume: 5
  start-page: 116
  year: 2007
  end-page: 24
  ident: bb0125
  article-title: Structure of fibrin: impact on clot stability
  publication-title: J Thromb Haemost
– volume: 48
  start-page: 3877
  year: 2009
  end-page: 86
  ident: bb0015
  article-title: Crystal structure of human fibrinogen
  publication-title: Biochemistry
– volume: 247
  start-page: 5223
  year: 1972
  end-page: 7
  ident: bb0035
  article-title: Human fibrinogen heterogeneities. 3. Identification of chain variants
  publication-title: J Biol Chem
– volume: 265
  start-page: 12119
  year: 1990
  end-page: 22
  ident: bb0240
  article-title: A unique recognition site mediates the interaction of fibrinogen with the leukocyte integrin Mac‐1 (CD11b/CD18)
  publication-title: J Biol Chem
– volume: 39
  start-page: 1078
  year: 2018
  end-page: 85
  ident: bb0320
  article-title: Fibrin clot properties independently predict adverse clinical outcome following acute coronary syndrome: a PLATO substudy
  publication-title: Eur Heart J
– volume: 35
  start-page: 458
  year: 2009
  end-page: 67
  ident: bb0205
  article-title: Heritability of clot formation
  publication-title: Semin Thromb Hemost
– volume: 6
  start-page: 206
  year: 2008
  end-page: 11
  ident: bb0215
  article-title: Alterations of fibrinogen structure in human disease
  publication-title: Cardiovasc Hematol Agents Med Chem
– volume: 92
  start-page: 1883
  year: 1995
  end-page: 90
  ident: bb0180
  article-title: Superficial accumulation of plasminogen during plasma clot lysis
  publication-title: Circulation
– volume: 60
  start-page: 264
  year: 2017
  end-page: 74
  ident: bb0195
  article-title: Stretching single fibrin fibers hampers their lysis
  publication-title: Acta Biomater
– volume: 126
  start-page: 2047
  year: 2015
  end-page: 58
  ident: bb0250
  article-title: Mice expressing a mutant form of fibrinogen that cannot support fibrin formation exhibit compromised antimicrobial host defense
  publication-title: Blood
– volume: 2017
  start-page: 2748340
  year: 2017
  ident: bb0155
  article-title: Biophysical mechanisms mediating fibrin fiber lysis
  publication-title: Biomed Res Int
– volume: 65
  start-page: 549
  year: 1991
  end-page: 52
  ident: bb0185
  article-title: Dependence of blood clot lysis on the mode of transport of urokinase into the clot – a magnetic resonance imaging study in vitro
  publication-title: Thromb Haemost
– volume: 60–61
  start-page: 16
  year: 2017
  end-page: 26
  ident: bb0210
  article-title: Candidate gene analysis of the fibrinogen phenotype reveals the importance of polygenic co‐regulation
  publication-title: Matrix Biol
– volume: 117
  start-page: 661
  year: 2011
  end-page: 8
  ident: bb0165
  article-title: The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: kinetic and microscopic studies
  publication-title: Blood
– volume: 1
  start-page: 883
  year: 1990
  end-page: 93
  ident: bb0245
  article-title: Affinity modulation of the alpha IIb beta 3 integrin (platelet GPIIb‐IIIa) is an intrinsic property of the receptor
  publication-title: Cell Regul
– volume: 139
  start-page: 44
  year: 2016
  end-page: 9
  ident: bb0335
  article-title: Prospective study of gamma’ fibrinogen and incident venous thromboembolism: the Longitudinal Investigation of Thromboembolism Etiology (LITE)
  publication-title: Thromb Res
– volume: 92
  start-page: 4721
  year: 1998
  end-page: 9
  ident: bb0150
  article-title: Structural studies of fibrinolysis by electron microscopy
  publication-title: Blood
– volume: 114
  start-page: 3994
  year: 2009
  end-page: 4001
  ident: bb0350
  article-title: The pleiotropic role of the fibrinogen gamma’ chain in hemostasis
  publication-title: Blood
– volume: 20
  start-page: 1354
  year: 2000
  end-page: 61
  ident: bb0145
  article-title: Influence of fibrin network conformation and fibrin fiber diameter on fibrinolysis speed: dynamic and structural approaches by confocal microscopy
  publication-title: Arterioscler Thromb Vasc Biol
– volume: 131
  start-page: 797
  year: 2018
  end-page: 807
  ident: bb0315
  article-title: Altered plasma clot properties increase the risk of recurrent deep vein thrombosis: a cohort study
  publication-title: Blood
– volume: 105
  start-page: 19438
  year: 2008
  end-page: 43
  ident: bb0055
  article-title: Ultrathin self‐assembled fibrin sheets
  publication-title: Proc Natl Acad Sci USA
– volume: 8
  start-page: e74682
  year: 2013
  ident: bb0280
  article-title: Loss of fibrinogen in zebrafish results in symptoms consistent with human hypofibrinogenemia
  publication-title: PLoS ONE
– volume: 11
  start-page: 294
  year: 2013
  end-page: 305
  ident: bb0305
