Antibody Engineering for the Development of Therapeutic Antibodies

Therapeutic antibodies represent one of the fastest growing areas of the pharmaceutical industry. There are currently 19 monoclonal antibodies in the market that have been approved by the FDA and over 150 in clinical developments. Driven by innovation and technological developments, therapeutic anti...

Full description

Saved in:
Bibliographic Details
Published inMolecules and cells Vol. 20; no. 1; pp. 17 - 29
Main Authors Kim, S.J. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea), Park, Y.W. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea), Hong, H.J. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea), E-mail: hjhong@kribb.re.kr
Format Journal Article
LanguageEnglish
Published United States 31.08.2005
Subjects
Affinity Maturation
Animals
Antibodies - chemistry
Antibodies - physiology
Antibodies, Monoclonal - chemistry
Antibody Affinity
Antibody Engineering
Antibody Fragments
Effector Functions
Human Monoclonal Antibodies
Humanized Antibodies
Humans
MEDICINAL PROPERTIES
Mice
Models, Molecular
Pharmacokinetics
PROPIEDADES MEDICINALES
PROPRIETE PHARMACOLOGIQUE
Protein Engineering - methods
Recombinant Fusion Proteins - chemistry
Technology, Pharmaceutical
Therapeutic Antibodies
Online AccessGet full text
ISSN1016-8478
0219-1032
DOI10.1016/s1016-8478(23)25245-0

Cover

Abstract Therapeutic antibodies represent one of the fastest growing areas of the pharmaceutical industry. There are currently 19 monoclonal antibodies in the market that have been approved by the FDA and over 150 in clinical developments. Driven by innovation and technological developments, therapeutic antibodies are the second largest biopharmaceutical product category after vaccines. Antibodies have been engineered by a variety of methods to suit a particular therapeutic use. This review describes the structural and functional characteristics of antibody and the antibody engineering for the generation and optimization of therapeutic antibodies.
AbstractList Therapeutic antibodies represent one of the fastest growing areas of the pharmaceutical industry. There are currently 19 monoclonal antibodies in the market that have been approved by the FDA and over 150 in clinical developments. Driven by innovation and technological developments, therapeutic antibodies are the second largest biopharmaceutical product category after vaccines. Antibodies have been engineered by a variety of methods to suit a particular therapeutic use. This review describes the structural and functional characteristics of antibody and the antibody engineering for the generation and optimization of therapeutic antibodies.
Therapeutic antibodies represent one of the fastest growing areas of the pharmaceutical industry. There are currently 19 monoclonal antibodies in the market that have been approved by the FDA and over 150 in clinical developments. Driven by innovation and technological developments, therapeutic antibodies are the second largest biopharmaceutical product category after vaccines. Antibodies have been engineered by a variety of methods to suit a particular therapeutic use. This review describes the structural and functional characteristics of antibody and the antibody engineering for the generation and optimization of therapeutic antibodies.Therapeutic antibodies represent one of the fastest growing areas of the pharmaceutical industry. There are currently 19 monoclonal antibodies in the market that have been approved by the FDA and over 150 in clinical developments. Driven by innovation and technological developments, therapeutic antibodies are the second largest biopharmaceutical product category after vaccines. Antibodies have been engineered by a variety of methods to suit a particular therapeutic use. This review describes the structural and functional characteristics of antibody and the antibody engineering for the generation and optimization of therapeutic antibodies.
Author Park, Y.W. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea)
Kim, S.J. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea)
Hong, H.J. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea), E-mail: hjhong@kribb.re.kr
Author_xml – sequence: 1
  fullname: Kim, S.J. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea)
– sequence: 2
  fullname: Park, Y.W. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea)
– sequence: 3
  fullname: Hong, H.J. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea), E-mail: hjhong@kribb.re.kr
BackLink https://www.ncbi.nlm.nih.gov/pubmed/16258237$$D View this record in MEDLINE/PubMed
BookMark eNqFkEtLxDAUhbNQnHH0JyhdiS6qSdq0Ka50fKIg6LgOaeZmjHSSmqTK_HvnhYIibu6Fy_ku55xttGGdBYT2CD4mmBQnYTFTnpf8kGZHlNGcpXgD9b_OPbQdwivGpCwo30I9UlDGaVb20fmZjaZ241lyaSfGAnhjJ4l2PokvkFzAOzSunYKNidPJ6AW8bKGLRiVrzkDYQZtaNgF213uAnq8uR8Ob9P7h-nZ4dp-qPKcxVYpxRsZUUpi7KEnFCl3XRCtZAqsUL3Fd0IxzTlgOmFVSg4a6rqCqgWkuswEqVn8728rZh2wa0XozlX4mCBaLrGJZhFgkFjQTyyIEnoMHK7D17q2DEMXUBAVNIy24LoiCl3mFCZsL99fCrp7C-Pv9uq65gK0EyrsQPOhfDp7-cHD6g1MmymicjV6a5l96b0Vr6YSceBPE3SPFuMAky6o8-wTLVZbX
CitedBy_id crossref_primary_10_1016_j_xphs_2023_03_026
crossref_primary_10_1021_bp070469z
crossref_primary_10_2174_0115680266281358240206112605
crossref_primary_10_1517_14712598_2011_594436
crossref_primary_10_4161_mabs_1_1_7377
crossref_primary_10_3389_fimmu_2023_1089395
crossref_primary_10_1002_cncr_22402
crossref_primary_10_1002_asia_200900129
crossref_primary_10_1016_j_wpi_2008_05_006
crossref_primary_10_3109_03008207_2013_778839
crossref_primary_10_1002_prot_25291
crossref_primary_10_1007_s40259_012_0007_0
crossref_primary_10_1016_j_biomaterials_2010_12_026
crossref_primary_10_4155_pbp_13_3
crossref_primary_10_1016_j_ab_2010_07_005
crossref_primary_10_1080_21645515_2015_1074362
crossref_primary_10_1517_14712598_8_5_609
crossref_primary_10_4161_mabs_3_4_15786
crossref_primary_10_1089_hyb_2009_0028
crossref_primary_10_1271_bbb_80640
crossref_primary_10_1042_BSR20150089
crossref_primary_10_4155_pbp_15_7
crossref_primary_10_1007_s12033_010_9298_x
crossref_primary_10_1007_s10059_009_0028_9
crossref_primary_10_1517_17425247_2015_999039
crossref_primary_10_3389_fddsv_2022_908870
crossref_primary_10_1007_s00432_016_2122_7
crossref_primary_10_1002_ijc_25038
crossref_primary_10_1016_j_canlet_2013_09_029
crossref_primary_10_1593_tlo_13409
crossref_primary_10_1016_j_molimm_2014_10_009
crossref_primary_10_1089_mab_2013_0059
crossref_primary_10_1373_clinchem_2016_266973
crossref_primary_10_3390_vaccines12121306
crossref_primary_10_1002_adhm_201601279
crossref_primary_10_3390_antib3020215
crossref_primary_10_1002_hep_22366
crossref_primary_10_1097_CAD_0000000000000452
crossref_primary_10_1007_s10529_006_9237_x
crossref_primary_10_1016_j_jim_2007_02_011
crossref_primary_10_3390_antib8010003
crossref_primary_10_1016_j_peptides_2009_12_009
crossref_primary_10_1016_j_molimm_2008_06_027
crossref_primary_10_3390_antib7010010
crossref_primary_10_1021_bc700349k
crossref_primary_10_1089_hyb_2008_0080
crossref_primary_10_1007_s00259_007_0560_9
crossref_primary_10_1080_19420862_2015_1068492
crossref_primary_10_1517_14712598_8_6_719
crossref_primary_10_15171_ijb_1472
crossref_primary_10_1007_s41745_018_0061_9
crossref_primary_10_1074_jbc_M607161200
crossref_primary_10_1007_s13346_011_0055_x
crossref_primary_10_1016_j_ijpharm_2024_124685
crossref_primary_10_4161_mabs_22593
crossref_primary_10_1111_j_1399_0012_2008_00816_x
crossref_primary_10_1128_AAC_02768_13
crossref_primary_10_1007_s10989_017_9670_9
crossref_primary_10_1186_s12014_018_9184_2
crossref_primary_10_1002_jcp_29346
crossref_primary_10_1016_j_jim_2013_01_011
crossref_primary_10_1161_CIRCULATIONAHA_113_002033
crossref_primary_10_1002_cjoc_200990021
crossref_primary_10_1016_j_chroma_2009_04_035
crossref_primary_10_1517_13543776_17_9_1047
crossref_primary_10_1155_2020_4638192
crossref_primary_10_1021_acs_chemrev_2c00915
crossref_primary_10_1080_19420862_2023_2185924
crossref_primary_10_1517_14712598_7_5_691
crossref_primary_10_1016_j_bbrc_2024_150945
crossref_primary_10_1158_0008_5472_CAN_07_0107
crossref_primary_10_4155_tde_10_98
Cites_doi 10.4049/jimmunol.164.8.4178
10.1038/ng0297-146
10.1038/321522a0
10.1073/pnas.81.21.6851
10.1093/nar/25.24.5132
10.1046/j.1365-2036.2000.00777.x
10.1038/nbt0796-845
10.4049/jimmunol.169.2.1110
10.1038/341544a0
10.1074/jbc.M202069200
10.1073/pnas.91.9.3809
10.1073/pnas.90.14.6444
10.1073/pnas.140210597
10.1016/S0952-7915(99)80031-4
10.1073/pnas.89.10.4457
10.1158/1078-0432.CCR-03-0799
10.1038/nbt800
10.1093/glycob/cwh001
10.1074/jbc.M409783200
10.4049/jimmunol.166.4.2571
10.1097/00002371-200105000-00011
10.1084/jem.178.2.661
10.4049/jimmunol.160.7.3393
10.1016/j.it.2004.01.008
10.1038/7023
10.1006/jmbi.1999.3141
10.1084/jem.173.4.1025
10.1073/pnas.90.22.10444
10.1016/j.ymeth.2005.01.007
10.1089/scd.1.1995.4.471
10.1073/pnas.95.24.14130
10.1006/jmbi.1996.0598
10.1146/annurev.immunol.15.1.203
10.1006/jmbi.1998.1948
10.1016/j.ymeth.2005.01.005
10.1038/nbt1291-1369
10.1016/j.ymeth.2005.01.003
10.1182/blood.V95.12.3900.012k14_3900_3908
10.1038/nbt0602-597
10.1038/82407
10.4049/jimmunol.149.12.3903
10.1016/0022-2836(91)90498-U
10.1128/jb.178.5.1341-1346.1996
10.1073/pnas.94.23.12297
10.1038/nbt0396-309
10.1016/S1380-2933(98)00007-4
10.1016/S0958-1669(97)80068-7
10.1006/jmbi.1999.3444
10.1073/pnas.90.16.7538
10.4049/jimmunol.157.11.4963
10.1038/nbt0697-553
10.1074/jbc.M210665200
10.1016/S0958-1669(98)80092-X
10.1016/j.ymeth.2005.01.004
10.1038/nbt0197-29
10.1073/pnas.91.19.9022
10.1200/JCO.1995.13.9.2281
10.1016/S0169-409X(02)00026-1
10.1073/pnas.95.11.6037
10.1002/j.1460-2075.1994.tb06626.x
10.1126/science.3140379
10.1038/nbt1094-999
10.1016/j.ymeth.2005.01.001
10.1016/0304-4157(92)90038-C
10.1016/0022-2836(92)90639-2
10.1006/jmbi.1995.0626
10.1038/9872
10.1111/j.1600-065X.1998.tb01434.x
10.1002/jlb.66.3.401
10.1002/eji.1830260319
10.1016/S0161-5890(97)00112-0
10.1074/jbc.C300470200
10.1073/pnas.78.1.524
10.1016/j.jmb.2003.09.055
10.1002/j.1460-2075.1994.tb06308.x
10.1002/1097-0215(20001215)88:6<962::AID-IJC20>3.0.CO;2-U
10.1006/jmbi.1995.0204
10.1038/11717
10.4049/jimmunol.169.9.5171
10.1016/0022-2836(92)90894-P
10.1006/jmbi.1996.0004
10.1074/jbc.M009483200
ContentType Journal Article
DBID FBQ
AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
ADTOC
UNPAY
DOI 10.1016/s1016-8478(23)25245-0
DatabaseName AGRIS
CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
Unpaywall for CDI: Periodical Content
Unpaywall
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
DatabaseTitleList
MEDLINE - Academic
MEDLINE
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 3
  dbid: UNPAY
  name: Unpaywall
  url: https://proxy.k.utb.cz/login?url=https://unpaywall.org/
  sourceTypes: Open Access Repository
– sequence: 4
  dbid: FBQ
  name: AGRIS
  url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN
  sourceTypes: Publisher
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EndPage 29
ExternalDocumentID 10.1016/s1016-8478(23)25245-0
16258237
10_1016_S1016_8478_23_25245_0
KR2006013394
Genre Research Support, Non-U.S. Gov't
Journal Article
Review
GroupedDBID ---
.UV
0VY
123
1N0
29M
2VQ
2WC
30V
3V.
4.4
408
40D
53G
5VS
67N
67Z
7X7
88A
88E
8AO
8FE
8FH
8FI
8FJ
8TC
8UJ
95.