  article-title: Fibrin(ogen) and thrombotic disease
  publication-title: J Thromb Haemost
– volume: 21
  start-page: 131
  year: 2007
  end-page: 42
  ident: bb0220
  article-title: Thrombin generation and fibrin clot structure
  publication-title: Blood Rev
– volume: 126
  start-page: 1601
  year: 2015
  end-page: 8
  ident: bb0230
  article-title: Fibrin activates GPVI in human and mouse platelets
  publication-title: Blood
– volume: 31
  start-page: e88
  year: 2011
  end-page: 99
  ident: bb0310
  article-title: Fibrin clot structure and function: a role in the pathophysiology of arterial and venous thromboembolic diseases
  publication-title: Arterioscler Thromb Vasc Biol
– volume: 2017
  start-page: 6385628
  year: 2017
  article-title: Nonuniform internal structure of fibrin fibers: protein density and bond density strongly decrease with increasing diameter
  publication-title: Biomed Res Int
– volume: 111
  start-page: 842
  year: 2014
  end-page: 50
  article-title: Roles of fibrin alpha‐ and gamma‐chain specific cross‐linking by FXIIIa in fibrin structure and function
  publication-title: Thromb Haemost
– volume: 99
  start-page: 3038
  year: 2010
  end-page: 47
  article-title: Evidence that alphaC region is origin of low modulus, high extensibility, and strain stiffening in fibrin fibers
  publication-title: Biophys J
– volume: 112
  start-page: 901
  year: 2014
  end-page: 8
  article-title: Clot properties and cardiovascular disease
  publication-title: Thromb Haemost
– volume: 134
  start-page: 963
  year: 2014
  end-page: 9
  article-title: CVD risk factors are related to plasma fibrin clot properties independent of total and or gamma’ fibrinogen concentration
  publication-title: Thromb Res
– volume: 131
  start-page: 797
  year: 2018
  end-page: 807
  article-title: Altered plasma clot properties increase the risk of recurrent deep vein thrombosis: a cohort study
  publication-title: Blood
– volume: 113
  start-page: 759
  year: 2015
  end-page: 71
  article-title: Safety of fibrinogen concentrate: analysis of more than 27 years of pharmacovigilance data
  publication-title: Thromb Haemost
– volume: 57
  start-page: 1340
  year: 2018
  end-page: 9
  article-title: Reduced plasma fibrin clot permeability is associated with recurrent thromboembolic events in patients with antiphospholipid syndrome
  publication-title: Rheumatology (Oxford)
– volume: 89
  start-page: 409
  year: 2003
  end-page: 4019
  article-title: Molecular mechanisms of initiation of fibrinolysis by fibrin
  publication-title: Thromb Haemost
– volume: 113
  start-page: 1596
  year: 2004
  end-page: 606
  article-title: Leukocyte engagement of fibrin(ogen) via the integrin receptor alphaMbeta2/Mac‐1 is critical for host inflammatory response in vivo
  publication-title: J Clin Invest
– volume: 15
  start-page: 5760
  year: 1996
  end-page: 57671
  article-title: Impaired platelet aggregation and sustained bleeding in mice lacking the fibrinogen motif bound by integrin alpha IIb beta 3
  publication-title: EMBO J
– volume: 1
  start-page: 1072
  year: 2012
  end-page: 80
  article-title: Evidence that fibrinogen gamma’ directly interferes with protofibril growth: implications for fibrin structure and clot stiffness
  publication-title: J Thromb Haemost
– volume: 60
  start-page: 264
  year: 2017
  end-page: 74
  article-title: Stretching single fibrin fibers hampers their lysis
  publication-title: Acta Biomater
– volume: 124
  start-page: 3590
  year: 2014
  end-page: 600
  article-title: Factor XIII activity mediates red blood cell retention in venous thrombi
  publication-title: J Clin Invest
– volume: 2
  start-page: 800
  year: 2018
  end-page: 11
  article-title: Identification and characterization of novel mutations implicated in congenital fibrinogen disorders
  publication-title: Res Pract Thromb Haemost
– volume: 35
  start-page: 458
  year: 2009
  end-page: 67
  article-title: Heritability of clot formation
  publication-title: Semin Thromb Hemost
– volume: 108
  start-page: 419
  year: 2012
  end-page: 26
  article-title: Fibrinogen gene regulation
  publication-title: Thromb Haemost
– volume: 105
  start-page: 19438
  year: 2008
  end-page: 43
  article-title: Ultrathin self‐assembled fibrin sheets
  publication-title: Proc Natl Acad Sci USA
– volume: 6
  start-page: 206
  year: 2008
  end-page: 11
  article-title: Alterations of fibrinogen structure in human disease
  publication-title: Cardiovasc Hematol Agents Med Chem
– volume: 8
  start-page: e74682
  year: 2013
  article-title: Loss of fibrinogen in zebrafish results in symptoms consistent with human hypofibrinogenemia
  publication-title: PLoS ONE
– volume: 39
  start-page: 1078
  year: 2018
  end-page: 85
  article-title: Fibrin clot properties independently predict adverse clinical outcome following acute coronary syndrome: a PLATO substudy
  publication-title: Eur Heart J
– volume: 79
  start-page: 1420
  year: 1992
  end-page: 7
  article-title: Inhibition of clot lysis and decreased binding of tissue‐type plasminogen activator as a consequence of clot retraction
  publication-title: Blood
– volume: 126
  start-page: 1940
  year: 2015
  end-page: 8
  article-title: Factor XIIIa‐dependent retention of red blood cells in clots is mediated by fibrin alpha‐chain crosslinking
  publication-title: Blood
– volume: 313
  start-page: 634
  year: 2006
  article-title: Fibrin fibers have extraordinary extensibility and elasticity
  publication-title: Science
– volume: 23
  start-page: 4232
  year: 1984
  end-page: 6
  article-title: Gamma and gamma’ chains of human fibrinogen are produced by alternative mRNA processing
  publication-title: Biochemistry
– volume: 14
  start-page: 1453
  year: 2016
  end-page: 61
  article-title: Compaction of fibrin clots reveals the antifibrinolytic effect of factor XIII
  publication-title: J Thromb Haemost
– volume: 10
  start-page: e0116350
  year: 2015
  article-title: Physical determinants of fibrinolysis in single fibrin fibers
  publication-title: PLoS ONE
– volume: 139
  start-page: 44
  year: 2016
  end-page: 9
  article-title: Prospective study of gamma’ fibrinogen and incident venous thromboembolism: the Longitudinal Investigation of Thromboembolism Etiology (LITE)
  publication-title: Thromb Res
– volume: 247
  start-page: 5223
  year: 1972
  end-page: 7
  article-title: Human fibrinogen heterogeneities. 3. Identification of chain variants
  publication-title: J Biol Chem
– volume: 60–61
  start-page: 16
  year: 2017
  end-page: 26
  article-title: Candidate gene analysis of the fibrinogen phenotype reveals the importance of polygenic co‐regulation
  publication-title: Matrix Biol
– volume: 20
  start-page: 1354
  year: 2000
  end-page: 61
  article-title: Influence of fibrin network conformation and fibrin fiber diameter on fibrinolysis speed: dynamic and structural approaches by confocal microscopy
  publication-title: Arterioscler Thromb Vasc Biol
– volume: 88
  start-page: 253
  year: 2002
  end-page: 8
  article-title: Inhibition of thrombin generation in plasma by fibrin formation (Antithrombin I)
  publication-title: Thromb Haemost
– volume: 5
  start-page: 116
  issue: suppl 1
  year: 2007
  end-page: 24
  article-title: Structure of fibrin: impact on clot stability
  publication-title: J Thromb Haemost
– volume: 42
  start-page: 344
  year: 2016
  end-page: 55
  article-title: The (patho)physiology of gibrinogen gamma’
  publication-title: Semin Thromb Hemost
– volume: 128
  start-page: 3356
  year: 2018
  end-page: 68
  article-title: A fibrin biofilm covers blood clots and protects from microbial invasion
  publication-title: J Clin Invest
– volume: 107
  start-page: 3555
  year: 2006
  end-page: 63
  article-title: Enhancement of thrombogenesis by plasma fibronectin cross‐linked to fibrin and assembled in platelet thrombi
  publication-title: Blood
– volume: 102
  start-page: 168
  year: 2012
  end-page: 75
  article-title: alpha‐alpha Cross‐links increase fibrin fiber elasticity and stiffness
  publication-title: Biophys J
– volume: 127
  start-page: 487
  year: 2016
  end-page: 95
  article-title: Thrombin and fibrinogen gamma’ impact clot structure by marked effects on intrafibrillar structure and protofibril packing
  publication-title: Blood
– volume: 11
  start-page: 294
  issue: suppl 1
  year: 2013
  end-page: 305
  article-title: Fibrin(ogen) and thrombotic disease
  publication-title: J Thromb Haemost
– volume: 6
  start-page: 161
  year: 2008
  end-page: 80
  article-title: The biochemical and physical process of fibrinolysis and effects of clot structure and stability on the lysis rate
  publication-title: Cardiovasc Hematol Agents Med Chem
– volume: 16
  start-page: 1887
  year: 2018
  end-page: 90
  article-title: Diagnosis and classification of congenital fibrinogen disorders: communication from the SSC of the ISTH
  publication-title: J Thromb Haemost
– volume: 126
  start-page: 1601
  year: 2015
  end-page: 8
  article-title: Fibrin activates GPVI in human and mouse platelets
  publication-title: Blood
– volume: 123
  start-page: 2278
  year: 2014
  end-page: 81
  article-title: Targeted mutation of zebrafish fga models human congenital afibrinogenemia
  publication-title: Blood
– volume: 110
  start-page: 902
  year: 2007
  end-page: 7