9ZL
AARHV
ABDBF
ABJNI
ABMNI
ABPTK
ABTEG
ABUWG
ACBXY
ACGFO
ACGFS
ACPRK
ACREN
ADBBV
ADINQ
ADKPE
AENEX
AFGCZ
AFKRA
AFLOW
AFNRJ
AGJBK
AHBYD
AHMBA
AHSBF
ALMA_UNASSIGNED_HOLDINGS
AMKLP
AMTXH
AOIJS
ASPBG
AVWKF
AZFZN
BBNVY
BENPR
BGNMA
BHPHI
BPHCQ
BVBZV
BVXVI
CAG
CCPQU
COF
CS3
CSCUP
DU5
E3Z
EAD
EAP
EBC
EBD
EBS
EJD
EMK
EMOBN
EST
ESX
F5P
FBQ
FDB
FYUFA
GX1
HCIFZ
HF~
HG6
HH5
HMCUK
HMJXF
HYE
HZ~
I09
I0C
IXC
I~X
JDI
KDC
KOV
KVFHK
LAS
LK8
M0L
M1P
M4Y
M7P
MA-
NU0
OK1
P2P
PQQKQ
PROAC
PSQYO
Q2X
R9I
ROL
RPM
RSV
S1Z
S27
S3A
S3B
SBL
SDH
SJN
SOJ
SV3
T13
TSK
TUS
U2A
UKHRP
VC2
WK8
Z45
~A9
0R~
AALRI
AAXUO
AAYWO
AAYXX
AAYZH
ABFSG
ACSTC
ACVFH
ADCNI
ADVLN
AEUPX
AEZWR
AFHIU
AFJKZ
AFPUW
AHWEU
AIGII
AITUG
AIXLP
AKBMS
AKRWK
AKYEP
AMRAJ
APXCP
CITATION
GROUPED_DOAJ
H13
M41
PHGZM
PHGZT
PJZUB
PPXIY
PQGLB
PUEGO
ALIPV
CGR
CUY
CVF
ECM
EIF
NPM
7X8
ADTOC
UNPAY
ID FETCH-LOGICAL-c442t-cc5851d2a2e76271956fbb1fca7e59c870b623888154e059afefebb9e9be5f8a3
IEDL.DBID UNPAY
ISSN 1016-8478
0219-1032
IngestDate Tue Aug 19 23:19:33 EDT 2025
Thu Sep 04 20:01:07 EDT 2025
Wed Feb 19 02:07:20 EST 2025
Thu Apr 24 22:55:58 EDT 2025
Wed Oct 01 04:23:01 EDT 2025
Wed Dec 27 19:18:17 EST 2023
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 1
Language English
License cc-by-nc-nd
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c442t-cc5851d2a2e76271956fbb1fca7e59c870b623888154e059afefebb9e9be5f8a3
Notes 2006013394
T10
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
content type line 23
OpenAccessLink https://proxy.k.utb.cz/login?url=https://doi.org/10.1016/s1016-8478(23)25245-0
PMID 16258237
PQID 68749015
PQPubID 23479
PageCount 13
ParticipantIDs unpaywall_primary_10_1016_s1016_8478_23_25245_0
proquest_miscellaneous_68749015
pubmed_primary_16258237
crossref_primary_10_1016_S1016_8478_23_25245_0
crossref_citationtrail_10_1016_S1016_8478_23_25245_0
fao_agris_KR2006013394
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 2005-08-31
PublicationDateYYYYMMDD 2005-08-31
PublicationDate_xml – month: 08
  year: 2005
  text: 2005-08-31
  day: 31
PublicationDecade 2000
PublicationPlace United States
PublicationPlace_xml – name: United States
PublicationTitle Molecules and cells
PublicationTitleAlternate Mol Cells
PublicationYear 2005
References Glaser (10.1016/S1016-8478(23)25245-0_bib26) 1992; 149
King (10.1016/S1016-8478(23)25245-0_bib51) 1994; 54
Maynard (10.1016/S1016-8478(23)25245-0_bib61) 2002; 20
Nissim (10.1016/S1016-8478(23)25245-0_bib67) 1994; 13
Golay (10.1016/S1016-8478(23)25245-0_bib27) 2000; 95
Chowdhury (10.1016/S1016-8478(23)25245-0_bib14) 2003; 2007
Ho (10.1016/S1016-8478(23)25245-0_bib38) 2005; 280
Barbas (10.1016/S1016-8478(23)25245-0_bib3) 1994; 91
Bruggemann (10.1016/S1016-8478(23)25245-0_bib9) 1997; 8
Yang (10.1016/S1016-8478(23)25245-0_bib97) 1995; 254
Roberts (10.1016/S1016-8478(23)25245-0_bib68) 1997; 94
Santimaria (10.1016/S1016-8478(23)25245-0_bib70) 2003; 9
Yang (10.1016/S1016-8478(23)25245-0_bib99) 1999; 59
Chowdhury (10.1016/S1016-8478(23)25245-0_bib15) 1999; 17
10.1016/S1016-8478(23)25245-0_bib79
Chames (10.1016/S1016-8478(23)25245-0_bib10) 2002; 169
Spada (10.1016/S1016-8478(23)25245-0_bib78) 1997; 378
Wu (10.1016/S1016-8478(23)25245-0_bib95) 1998; 95
Medzihradszky (10.1016/S1016-8478(23)25245-0_bib62) 2004; 14
Wu (10.1016/S1016-8478(23)25245-0_bib93) 2004; 248
Neuberger (10.1016/S1016-8478(23)25245-0_bib66) 1998; 162
Hwang (10.1016/S1016-8478(23)25245-0_bib45) 2005; 36
Woodle (10.1016/S1016-8478(23)25245-0_bib91) 1992; 1113
Huls (10.1016/S1016-8478(23)25245-0_bib42) 1999; 17
Hoogenboom (10.1016/S1016-8478(23)25245-0_bib40) 1992; 227
Tao (10.1016/S1016-8478(23)25245-0_bib81) 1993; 178
Hinton (10.1016/S1016-8478(23)25245-0_bib37) 2003; 279
Knappik (10.1016/S1016-8478(23)25245-0_bib53) 2000; 296
Hanes (10.1016/S1016-8478(23)25245-0_bib32) 1998; 95
Boder (10.1016/S1016-8478(23)25245-0_bib7) 1997; 15
Tsutsumi (10.1016/S1016-8478(23)25245-0_bib84) 2000; 97
Kuby (10.1016/S1016-8478(23)25245-0_bib56) 1997
Morrison (10.1016/S1016-8478(23)25245-0_bib64) 1984; 21
Francisco (10.1016/S1016-8478(23)25245-0_bib22) 1993; 90
Wright (10.1016/S1016-8478(23)25245-0_bib92) 1998; 160
Tsurushita (10.1016/S1016-8478(23)25245-0_bib83) 2005; 36
Hanes (10.1016/S1016-8478(23)25245-0_bib31) 1999; 243
Fishwild (10.1016/S1016-8478(23)25245-0_bib21) 1996; 14
Neal (10.1016/S1016-8478(23)25245-0_bib65) 2004; 10
Sensel (10.1016/S1016-8478(23)25245-0_bib73) 1977; 34
Schier (10.1016/S1016-8478(23)25245-0_bib71) 1996; 255
Fuchs (10.1016/S1016-8478(23)25245-0_bib23) 1991; 9
Colcher (10.1016/S1016-8478(23)25245-0_bib16) 1998; 42
10.1016/S1016-8478(23)25245-0_bib57
Duenas (10.1016/S1016-8478(23)25245-0_bib20) 1994; 12
Wu (10.1016/S1016-8478(23)25245-0_bib94) 2000; 44
Yang (10.1016/S1016-8478(23)25245-0_bib98) 1999; 66
Hassan (10.1016/S1016-8478(23)25245-0_bib34) 2002; 8
Hu (10.1016/S1016-8478(23)25245-0_bib43) 1996; 56
Shields (10.1016/S1016-8478(23)25245-0_bib74) 2001; 276
Schier (10.1016/S1016-8478(23)25245-0_bib72) 1996; 263
Bera (10.1016/S1016-8478(23)25245-0_bib5) 1998; 281
Chapman (10.1016/S1016-8478(23)25245-0_bib12) 2002; 54
Idusogie (10.1016/S1016-8478(23)25245-0_bib47) 2001; 166
Chang (10.1016/S1016-8478(23)25245-0_bib11) 2002; 1
Mattheakis (10.1016/S1016-8478(23)25245-0_bib60) 1994; 91
Tao (10.1016/S1016-8478(23)25245-0_bib80) 1991; 173
Valone (10.1016/S1016-8478(23)25245-0_bib85) 1995; 13
Hawkins (10.1016/S1016-8478(23)25245-0_bib35) 1992; 226
Shields (10.1016/S1016-8478(23)25245-0_bib75) 2002; 277
Griffiths (10.1016/S1016-8478(23)25245-0_bib29) 1994; 13
Daeron (10.1016/S1016-8478(23)25245-0_bib17) 1997; 15
Kuan (10.1016/S1016-8478(23)25245-0_bib55) 2000; 88
Dall’Acqua (10.1016/S1016-8478(23)25245-0_bib18) 2002; 169
Dall’Acqua (10.1016/S1016-8478(23)25245-0_bib19) 2005; 36
Valone (10.1016/S1016-8478(23)25245-0_bib86) 1995; 4
Georgiou (10.1016/S1016-8478(23)25245-0_bib25) 1997; 15
Gelderman (10.1016/S1016-8478(23)25245-0_bib24) 2004; 25
Wabl (10.1016/S1016-8478(23)25245-0_bib88) 1999; 11
Marks (10.1016/S1016-8478(23)25245-0_bib59) 1991; 222
Zhang (10.1016/S1016-8478(23)25245-0_bib100) 2004; 335
Bell (10.1016/S1016-8478(23)25245-0_bib4) 2000; 14
Holliger (10.1016/S1016-8478(23)25245-0_bib39) 1993; 90
Hoogenboom (10.1016/S1016-8478(23)25245-0_bib41) 1998; 4
Klein (10.1016/S1016-8478(23)25245-0_bib52) 1981; 78
Shinkawa (10.1016/S1016-8478(23)25245-0_bib76) 2003; 278
Vaughan (10.1016/S1016-8478(23)25245-0_bib87) 1996; 14
Ward (10.1016/S1016-8478(23)25245-0_bib89) 1989; 341
de Wildt (10.1016/S1016-8478(23)25245-0_bib90) 1996; 26
Treon (10.1016/S1016-8478(23)25245-0_bib82) 2001; 24
Chapman (10.1016/S1016-8478(23)25245-0_bib13) 1999; 17
Jones (10.1016/S1016-8478(23)25245-0_bib48) 1996; 321
Mendez (10.1016/S1016-8478(23)25245-0_bib63) 1997; 15
Kabat (10.1016/S1016-8478(23)25245-0_bib49) 1991
Gunneriusson (10.1016/S1016-8478(23)25245-0_bib30) 1996; 178
Brinkmann (10.1016/S1016-8478(23)25245-0_bib8) 1993; 90
Bird (10.1016/S1016-8478(23)25245-0_bib6) 1988; 242
Idusogie (10.1016/S1016-8478(23)25245-0_bib46) 2000; 164
Hanes (10.1016/S1016-8478(23)25245-0_bib33) 2000; 18
de Kruif (10.1016/S1016-8478(23)25245-0_bib54) 1995; 248
He (10.1016/S1016-8478(23)25245-0_bib36) 1997; 25
Griffiths (10.1016/S1016-8478(23)25245-0_bib28) 1998; 9
Barbas (10.1016/S1016-8478(23)25245-0_bib2) 1992; 89
Hwang (10.1016/S1016-8478(23)25245-0_bib44) 2005; 36
Salvatore (10.1016/S1016-8478(23)25245-0_bib69) 2002; 8
Smallshaw (10.1016/S1016-8478(23)25245-0_bib77) 2003; 21
Lund (10.1016/S1016-8478(23)25245-0_bib58) 1996; 157
Wu (10.1016/S1016-8478(23)25245-0_bib96) 1999; 294
Adams (10.1016/S1016-8478(23)25245-0_bib1) 1998; 58
Kashmiri (10.1016/S1016-8478(23)25245-0_bib50) 2005; 36
References_xml – volume: 164
  start-page: 4178
  year: 2000
  ident: 10.1016/S1016-8478(23)25245-0_bib46
  article-title: Mapping of the C1q binding site on rituxan, a chimeric antibody with a human IgG1 Fc.
  publication-title: J. Immunol.
  doi: 10.4049/jimmunol.164.8.4178
– volume: 15
  start-page: 146
  year: 1997
  ident: 10.1016/S1016-8478(23)25245-0_bib63
  article-title: Functional transplant of megabase human immunoglobulin loci recapitulates human antibody response in mice.
  publication-title: Nat. Genet.
  doi: 10.1038/ng0297-146
– volume: 321
  start-page: 522
  year: 1996
  ident: 10.1016/S1016-8478(23)25245-0_bib48
  article-title: Replacing the complementarity-determining regions in a human antibody with those from a mouse.
  publication-title: Nature
  doi: 10.1038/321522a0
– volume: 21
  start-page: 6851
  year: 1984
  ident: 10.1016/S1016-8478(23)25245-0_bib64
  article-title: Chimeric human antibody molecules; mouse antigen binding domains with human constant region domains.
  publication-title: Proc. Nat1 Acad. Sci. USA
  doi: 10.1073/pnas.81.21.6851
– volume: 25
  start-page: 5132
  year: 1997
  ident: 10.1016/S1016-8478(23)25245-0_bib36
  article-title: Antibodyribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites.
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/25.24.5132
– volume: 14
  start-page: 501
  year: 2000
  ident: 10.1016/S1016-8478(23)25245-0_bib4
  article-title: The clinical role of anti-TNFa antibody treatment in Crohn’s disease.
  publication-title: Aliment. Phamacol. Ther.
  doi: 10.1046/j.1365-2036.2000.00777.x
– volume: 14
  start-page: 845
  year: 1996
  ident: 10.1016/S1016-8478(23)25245-0_bib21
  article-title: High-avidity human IgG kappa monoclonal antibodies from a novel strain of minilocus transgenic mice.
  publication-title: Nat. Biotechnol.
  doi: 10.1038/nbt0796-845
– volume: 169
  start-page: 1110
  year: 2002
  ident: 10.1016/S1016-8478(23)25245-0_bib10
  article-title: TCR-like human antibodies expressed on human CTLs mediate antibody affinity-dependent cytolytic activity.
  publication-title: J. Immunol.
  doi: 10.4049/jimmunol.169.2.1110
– volume: 341
  start-page: 544
  year: 1989
  ident: 10.1016/S1016-8478(23)25245-0_bib89
  article-title: Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli.
  publication-title: Nature
  doi: 10.1038/341544a0
– volume: 277
  start-page: 26733
  year: 2002
  ident: 10.1016/S1016-8478(23)25245-0_bib75
  article-title: Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcΓRIII and antibodydependent cellular toxicity.
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M202069200
– volume: 91
  start-page: 3809
  year: 1994
  ident: 10.1016/S1016-8478(23)25245-0_bib3
  article-title: In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity.
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.91.9.3809
– volume: 90
  start-page: 6444
  year: 1993
  ident: 10.1016/S1016-8478(23)25245-0_bib39
  article-title: ‘Diabodies’: Small bivalent and bispecific antibody fragments.
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.90.14.6444
– volume: 97
  start-page: 8548
  year: 2000
  ident: 10.1016/S1016-8478(23)25245-0_bib84
  article-title: Site-specific chemical modification with polyethylene glycol of recombinant immunotoxin anti-Tac(Fv)-PE38 (LMB-2) improves antitumor activity and reduces animal toxicity and immunogenicity.
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.140210597
– volume: 11
  start-page: 186
  year: 1999
  ident: 10.1016/S1016-8478(23)25245-0_bib88
  article-title: Hypermutation in antibody affinity maturation.
  publication-title: Curr. Opin. Immunol.
  doi: 10.1016/S0952-7915(99)80031-4
– volume: 89
  start-page: 4457
  year: 1992
  ident: 10.1016/S1016-8478(23)25245-0_bib2
  article-title: Semisynthetic combinatorial antibody libraries: a chemical solution to the diversity problem.