  article-title: Functional analysis of fibrin {gamma}‐chain cross‐linking by activated factor XIII: determination of a cross‐linking pattern that maximizes clot stiffness
  publication-title: Blood
– volume: 31
  start-page: 17
  year: 2014
  end-page: 44
  article-title: Modelling fibrinolysis: a 3D stochastic multiscale model
  publication-title: Math Med Biol
– volume: 24
  start-page: 1558
  year: 2004
  end-page: 66
  article-title: Genetic and environmental determinants of fibrin structure and function: relevance to clinical disease
  publication-title: Arterioscler Thromb Vasc Biol
– volume: 16
  start-page: 2070
  year: 2018
  end-page: 82
  article-title: Local chromatin interactions contribute to expression of the fibrinogen gene cluster
  publication-title: J Thromb Haemost
– volume: 65
  start-page: 549
  year: 1991
  end-page: 52
  article-title: Dependence of blood clot lysis on the mode of transport of urokinase into the clot – a magnetic resonance imaging study in vitro
  publication-title: Thromb Haemost
– volume: 92
  start-page: 1883
  year: 1995
  end-page: 90
  article-title: Superficial accumulation of plasminogen during plasma clot lysis
  publication-title: Circulation
– volume: 2017
  start-page: 2748340
  year: 2017
  article-title: Biophysical mechanisms mediating fibrin fiber lysis
  publication-title: Biomed Res Int
– volume: 156
  start-page: 477
  year: 1988
  end-page: 84
  article-title: Fibrinogen association with human monocytes: evidence for constitutive expression of fibrinogen receptors and for involvement of Mac‐1 (CD18, CR3) in the binding
  publication-title: Biochem Biophys Res Commun
– volume: 9
  start-page: 2020
  year: 1995
  end-page: 33
  article-title: Resolution of spontaneous bleeding events but failure of pregnancy in fibrinogen‐deficient mice
  publication-title: Genes Dev
– volume: 126
  start-page: 2047
  year: 2015
  end-page: 58
  article-title: Mice expressing a mutant form of fibrinogen that cannot support fibrin formation exhibit compromised antimicrobial host defense
  publication-title: Blood
– volume: 265
  start-page: 12119
  year: 1990
  end-page: 22
  article-title: A unique recognition site mediates the interaction of fibrinogen with the leukocyte integrin Mac‐1 (CD11b/CD18)
  publication-title: J Biol Chem
– volume: 273
  start-page: 27220
  year: 1998
  end-page: 4
  article-title: Human procarboxypeptidase U, or thrombin‐activable fibrinolysis inhibitor, is a substrate for transglutaminases. Evidence for transglutaminase‐catalyzed cross‐linking to fibrin
  publication-title: J Biol Chem
– volume: 48
  start-page: 3877
  year: 2009
  end-page: 86
  article-title: Crystal structure of human fibrinogen
  publication-title: Biochemistry
– volume: 117
  start-page: 661
  year: 2011
  end-page: 8
  article-title: The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: kinetic and microscopic studies
  publication-title: Blood
– volume: 39
  start-page: 477
  year: 1995
  end-page: 92
  article-title: Malpighi's De polypo cordis: an annotated translation
  publication-title: Med Hist
– volume: 106
  start-page: 3824
  year: 2005
  end-page: 30
  article-title: The alphaC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis
  publication-title: Blood
– volume: 31
  start-page: e88
  year: 2011
  end-page: 99
  article-title: Fibrin clot structure and function: a role in the pathophysiology of arterial and venous thromboembolic diseases
  publication-title: Arterioscler Thromb Vasc Biol
– volume: 21
  start-page: 131
  year: 2007
  end-page: 42
  article-title: Thrombin generation and fibrin clot structure
  publication-title: Blood Rev
– volume: 7
  start-page: 6914
  year: 2017
  article-title: Molecular and physical mechanisms of fibrinolysis and thrombolysis from mathematical modeling and experiments
  publication-title: Sci Rep
– volume: 114
  start-page: 3994
  year: 2009
  end-page: 4001
  article-title: The pleiotropic role of the fibrinogen gamma’ chain in hemostasis
  publication-title: Blood
– volume: 92
  start-page: 4721
  year: 1998
  end-page: 9
  article-title: Structural studies of fibrinolysis by electron microscopy
  publication-title: Blood
– volume: 23
  start-page: 130
  year: 2003
  end-page: 5
  article-title: Effects of hyperfibrinogenemia on vasculature of C57BL/6 mice with and without atherogenic diet
  publication-title: Arterioscler Thromb Vasc Biol
– volume: 1
  start-page: 883
  year: 1990
  end-page: 93
  article-title: Affinity modulation of the alpha IIb beta 3 integrin (platelet GPIIb‐IIIa) is an intrinsic property of the receptor
  publication-title: Cell Regul
– volume: 65
  start-page: 290
  year: 1980
  end-page: 7
  article-title: Cross‐linking of alpha 2‐plasmin inhibitor to fibrin by fibrin‐stabilizing factor