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.89.10.4457
– volume: 10
  start-page: 4839
  year: 2004
  ident: 10.1016/S1016-8478(23)25245-0_bib65
  article-title: Enhanced activity of hu14.18-IL2 immunocytokine against murine NXS2 neuroblastoma when combined with interleukin 2 therapy.
  publication-title: Clin. Cancer Res.
  doi: 10.1158/1078-0432.CCR-03-0799
– volume: 21
  start-page: 387
  year: 2003
  ident: 10.1016/S1016-8478(23)25245-0_bib77
  article-title: Genetic engineering of an immunotoxin to eliminate pulmonary vascular leak in mice.
  publication-title: Nat. Biotechnol.
  doi: 10.1038/nbt800
– volume: 56
  start-page: 3055
  year: 1996
  ident: 10.1016/S1016-8478(23)25245-0_bib43
  article-title: Minibody: A novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-C(H)3) which exhibits rapid, high-level targeting of xenografts.
  publication-title: Cancer Res.
– volume: 14
  start-page: 27
  year: 2004
  ident: 10.1016/S1016-8478(23)25245-0_bib62
  article-title: Glycoforms obtained by expression in Pichia pastoris improve cancer targeting potential of a recombinant antibody-enzyme fusion protein.
  publication-title: Glycobiology
  doi: 10.1093/glycob/cwh001
– volume: 42
  start-page: 225
  year: 1998
  ident: 10.1016/S1016-8478(23)25245-0_bib16
  article-title: Pharmacokinetics and biodistribution of genetically-engineered antibodies.
  publication-title: Q. J. Nucl. Med.
– ident: 10.1016/S1016-8478(23)25245-0_bib79
– volume: 248
  start-page: 209
  year: 2004
  ident: 10.1016/S1016-8478(23)25245-0_bib93
  article-title: Engineering multivalent antibody fragments for in vivo targeting.
  publication-title: Methods Mol. Biol.
– volume: 280
  start-page: 607
  year: 2005
  ident: 10.1016/S1016-8478(23)25245-0_bib38
  article-title: In vitro antibody evolution targeting germline hot spots to increase activity of an anti-CD22 immunotoxin.
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M409783200
– volume: 166
  start-page: 2571
  year: 2001
  ident: 10.1016/S1016-8478(23)25245-0_bib47
  article-title: Engineered antibodies with increased activity to recruit complement.
  publication-title: J. Immunol.
  doi: 10.4049/jimmunol.166.4.2571
– volume: 24
  start-page: 263
  year: 2001
  ident: 10.1016/S1016-8478(23)25245-0_bib82
  article-title: Tumor cell expression of CD59 is associated with resistance to CD20 serotherapy in patients with B-cell malignancies.
  publication-title: J. Immunother.
  doi: 10.1097/00002371-200105000-00011
– volume: 44
  start-page: 268
  year: 2000
  ident: 10.1016/S1016-8478(23)25245-0_bib94
  article-title: Designer genes: recombinant antibody fragments for biological imaging.
  publication-title: Q. J. Nucl. Med.
– volume: 178
  start-page: 661
  year: 1993
  ident: 10.1016/S1016-8478(23)25245-0_bib81
  article-title: Structural features of human immunoglobulin G that determine isotypespecific differences in complement activation.
  publication-title: J. Exp. Med.
  doi: 10.1084/jem.178.2.661
– volume: 160
  start-page: 3393
  year: 1998
  ident: 10.1016/S1016-8478(23)25245-0_bib92
  article-title: Effect of C2-associated carbohydrate structure on Ig effector function: studies with chimeric mouse-human IgG1 antibodies in glycosylation mutants of Chinese hamster ovary cells.
  publication-title: J. Immunol.
  doi: 10.4049/jimmunol.160.7.3393
– volume: 58
  start-page: 485
  year: 1998
  ident: 10.1016/S1016-8478(23)25245-0_bib1
  article-title: Increased affinity leads to improved selective tumor delivery of single-chain Fv antibodies.
  publication-title: Cancer Res.
– volume: 25
  start-page: 158
  year: 2004
  ident: 10.1016/S1016-8478(23)25245-0_bib24
  article-title: Complement function in mAb-mediated cancer immunotherapy.
  publication-title: Trends Immunol.
  doi: 10.1016/j.it.2004.01.008
– volume: 17
  start-page: 276
  year: 1999
  ident: 10.1016/S1016-8478(23)25245-0_bib42
  article-title: A recombinant, fully human monoclonal antibody with antitumor activity constructed from phage-displayed antibody fragments.
  publication-title: Nat. Biotechnol.
  doi: 10.1038/7023
– volume: 59
  start-page: 1236
  year: 1999
  ident: 10.1016/S1016-8478(23)25245-0_bib99
  article-title: Eradication of established tumors by a fully human monoclonal antibody to the epidermal growth factor receptor without concomitant chemotherapy.
  publication-title: Cancer Res.
– volume: 294
  start-page: 151
  year: 1999
  ident: 10.1016/S1016-8478(23)25245-0_bib96
  article-title: Humanization of a murine monoclonal antibody by simultaneous optimization of framework and CDR residues.
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1999.3141
– volume: 173
  start-page: 1025
  year: 1991
  ident: 10.1016/S1016-8478(23)25245-0_bib80
  article-title: The differential ability of human IgG1 and IgG4 to activate complement is determined by the COOH-terminal sequence of the CH2 domain.
  publication-title: J. Exp. Med.
  doi: 10.1084/jem.173.4.1025
– start-page: 664
  year: 1997
  ident: 10.1016/S1016-8478(23)25245-0_bib56
– volume: 9
  start-page: 571
  year: 2003
  ident: 10.1016/S1016-8478(23)25245-0_bib70
  article-title: Immunoscintigraphic detection of the ED-B domain of fibronectin, a marker of angiogenesis, in patients with cancer.
  publication-title: Clin. Cancer Res.
– volume: 90
  start-page: 10444
  year: 1993
  ident: 10.1016/S1016-8478(23)25245-0_bib22
  article-title: Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface.
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.90.22.10444
– volume: 36
  start-page: 69
  year: 2005
  ident: 10.1016/S1016-8478(23)25245-0_bib83
  article-title: Design of humanized antibodies: from anti-Tac to Zenapax.
  publication-title: Methods
  doi: 10.1016/j.ymeth.2005.01.007
– volume: 4
  start-page: 471
  year: 1995
  ident: 10.1016/S1016-8478(23)25245-0_bib86
  article-title: Clinical trials of bispecific antibody MDX-210 in women with advanced breast or ovarian cancer that overexpresses HER-2/neu.
  publication-title: J. Hematother.
  doi: 10.1089/scd.1.1995.4.471
– volume: 95
  start-page: 14130
  year: 1998
  ident: 10.1016/S1016-8478(23)25245-0_bib32
  article-title: Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries.
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.95.24.14130
– volume: 263
  start-page: 551
  year: 1996
  ident: 10.1016/S1016-8478(23)25245-0_bib72
  article-title: Isolation of picomolar affinity anti-c-erbB-2 single-chain Fv by molecular evolution of the complementarity determining regions in the center of the antibody binding site.