  publication-title: J Clin Invest
– volume: 121
  start-page: 1712
  year: 2013
  end-page: 9
  article-title: Mechanisms of fibrin polymerization and clinical implications
  publication-title: Blood
– volume: 936
  start-page: 480
  year: 2001
  end-page: 95
  article-title: Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion
  publication-title: Ann N Y Acad Sci
– volume: 111
  start-page: 842
  year: 2014
  ident: 10.1002/rth2.12191_bb0075
  article-title: Roles of fibrin alpha‐ and gamma‐chain specific cross‐linking by FXIIIa in fibrin structure and function
  publication-title: Thromb Haemost
  doi: 10.1160/TH13-10-0855
– volume: 2017
  start-page: 6385628
  year: 2017
  ident: 10.1002/rth2.12191_bb0050
  article-title: Nonuniform internal structure of fibrin fibers: protein density and bond density strongly decrease with increasing diameter
  publication-title: Biomed Res Int
– volume: 7
  start-page: 6914
  year: 2017
  ident: 10.1002/rth2.12191_bb0140
  article-title: Molecular and physical mechanisms of fibrinolysis and thrombolysis from mathematical modeling and experiments
  publication-title: Sci Rep
  doi: 10.1038/s41598-017-06383-w
– volume: 1
  start-page: 883
  year: 1990
  ident: 10.1002/rth2.12191_bb0245
  article-title: Affinity modulation of the alpha IIb beta 3 integrin (platelet GPIIb‐IIIa) is an intrinsic property of the receptor
  publication-title: Cell Regul
  doi: 10.1091/mbc.1.12.883
– volume: 117
  start-page: 661
  year: 2011
  ident: 10.1002/rth2.12191_bb0165
  article-title: The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: kinetic and microscopic studies
  publication-title: Blood
  doi: 10.1182/blood-2010-06-290338
– volume: 156
  start-page: 477
  year: 1988
  ident: 10.1002/rth2.12191_bb0235
  article-title: Fibrinogen association with human monocytes: evidence for constitutive expression of fibrinogen receptors and for involvement of Mac‐1 (CD18, CR3) in the binding
  publication-title: Biochem Biophys Res Commun
  doi: 10.1016/S0006-291X(88)80866-0
– volume: 99
  start-page: 3038
  year: 2010
  ident: 10.1002/rth2.12191_bb0130
  article-title: Evidence that alphaC region is origin of low modulus, high extensibility, and strain stiffening in fibrin fibers
  publication-title: Biophys J
  doi: 10.1016/j.bpj.2010.08.060
– volume: 65
  start-page: 549
  year: 1991
  ident: 10.1002/rth2.12191_bb0185
  article-title: Dependence of blood clot lysis on the mode of transport of urokinase into the clot – a magnetic resonance imaging study in vitro
  publication-title: Thromb Haemost
  doi: 10.1055/s-0038-1648188
– volume: 60–61
  start-page: 16
  year: 2017
  ident: 10.1002/rth2.12191_bb0210
  article-title: Candidate gene analysis of the fibrinogen phenotype reveals the importance of polygenic co‐regulation
  publication-title: Matrix Biol
  doi: 10.1016/j.matbio.2016.10.005
– volume: 6
  start-page: 161
  year: 2008
  ident: 10.1002/rth2.12191_bb0160
  article-title: The biochemical and physical process of fibrinolysis and effects of clot structure and stability on the lysis rate
  publication-title: Cardiovasc Hematol Agents Med Chem
  doi: 10.2174/187152508784871963
– volume: 65
  start-page: 290
  year: 1980
  ident: 10.1002/rth2.12191_bb0105
  article-title: Cross‐linking of alpha 2‐plasmin inhibitor to fibrin by fibrin‐stabilizing factor
  publication-title: J Clin Invest
  doi: 10.1172/JCI109671
– volume: 35
  start-page: 458
  year: 2009
  ident: 10.1002/rth2.12191_bb0205
  article-title: Heritability of clot formation
  publication-title: Semin Thromb Hemost
  doi: 10.1055/s-0029-1234141
– volume: 102
  start-page: 168
  year: 2012
  ident: 10.1002/rth2.12191_bb0100
  article-title: alpha‐alpha Cross‐links increase fibrin fiber elasticity and stiffness
  publication-title: Biophys J
  doi: 10.1016/j.bpj.2011.11.4016
– volume: 5
  start-page: 116
  issue: suppl 1
  year: 2007
  ident: 10.1002/rth2.12191_bb0125
  article-title: Structure of fibrin: impact on clot stability
  publication-title: J Thromb Haemost
  doi: 10.1111/j.1538-7836.2007.02504.x
– volume: 31
  start-page: e88
  year: 2011
  ident: 10.1002/rth2.12191_bb0310
  article-title: Fibrin clot structure and function: a role in the pathophysiology of arterial and venous thromboembolic diseases
  publication-title: Arterioscler Thromb Vasc Biol
  doi: 10.1161/ATVBAHA.111.230631
– volume: 2017
  start-page: 2748340
  year: 2017
  ident: 10.1002/rth2.12191_bb0155
  article-title: Biophysical mechanisms mediating fibrin fiber lysis
  publication-title: Biomed Res Int
  doi: 10.1155/2017/2748340
– volume: 124
  start-page: 3590
  year: 2014
  ident: 10.1002/rth2.12191_bb0270
  article-title: Factor XIII activity mediates red blood cell retention in venous thrombi
  publication-title: J Clin Invest
  doi: 10.1172/JCI75386
– volume: 8
  start-page: e74682
  year: 2013
  ident: 10.1002/rth2.12191_bb0280
  article-title: Loss of fibrinogen in zebrafish results in symptoms consistent with human hypofibrinogenemia
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0074682
– volume: 113
  start-page: 759
  year: 2015
  ident: 10.1002/rth2.12191_bb0300
  article-title: Safety of fibrinogen concentrate: analysis of more than 27 years of pharmacovigilance data
  publication-title: Thromb Haemost
  doi: 10.1160/TH14-06-0514
– volume: 128
  start-page: 3356
  year: 2018
  ident: 10.1002/rth2.12191_bb0060
  article-title: A fibrin biofilm covers blood clots and protects from microbial invasion
  publication-title: J Clin Invest
  doi: 10.1172/JCI98734
– volume: 121
  start-page: 1712
  year: 2013
  ident: 10.1002/rth2.12191_bb0045
  article-title: Mechanisms of fibrin polymerization and clinical implications
  publication-title: Blood
  doi: 10.1182/blood-2012-09-306639
– volume: 79
  start-page: 1420
  year: 1992
  ident: 10.1002/rth2.12191_bb0190
  article-title: Inhibition of clot lysis and decreased binding of tissue‐type plasminogen activator as a consequence of clot retraction
  publication-title: Blood
  doi: 10.1182/blood.V79.6.1420.1420
– volume: 113
  start-page: 1596
  year: 2004
  ident: 10.1002/rth2.12191_bb0265
  article-title: Leukocyte engagement of fibrin(ogen) via the integrin receptor alphaMbeta2/Mac‐1 is critical for host inflammatory response in vivo
  publication-title: J Clin Invest
  doi: 10.1172/JCI20741
– volume: 2
  start-page: 800
  year: 2018
  ident: 10.1002/rth2.12191_bb0295
  article-title: Identification and characterization of novel mutations implicated in congenital fibrinogen disorders
  publication-title: Res Pract Thromb Haemost
  doi: 10.1002/rth2.12127
– volume: 42
  start-page: 344
  year: 2016
  ident: 10.1002/rth2.12191_bb0340
  article-title: The (patho)physiology of gibrinogen gamma’
  publication-title: Semin Thromb Hemost
  doi: 10.1055/s-0036-1572353
– volume: 16
  start-page: 2070
  year: 2018
  ident: 10.1002/rth2.12191_bb0020
  article-title: Local chromatin interactions contribute to expression of the fibrinogen gene cluster
  publication-title: J Thromb Haemost
  doi: 10.1111/jth.14248
– volume: 123
  start-page: 2278
  year: 2014
  ident: 10.1002/rth2.12191_bb0285
  article-title: Targeted mutation of zebrafish fga models human congenital afibrinogenemia
  publication-title: Blood
  doi: 10.1182/blood-2013-12-547182
– volume: 16
  start-page: 1887
  year: 2018
  ident: 10.1002/rth2.12191_bb0290
  article-title: Diagnosis and classification of congenital fibrinogen disorders: communication from the SSC of the ISTH
  publication-title: J Thromb Haemost
  doi: 10.1111/jth.14216
– volume: 9
  start-page: 2020
  year: 1995
  ident: 10.1002/rth2.12191_bb0260
  article-title: Resolution of spontaneous bleeding events but failure of pregnancy in fibrinogen‐deficient mice
  publication-title: Genes Dev
  doi: 10.1101/gad.9.16.2020
– volume: 57
  start-page: 1340
  year: 2018
  ident: 10.1002/rth2.12191_bb0325
  article-title: Reduced plasma fibrin clot permeability is associated with recurrent thromboembolic events in patients with antiphospholipid syndrome
  publication-title: Rheumatology (Oxford)
  doi: 10.1093/rheumatology/key089
– volume: 126
  start-page: 2047
  year: 2015
  ident: 10.1002/rth2.12191_bb0250
  article-title: Mice expressing a mutant form of fibrinogen that cannot support fibrin formation exhibit compromised antimicrobial host defense
  publication-title: Blood
  doi: 10.1182/blood-2015-04-639849
– volume: 131
  start-page: 797
  year: 2018
  ident: 10.1002/rth2.12191_bb0315
  article-title: Altered plasma clot properties increase the risk of recurrent deep vein thrombosis: a cohort study
  publication-title: Blood
  doi: 10.1182/blood-2017-07-798306
– volume: 127
  start-page: 487
  year: 2016
  ident: 10.1002/rth2.12191_bb0065
  article-title: Thrombin and fibrinogen gamma’ impact clot structure by marked effects on intrafibrillar structure and protofibril packing
  publication-title: Blood
  doi: 10.1182/blood-2015-06-652214
– volume: 31
  start-page: 17
  year: 2014
  ident: 10.1002/rth2.12191_bb0175
  article-title: Modelling fibrinolysis: a 3D stochastic multiscale model
  publication-title: Math Med Biol
  doi: 10.1093/imammb/dqs029
– volume: 107
  start-page: 3555
  year: 2006
  ident: 10.1002/rth2.12191_bb0115
  article-title: Enhancement of thrombogenesis by plasma fibronectin cross‐linked to fibrin and assembled in platelet thrombi