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1996.0598
– volume: 15
  start-page: 203
  year: 1997
  ident: 10.1016/S1016-8478(23)25245-0_bib17
  article-title: Fc receptor biology.
  publication-title: Ann. Rev. Immunol.
  doi: 10.1146/annurev.immunol.15.1.203
– volume: 281
  start-page: 475
  year: 1998
  ident: 10.1016/S1016-8478(23)25245-0_bib5
  article-title: A bivalent disulfide-stabilized fv with improved antigen binding to erbb2.
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1998.1948
– volume: 36
  start-page: 43
  year: 2005
  ident: 10.1016/S1016-8478(23)25245-0_bib19
  article-title: Antibody humanization by framework shuffling.
  publication-title: Methods.
  doi: 10.1016/j.ymeth.2005.01.005
– volume: 9
  start-page: 1369
  year: 1991
  ident: 10.1016/S1016-8478(23)25245-0_bib23
  article-title: Targeting recombinant antibodies to the surface of Escherichia coli: fusion to a peptidoglycan associated lipoprotein.
  publication-title: Bio-Technology
  doi: 10.1038/nbt1291-1369
– volume: 36
  start-page: 25
  year: 2005
  ident: 10.1016/S1016-8478(23)25245-0_bib50
  article-title: SDR grafting--a new approach to antibody humanization.
  publication-title: Methods.
  doi: 10.1016/j.ymeth.2005.01.003
– volume: 95
  start-page: 3900
  year: 2000
  ident: 10.1016/S1016-8478(23)25245-0_bib27
  article-title: Biologic response of B lymphoma cells to anti-CD20 monoclonal antibody rituximab in vitro: CD55 and CD59 regulate complement-mediated cell lysis
  publication-title: Blood
  doi: 10.1182/blood.V95.12.3900.012k14_3900_3908
– volume: 20
  start-page: 597
  year: 2002
  ident: 10.1016/S1016-8478(23)25245-0_bib61
  article-title: Protection against anthrax toxin by recombinant antibody fragments correlates with antigen affinity.
  publication-title: Nat. Biotechnol.
  doi: 10.1038/nbt0602-597
– volume: 18
  start-page: 1287
  year: 2000
  ident: 10.1016/S1016-8478(23)25245-0_bib33
  article-title: Picomolar affinity antibodies from a fully synthetic naive library selected and evolved by ribosome display.
  publication-title: Nat. Biotechnol.
  doi: 10.1038/82407
– volume: 378
  start-page: 445
  year: 1997
  ident: 10.1016/S1016-8478(23)25245-0_bib78
  article-title: Selectively infective phages (SIP).
  publication-title: Biol. Chem.
– volume: 149
  start-page: 3903
  year: 1992
  ident: 10.1016/S1016-8478(23)25245-0_bib26
  article-title: Antibody engineering by codon-based mutagenesis in a filamentous phage vector system.
  publication-title: J. Immunol.
  doi: 10.4049/jimmunol.149.12.3903
– volume: 222
  start-page: 581
  year: 1991
  ident: 10.1016/S1016-8478(23)25245-0_bib59
  article-title: Bypassing immunization. Human antibodies from V-gene libraries displayed on phage.
  publication-title: J. Mol. Biol.
  doi: 10.1016/0022-2836(91)90498-U
– volume: 1
  start-page: 553
  year: 2002
  ident: 10.1016/S1016-8478(23)25245-0_bib11
  article-title: Molecular advances in pretargeting radioimunotherapy with bispecific antibodies.
  publication-title: Mol. Cancer Ther.
– volume: 178
  start-page: 1341
  year: 1996
  ident: 10.1016/S1016-8478(23)25245-0_bib30
  article-title: Surface display of a functional single-chain Fv antibody on staphylococci.
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.178.5.1341-1346.1996
– volume: 94
  start-page: 12297
  year: 1997
  ident: 10.1016/S1016-8478(23)25245-0_bib68
  article-title: RNApeptide fusions for the in vitro selection of peptides and proteins.
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.94.23.12297
– volume: 14
  start-page: 309
  year: 1996
  ident: 10.1016/S1016-8478(23)25245-0_bib87
  article-title: Human antibodies with subnanomolar affinities isolated from a large non-immunized phage display library.
  publication-title: Nat. Biotechnol.
  doi: 10.1038/nbt0396-309
– volume: 4
  start-page: 1
  year: 1998
  ident: 10.1016/S1016-8478(23)25245-0_bib41
  article-title: Antibody phage display technology and its applications.
  publication-title: Immunotechnology
  doi: 10.1016/S1380-2933(98)00007-4
– volume: 8
  start-page: 455
  year: 1997
  ident: 10.1016/S1016-8478(23)25245-0_bib9
  article-title: Production of human antibody repertoires in transgenic mice.
  publication-title: Curr. Opin. Biotechnol.
  doi: 10.1016/S0958-1669(97)80068-7
– volume: 296
  start-page: 57
  year: 2000
  ident: 10.1016/S1016-8478(23)25245-0_bib53
  article-title: Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs with randomized trinucleotides.
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1999.3444
– volume: 8
  start-page: 995
  year: 2002
  ident: 10.1016/S1016-8478(23)25245-0_bib69
  article-title: Improved cytotoxic activity toward cell lines and fresh leukemia cells of a mutant anti-CD22 immunotoxin obtained by antibody phage display.
  publication-title: Clin. Cancer Res.
– volume: 90
  start-page: 7538
  year: 1993
  ident: 10.1016/S1016-8478(23)25245-0_bib8
  article-title: A recombinant immunotoxin containing a disulfidestabilized Fv fragment
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.90.16.7538
– year: 1991
  ident: 10.1016/S1016-8478(23)25245-0_bib49
  article-title: Sequences of Proteins of Immunological Interests,
– volume: 243
  start-page: 107
  year: 1999
  ident: 10.1016/S1016-8478(23)25245-0_bib31
  article-title: In vitro selection methods for screening of peptide and protein libraries.
  publication-title: Curr. Top. Microbiol. Immunol.
– volume: 157
  start-page: 4963
  year: 1996
  ident: 10.1016/S1016-8478(23)25245-0_bib58
  article-title: Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fcγ receptor I and influence the synthesis of its oligosaccharide chains.
  publication-title: J. Immunol.
  doi: 10.4049/jimmunol.157.11.4963
– volume: 15
  start-page: 553
  year: 1997
  ident: 10.1016/S1016-8478(23)25245-0_bib7
  article-title: Yeast surface display for screening combinatorial polypeptide libraries.
  publication-title: Nat. Biotechnol.
  doi: 10.1038/nbt0697-553
– volume: 278
  start-page: 3466
  year: 2003
  ident: 10.1016/S1016-8478(23)25245-0_bib76
  article-title: The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity.
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M210665200
– volume: 9
  start-page: 102
  year: 1998
  ident: 10.1016/S1016-8478(23)25245-0_bib28
  article-title: Strategies for selection of antibodies by phage display.
  publication-title: Curr. Opin. Biotechnol.
  doi: 10.1016/S0958-1669(98)80092-X
– volume: 36
  start-page: 35
  year: 2005
  ident: 10.1016/S1016-8478(23)25245-0_bib45
  article-title: Use of human germline genes in a CDR homologybased approach to antibody humanization.
  publication-title: Methods
  doi: 10.1016/j.ymeth.2005.01.004
– volume: 15
  start-page: 29
  year: 1997
  ident: 10.1016/S1016-8478(23)25245-0_bib25
  article-title: Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines.
  publication-title: Nat. Biotechnol.
  doi: 10.1038/nbt0197-29
– volume: 2007
  start-page: 179
  year: 2003
  ident: 10.1016/S1016-8478(23)25245-0_bib14
  article-title: Engineering hot spots for affinity enhancement of antibodies.
  publication-title: Methods Mol. Biol.
– volume: 8
  start-page: 3520
  year: 2002
  ident: 10.1016/S1016-8478(23)25245-0_bib34
  article-title: Antitumor activity of SS (dsFv) PE38 and SS1(dsFv)PE38, recombinant antimesothelin immunotoxins against human gynecologic cancers grown in organotypic culture in vitro.
  publication-title: Clin. Cancer Res.
– volume: 91
  start-page: 9022
  year: 1994
  ident: 10.1016/S1016-8478(23)25245-0_bib60
  article-title: An in vitro polysome display system for identifying ligands from very large peptide libraries.
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.91.19.9022
– volume: 13
  start-page: 2281
  year: 1995
  ident: 10.1016/S1016-8478(23)25245-0_bib85
  article-title: Phase Ia/Ib trial of bispecific antibody MDX-210 in patients with advanced breast or ovarian cancer that overexpresses the proto-oncogene HER-2/neu.
  publication-title: J. Clin. Oncol.
  doi: 10.1200/JCO.1995.13.9.2281
– volume: 54
  start-page: 531
  year: 2002
  ident: 10.1016/S1016-8478(23)25245-0_bib12
  article-title: PEGylated antibodies and antibody fragments for improved therapy: a review.
  publication-title: Adv. Drug Deliv. Rev
  doi: 10.1016/S0169-409X(02)00026-1
– volume: 95
  start-page: 6037
  year: 1998
  ident: 10.1016/S1016-8478(23)25245-0_bib95
  article-title: Stepwise in vitro affinity maturation of Vitaxin, an α(v)β3-specific humanized mAb.
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.95.11.6037
– volume: 13
  start-page: 3245
  year: 1994
  ident: 10.1016/S1016-8478(23)25245-0_bib29
  article-title: Isolation of high affinity human antibodies directly from large synthetic repertoires.
  publication-title: EMBO J.
  doi: 10.1002/j.1460-2075.1994.tb06626.x
– ident: 10.1016/S1016-8478(23)25245-0_bib57
– volume: 242
  start-page: 423
  year: 1988
  ident: 10.1016/S1016-8478(23)25245-0_bib6
  article-title: Single-chain antigen-binding proteins.
  publication-title: Science
  doi: 10.1126/science.3140379
– volume: 12
  start-page: 999
  year: 1994
  ident: 10.1016/S1016-8478(23)25245-0_bib20
  article-title: Clonal selection and amplification of phage displayed antibodies by linking antigen recognition and phage replication.
  publication-title: Bio-Technology
  doi: 10.1038/nbt1094-999
– volume: 36
  start-page: 3
  year: 2005
  ident: 10.1016/S1016-8478(23)25245-0_bib44
  article-title: Immunogenicity of engineered antibodies.
  publication-title: Methods
  doi: 10.1016/j.ymeth.2005.01.001
– volume: 1113
  start-page: 171
  year: 1992
  ident: 10.1016/S1016-8478(23)25245-0_bib91
  article-title: Sterically stabilized liposomes.
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0304-4157(92)90038-C
– volume: 226
  start-page: 889
  year: 1992
  ident: 10.1016/S1016-8478(23)25245-0_bib35
  article-title: Selection of phage antibodies by binding affinity. Mimicking affinity maturation.
  publication-title: J. Mol. Biol.
  doi: 10.1016/0022-2836(92)90639-2
– volume: 254
  start-page: 392
  year: 1995
  ident: 10.1016/S1016-8478(23)25245-0_bib97
  article-title: CDR Walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range.
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1995.0626
– volume: 17
  start-page: 568
  year: 1999
  ident: 10.1016/S1016-8478(23)25245-0_bib15
  article-title: Improving antibody affinity by mimicking somatic hypermutation in vitro.
  publication-title: Nat. Biotechnol.
  doi: 10.1038/9872
– volume: 162
  start-page: 107
  year: 1998
  ident: 10.1016/S1016-8478(23)25245-0_bib66
  article-title: Monitoring and interpreting the intrinsic features of somatic hypermutation.
  publication-title: Immunol. Rev.
  doi: 10.1111/j.1600-065X.1998.tb01434.x
– volume: 66
  start-page: 401
  year: 1999
  ident: 10.1016/S1016-8478(23)25245-0_bib98
  article-title: Fully human antiinterleukin-8 monoclonal antibodies: potential therapeutics for the treatment of inflammatory disease states.
  publication-title: J. Leukocyte Biol.
  doi: 10.1002/jlb.66.3.401
– volume: 26
  start-page: 629
  year: 1996
  ident: 10.1016/S1016-8478(23)25245-0_bib90
  article-title: Characterization of human variable domain antibody fragments against the U1 RNA-associated A protein, selected from a synthetic and patient-derived combinatorial V gene library.
  publication-title: Eur. J. Immunol.
  doi: 10.1002/eji.1830260319
– volume: 34
  start-page: 1019
  year: 1977
  ident: 10.1016/S1016-8478(23)25245-0_bib73
  article-title: Amino acid differences in the N-terminus of CH2 influence the relative abilities of IgG2 and IgG3 to active complement.
  publication-title: Mol. Immunol.
  doi: 10.1016/S0161-5890(97)00112-0
– volume: 279
  start-page: 6213
  year: 2003
  ident: 10.1016/S1016-8478(23)25245-0_bib37
  article-title: Engineered human IgG antibodies with longer serum half-lives in primates.
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.C300470200
– volume: 78
  start-page: 524
  year: 1981
  ident: 10.1016/S1016-8478(23)25245-0_bib52
  article-title: Expression of biological effector functions by immunoglobulin G molecules lacking the hinge region.
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.78.1.524
– volume: 54
  start-page: 6176
  year: 1994
  ident: 10.1016/S1016-8478(23)25245-0_bib51
  article-title: Improved tumor targeting with chemically cross-linked recombinant antibody fragments.
  publication-title: Cancer Res.
– volume: 335
  start-page: 209
  year: 2004
  ident: 10.1016/S1016-8478(23)25245-0_bib100
  article-title: Improved breadth and potency of an HIV-1-neutralizing human single-chain antibody by random mutagenesis and sequential antigen panning.
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2003.09.055
– volume: 13
  start-page: 692
  year: 1994
  ident: 10.1016/S1016-8478(23)25245-0_bib67
  article-title: Antibody fragments from a ‘single pot’ phage display library as immunochemical reagents.
  publication-title: EMBO J.
  doi: 10.1002/j.1460-2075.1994.tb06308.x
– volume: 88
  start-page: 962
  year: 2000
  ident: 10.1016/S1016-8478(23)25245-0_bib55
  article-title: Increased binding affinity enhances targeting of glioma xenografts by EGFRVIII-specific scFV.
  publication-title: Int. J. Cancer
  doi: 10.1002/1097-0215(20001215)88:6<962::AID-IJC20>3.0.CO;2-U
– volume: 248
  start-page: 97
  year: 1995
  ident: 10.1016/S1016-8478(23)25245-0_bib54
  article-title: Selection and application of human single chain Fv antibody fragments from a semi-synthetic phage antibody display library with designed CDR3 regions.