  publication-title: Blood
  doi: 10.1182/blood-2005-10-4168
– volume: 265
  start-page: 12119
  year: 1990
  ident: 10.1002/rth2.12191_bb0240
  article-title: A unique recognition site mediates the interaction of fibrinogen with the leukocyte integrin Mac‐1 (CD11b/CD18)
  publication-title: J Biol Chem
  doi: 10.1016/S0021-9258(19)38316-4
– volume: 1
  start-page: 1072
  year: 2012
  ident: 10.1002/rth2.12191_bb0070
  article-title: Evidence that fibrinogen gamma’ directly interferes with protofibril growth: implications for fibrin structure and clot stiffness
  publication-title: J Thromb Haemost
  doi: 10.1111/j.1538-7836.2012.04717.x
– volume: 23
  start-page: 130
  year: 2003
  ident: 10.1002/rth2.12191_bb0275
  article-title: Effects of hyperfibrinogenemia on vasculature of C57BL/6 mice with and without atherogenic diet
  publication-title: Arterioscler Thromb Vasc Biol
  doi: 10.1161/01.ATV.0000041037.06509.C2
– volume: 88
  start-page: 253
  year: 2002
  ident: 10.1002/rth2.12191_bb0345
  article-title: Inhibition of thrombin generation in plasma by fibrin formation (Antithrombin I)
  publication-title: Thromb Haemost
  doi: 10.1055/s-0037-1613195
– volume: 247
  start-page: 5223
  year: 1972
  ident: 10.1002/rth2.12191_bb0035
  article-title: Human fibrinogen heterogeneities. 3. Identification of chain variants
  publication-title: J Biol Chem
  doi: 10.1016/S0021-9258(19)44960-0
– volume: 114
  start-page: 3994
  year: 2009
  ident: 10.1002/rth2.12191_bb0350
  article-title: The pleiotropic role of the fibrinogen gamma’ chain in hemostasis
  publication-title: Blood
  doi: 10.1182/blood-2009-05-217968
– volume: 39
  start-page: 1078
  year: 2018
  ident: 10.1002/rth2.12191_bb0320
  article-title: Fibrin clot properties independently predict adverse clinical outcome following acute coronary syndrome: a PLATO substudy
  publication-title: Eur Heart J
  doi: 10.1093/eurheartj/ehy013
– volume: 39
  start-page: 477
  year: 1995
  ident: 10.1002/rth2.12191_bb0010
  article-title: Malpighi's De polypo cordis: an annotated translation
  publication-title: Med Hist
  doi: 10.1017/S0025727300060385
– volume: 23
  start-page: 4232
  year: 1984
  ident: 10.1002/rth2.12191_bb0040
  article-title: Gamma and gamma’ chains of human fibrinogen are produced by alternative mRNA processing
  publication-title: Biochemistry
  doi: 10.1021/bi00313a033
– volume: 126
  start-page: 1601
  year: 2015
  ident: 10.1002/rth2.12191_bb0230
  article-title: Fibrin activates GPVI in human and mouse platelets
  publication-title: Blood
  doi: 10.1182/blood-2015-04-641654
– volume: 126
  start-page: 1940
  year: 2015
  ident: 10.1002/rth2.12191_bb0090
  article-title: Factor XIIIa‐dependent retention of red blood cells in clots is mediated by fibrin alpha‐chain crosslinking
  publication-title: Blood
  doi: 10.1182/blood-2015-06-652263
– volume: 92
  start-page: 4721
  year: 1998
  ident: 10.1002/rth2.12191_bb0150
  article-title: Structural studies of fibrinolysis by electron microscopy
  publication-title: Blood
  doi: 10.1182/blood.V92.12.4721
– volume: 24
  start-page: 1558
  year: 2004
  ident: 10.1002/rth2.12191_bb0200
  article-title: Genetic and environmental determinants of fibrin structure and function: relevance to clinical disease
  publication-title: Arterioscler Thromb Vasc Biol
  doi: 10.1161/01.ATV.0000136649.83297.bf
– volume: 134
  start-page: 963
  year: 2014
  ident: 10.1002/rth2.12191_bb0330
  article-title: CVD risk factors are related to plasma fibrin clot properties independent of total and or gamma’ fibrinogen concentration
  publication-title: Thromb Res
  doi: 10.1016/j.thromres.2014.08.018
– volume: 108
  start-page: 419
  year: 2012
  ident: 10.1002/rth2.12191_bb0025
  article-title: Fibrinogen gene regulation
  publication-title: Thromb Haemost
  doi: 10.1160/TH12-04-0273
– volume: 89
  start-page: 409
  year: 2003
  ident: 10.1002/rth2.12191_bb0135
  article-title: Molecular mechanisms of initiation of fibrinolysis by fibrin
  publication-title: Thromb Haemost
  doi: 10.1055/s-0037-1613368
– volume: 11
  start-page: 294
  issue: suppl 1
  year: 2013
  ident: 10.1002/rth2.12191_bb0305
  article-title: Fibrin(ogen) and thrombotic disease
  publication-title: J Thromb Haemost
  doi: 10.1111/jth.12229
– volume: 92
  start-page: 1883
  year: 1995
  ident: 10.1002/rth2.12191_bb0180
  article-title: Superficial accumulation of plasminogen during plasma clot lysis
  publication-title: Circulation
  doi: 10.1161/01.CIR.92.7.1883
– volume: 48
  start-page: 3877
  year: 2009
  ident: 10.1002/rth2.12191_bb0015
  article-title: Crystal structure of human fibrinogen
  publication-title: Biochemistry
  doi: 10.1021/bi802205g