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1995.0204
– volume: 17
  start-page: 780
  year: 1999
  ident: 10.1016/S1016-8478(23)25245-0_bib13
  article-title: Therapeutic antibody fragments with prolonged in vivo half-lives.
  publication-title: Nat. Biotechnol.
  doi: 10.1038/11717
– volume: 169
  start-page: 5171
  year: 2002
  ident: 10.1016/S1016-8478(23)25245-0_bib18
  article-title: Increasing the affinity of a human IgG1 for the neonatal Fc receptor: Biological consequences.
  publication-title: J. Immunol.
  doi: 10.4049/jimmunol.169.9.5171
– volume: 227
  start-page: 381
  year: 1992
  ident: 10.1016/S1016-8478(23)25245-0_bib40
  article-title: Bypassing immunisation. Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro.
  publication-title: J. Mol. Biol.
  doi: 10.1016/0022-2836(92)90894-P
– volume: 255
  start-page: 28
  year: 1996
  ident: 10.1016/S1016-8478(23)25245-0_bib71
  article-title: Isolation of high-affinity monomeric human anti-c-erbB-2 single chain Fv using affinity-driven selection.
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1996.0004
– volume: 276
  start-page: 6591
  year: 2001
  ident: 10.1016/S1016-8478(23)25245-0_bib74
  article-title: High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR.
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M009483200
SSID ssj0017628
Score 2.1356914
SecondaryResourceType review_article
Snippet Therapeutic antibodies represent one of the fastest growing areas of the pharmaceutical industry. There are currently 19 monoclonal antibodies in the market...
SourceID unpaywall
proquest
pubmed
crossref
fao
SourceType Open Access Repository
Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 17
SubjectTerms Affinity Maturation
Animals
Antibodies - chemistry
Antibodies - physiology
Antibodies, Monoclonal - chemistry
Antibody Affinity
Antibody Engineering
Antibody Fragments
Effector Functions
Human Monoclonal Antibodies
Humanized Antibodies
Humans
MEDICINAL PROPERTIES
Mice
Models, Molecular
Pharmacokinetics
PROPIEDADES MEDICINALES
PROPRIETE PHARMACOLOGIQUE
Protein Engineering - methods
Recombinant Fusion Proteins - chemistry
Technology, Pharmaceutical
Therapeutic Antibodies
Title Antibody Engineering for the Development of Therapeutic Antibodies
URI https://www.ncbi.nlm.nih.gov/pubmed/16258237
https://www.proquest.com/docview/68749015
https://doi.org/10.1016/s1016-8478(23)25245-0
UnpaywallVersion publishedVersion
Volume 20
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
journalDatabaseRights – providerCode: PRVFSB
  databaseName: Free Full-Text Journals in Chemistry
  issn: 1016-8478
  databaseCode: HH5
  dateStart: 19900101
  customDbUrl:
  isFulltext: true
  dateEnd: 20081231
  titleUrlDefault: http://abc-chemistry.org/
  omitProxy: true
  ssIdentifier: ssj0017628
  providerName: ABC ChemistRy
– providerCode: PRVFQY
  databaseName: GFMER Free Medical Journals
  issn: 1016-8478
  databaseCode: GX1
  dateStart: 0
  customDbUrl:
  isFulltext: true
  dateEnd: 99991231
  titleUrlDefault: http://www.gfmer.ch/Medical_journals/Free_medical.php
  omitProxy: true
  ssIdentifier: ssj0017628
  providerName: Geneva Foundation for Medical Education and Research
– providerCode: PRVLSH
  databaseName: Elsevier Journals
  issn: 1016-8478
  databaseCode: AKRWK
  dateStart: 19901001
  customDbUrl:
  isFulltext: true
  mediaType: online
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0017628
  providerName: Library Specific Holdings
– providerCode: PRVAVX
  databaseName: SpringerLink Journals (ICM)
  issn: 1016-8478
  databaseCode: U2A
  dateStart: 20000201
  customDbUrl:
  isFulltext: true
  dateEnd: 99991231
  titleUrlDefault: http://www.springerlink.com/journals/
  omitProxy: true
  ssIdentifier: ssj0017628
  providerName: Springer Nature
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1dT9swFL0aRRPwsA-gEBjFD3uAh5TYcdLmsUOrKiYqhKjUPVm24yBElVQ0FSq_nusk_WCrNPaSt5M4_jzX1-cY4HvAtR-248ClCTcu58pzVYSBK8ZCfkBbNOaFKu26H_YG_GoYDCuxutXCvMnf09BK3CgiEXHG_HMWMB64GKFvhjafVIPNQf-m87vYR6GRa83hiuxmBVkqdta_581atJHIbB3N3IGtaTqWs2c5Gq0sPd3P0J8Xujxx8tic5qqpX_7wc3z3X32BTxUJJZ2y13yFDybdhY_ltZSzPfjRSfMHlcUzsuJWSJDdEmSLZOWYEckScrcUcJEKh8H3Pgy6P-8ue25114KrOWe5q7XND8ZMMoPTY8uqCBOlaKJlywSRxlGtkChhuIyUyyAlk4lJjFKRiZQJkrb061BLs9QcAuGyLZVizFNUcYPrXUwRiMTRiz3DtHaAz2td6MqI3N6HMRKLE2fF01aPYL4oqkd4DjQXsHHpxPEvQB2bVMh7nC3Fr1tWWM_4fsQdOJ23ssDBZDMkMjXZdCLCdotbguTAQdn4yy9hnGh9fRy4WPSGv4oxWVeMo_9GHMN2YRBb7Fx_g1r-NDUnSH1y1YCNAes0qm7_ClvB8MQ
linkProvider Unpaywall
linkToUnpaywall http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1db9MwFL3aWqHBAxtsg4wBfuABHlJix_l6LGhVBVqFUCuVJ8t2HDRRJRVNhMqv33WSfkGlbS95O4njz3N9fY4B3gVc-2GcBi7NuHE5V56rEgxcMRbyAxrRlNeqtOtROJzwL9Ng2orVrRZmJ39PQytxo4hExHvmf2AB44GLEXo3tPmkDnQno2_9H_U-Ck1caw5XZzdbyEaxs_89O2vRYSaLfTTzCRxV-Vwu_8jZbGvpGRzDaFXo5sTJr15Vqp7--4-f473_6gSetiSU9Jte8wwOTP4cHjXXUi5P4VM_L29UkS7JllshQXZLkC2SrWNGpMjIeCPgIi0Og-8zmAyuxp-HbnvXgqs5Z6Wrtc0Ppkwyg9NjZFWEmVI00zIyQaJxVCskShguI-UySMlkZjKjVGISZYIslv45dPIiNy-BcBlLpRjzFFXc4HqXUgQicfRSzzCtHeCrWhe6NSK392HMxPrEWf201SOYL-rqEZ4DvTVs3jhx3AU4xyYV8ifOluLrd1Zbz_h-wh14u2plgYPJZkhkbopqIcI44pYgOfCiafzNlzBOtL4-Dnxc94b_irHYV4yLByNewePaILbeub6ETvm7Mq-R-pTqTdvhbwG8ue_b
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Antibody+engineering+for+the+development+of+therapeutic+antibodies&rft.jtitle=Molecules+and+cells&rft.au=Kim%2C+Sang+Jick&rft.au=Park%2C+Youngwoo&rft.au=Hong%2C+Hyo+Jeong&rft.date=2005-08-31&rft.issn=1016-8478&rft.volume=20&rft.issue=1&rft.spage=17&rft_id=info:doi/10.1016%2Fs1016-8478%2823%2925245-0&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1016-8478&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1016-8478&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1016-8478&client=summon