– volume: 110
  start-page: 902
  year: 2007
  ident: 10.1002/rth2.12191_bb0080
  article-title: Functional analysis of fibrin {gamma}‐chain cross‐linking by activated factor XIII: determination of a cross‐linking pattern that maximizes clot stiffness
  publication-title: Blood
  doi: 10.1182/blood-2007-01-066837
– volume: 14
  start-page: 1453
  year: 2016
  ident: 10.1002/rth2.12191_bb0095
  article-title: Compaction of fibrin clots reveals the antifibrinolytic effect of factor XIII
  publication-title: J Thromb Haemost
  doi: 10.1111/jth.13354
– volume: 10
  start-page: e0116350
  year: 2015
  ident: 10.1002/rth2.12191_bb0170
  article-title: Physical determinants of fibrinolysis in single fibrin fibers
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0116350
– volume: 6
  start-page: 206
  year: 2008
  ident: 10.1002/rth2.12191_bb0215
  article-title: Alterations of fibrinogen structure in human disease
  publication-title: Cardiovasc Hematol Agents Med Chem
  doi: 10.2174/187152508784871981
– volume: 112
  start-page: 901
  year: 2014
  ident: 10.1002/rth2.12191_bb0225
  article-title: Clot properties and cardiovascular disease
  publication-title: Thromb Haemost
  doi: 10.1160/th14-02-0184
– volume: 936
  start-page: 480
  year: 2001
  ident: 10.1002/rth2.12191_bb0030
  article-title: Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion
  publication-title: Ann N Y Acad Sci
  doi: 10.1111/j.1749-6632.2001.tb03535.x
– volume: 313
  start-page: 634
  year: 2006
  ident: 10.1002/rth2.12191_bb0120
  article-title: Fibrin fibers have extraordinary extensibility and elasticity
  publication-title: Science
  doi: 10.1126/science.1127317
– volume: 60
  start-page: 264
  year: 2017
  ident: 10.1002/rth2.12191_bb0195
  article-title: Stretching single fibrin fibers hampers their lysis
  publication-title: Acta Biomater
  doi: 10.1016/j.actbio.2017.07.037
– volume: 105
  start-page: 19438
  year: 2008
  ident: 10.1002/rth2.12191_bb0055
  article-title: Ultrathin self‐assembled fibrin sheets
  publication-title: Proc Natl Acad Sci USA
  doi: 10.1073/pnas.0804865105
– volume: 273
  start-page: 27220
  year: 1998
  ident: 10.1002/rth2.12191_bb0110
  article-title: Human procarboxypeptidase U, or thrombin‐activable fibrinolysis inhibitor, is a substrate for transglutaminases. Evidence for transglutaminase‐catalyzed cross‐linking to fibrin
  publication-title: J Biol Chem
  doi: 10.1074/jbc.273.42.27220
– volume: 139
  start-page: 44
  year: 2016
  ident: 10.1002/rth2.12191_bb0335
  article-title: Prospective study of gamma’ fibrinogen and incident venous thromboembolism: the Longitudinal Investigation of Thromboembolism Etiology (LITE)
  publication-title: Thromb Res
  doi: 10.1016/j.thromres.2016.01.008
– volume: 20
  start-page: 1354
  year: 2000
  ident: 10.1002/rth2.12191_bb0145
  article-title: Influence of fibrin network conformation and fibrin fiber diameter on fibrinolysis speed: dynamic and structural approaches by confocal microscopy
  publication-title: Arterioscler Thromb Vasc Biol
  doi: 10.1161/01.ATV.20.5.1354
– volume: 106
  start-page: 3824
  year: 2005
  ident: 10.1002/rth2.12191_bb0085
  article-title: The alphaC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis
  publication-title: Blood
  doi: 10.1182/blood-2005-05-2150
– volume: 21
  start-page: 131
  year: 2007
  ident: 10.1002/rth2.12191_bb0220
  article-title: Thrombin generation and fibrin clot structure
  publication-title: Blood Rev
  doi: 10.1016/j.blre.2006.11.001
– volume: 15
  start-page: 5760
  year: 1996
  ident: 10.1002/rth2.12191_bb0255
  article-title: Impaired platelet aggregation and sustained bleeding in mice lacking the fibrinogen motif bound by integrin alpha IIb beta 3
  publication-title: EMBO J
  doi: 10.1002/j.1460-2075.1996.tb00962.x
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Snippet Since its discovery over 350 years ago, studies of fibrinogen have revealed remarkable characteristics. Its complex structure as a large (340 kDa) hexameric...
Since its discovery over 350 years ago, studies of fibrinogen have revealed remarkable characteristics. Its complex structure as a large (340 kDa) hexameric...
Since its discovery over 350 years ago, studies of fibrinogen have revealed remarkable characteristics. Its complex structure as a large (340  kD a) hexameric...
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StartPage 161
SubjectTerms factor XIII
fibrin
fibrinogen
fibrinolysis
Gene expression
hemostasis
Illustrated Review
infection
thrombosis
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Title Fibrinogen and fibrin: An illustrated review
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