Revisiting the role of glycosylation in the structure of human IgG Fc. - Wikidata - awgldk - TriplyDB

Revisiting the role of glycosylation in the structure of human IgG Fc.

Revisiting the role of glycosylation in the structure of human IgG Fc.

http://www.wikidata.org/entity/Q36252642

about

Advances in alloimmune thrombocytopenia: perspectives on current concepts of human platelet antigens, antibody detection strategies, and genotyping A perspective on the structure and receptor binding properties of immunoglobulin G Fc Chemical and Structural Analysis of an Antibody Folding Intermediate Trapped during Glycan Biosynthesis High-resolution structures of the IgM Fc domains reveal principles of its hexamer formation Engineering Hydrophobic Protein–Carbohydrate Interactions to Fine-Tune Monoclonal Antibodies Immunoglobulin G1 Fc Domain Motions: Implications for Fc Engineering Crystal structure of deglycosylated human IgG4-Fc Advances in Therapeutic Fc Engineering - Modulation of IgG-Associated Effector Functions and Serum Half-life High-throughput biophysical analysis and data visualization of conformational stability of an IgG1 monoclonal antibody after deglycosylation.A Novel Platform for the Potentiation of Therapeutic Antibodies Based on Antigen-Dependent Formation of IgG Hexamers at the Cell Surface.The Structural Role of Antibody N-Glycosylation in Receptor Interactions Glycoproteomic analysis of antibodies.Stabilizing the CH2 Domain of an Antibody by Engineering in an Enhanced Aromatic Sequon General mechanism for modulating immunoglobulin effector function.Therapeutic potential of deglycosylated antibodies.Knobs-into-holes antibody production in mammalian cell lines reveals that asymmetric afucosylation is sufficient for full antibody-dependent cellular cytotoxicity.Fc-mediated activity of EGFR x c-Met bispecific antibody JNJ-61186372 enhanced killing of lung cancer cells Type I and type II Fc receptors regulate innate and adaptive immunity.Fcγ receptor pathways during active and passive immunization.Structural analysis of Fc/FcγR complexes: a blueprint for antibody design.IgG Fc domains that bind C1q but not effector Fcγ receptors delineate the importance of complement-mediated effector functions.Fc Engineering of Human IgG1 for Altered Binding to the Neonatal Fc Receptor Affects Fc Effector Functions.Recombinant H22(scFv) blocks CD64 and prevents the capture of anti-TNF monoclonal antibody. A potential strategy to enhance anti-TNF therapy.Effect of glucose feeding on the glycosylation quality of antibody produced by a human cell line, F2N78, in fed-batch culture.The Role and Function of Fcγ Receptors on Myeloid Cells.Glycosylation engineering of therapeutic IgG antibodies: challenges for the safety, functionality and efficacy.Glycosylation of IgG-Fc: a molecular perspective.Fragments of bacterial endoglycosidase s and immunoglobulin g reveal subdomains of each that contribute to deglycosylation.Analytical characterization of IgG Fc subclass variants through high-resolution separation combined with multiple LC-MS identification.Advanced analyses of kinetic stabilities of iggs modified by mutations and glycosylation Lysine conjugation properties in human IgGs studied by integrating high-resolution native mass spectrometry and bottom-up proteomics.Two-faced Fcab prevents polymerization with VEGF and reveals thermodynamics and the 2.15 Å crystal structure of the complex.Effects of N-Glycan Composition on Structure and Dynamics of IgG1 Fc and Their Implications for Antibody Engineering.Physical stability comparisons of IgG1-Fc variants: effects of N-glycosylation site occupancy and Asp/Gln residues at site Asn 297.Increased in vivo effector function of human IgG4 isotype antibodies through afucosylation.Reply to Crispin et al.: Molecular model that accounts for the biological and physical properties of sialylated Fc.Crystallizable Fragment Glycoengineering for Therapeutic Antibodies Development.Structural characterization of the Man5 glycoform of human IgG3 Fc.Higher-order structural interrogation of antibodies using middle-down hydrogen/deuterium exchange mass spectrometry.Changes in N-glycans of IgG4 and its relationship with the existence of hypocomplementemia and individual organ involvement in patients with IgG4-related disease.

P2860

Q26823205-BF26AC7C-C962-4732-A924-540699FBDB09 Q26827579-01A4F4B7-5559-4C9E-B9E3-8D1E3F956484 Q27673777-8BC82B17-2933-4460-9EBC-3CDF15501960 Q27678488-FD9FA674-CF2D-4B6A-9343-8BE5915A8580 Q27678524-B43199B0-CE48-4FBB-BA71-194ED1E77DB5 Q27681704-A2702286-EAE1-4FD0-ABED-CBC6FD2ADD55 Q27684440-A6AAFC1E-E199-453E-9844-2B454D2BE678 Q28079016-2AE90F0B-F94A-4197-AAEF-AC89D3DE203C Q30675226-9EE2B54F-CF1A-4A06-9755-B6B6F22110F8 Q35886917-1EFA6968-1812-4E20-BEA8-F4CF7816C2C6 Q36021825-2E84C206-5DD6-48FA-970A-B443C6594514 Q36742404-B4C3E770-3BBC-46D0-B051-6956A935E4D1 Q36855617-78607394-B76C-461F-942B-2950AB658352 Q36932153-6E9FFDDE-AB6F-4EDD-9F03-02126C899B87 Q36950457-D5EFA6CD-6AA6-4DFA-A33F-AE3F9840F99A Q37496563-48582B22-8E31-49F7-8DD4-B9E285FB4A89 Q37589825-2DACEB84-683C-442F-A427-9D38249996EE Q38232105-5DDE371D-5F81-4732-8602-FAD0B1E37A19 Q38615357-A52EB1F0-9119-4FA2-A8F5-1B44178384B7 Q38615376-AF775E70-DA19-46C5-8DC9-840A0AB6FA29 Q38730371-853DD38A-7BB5-4F7D-88A2-18B8F8A3B2D7 Q38883267-24CF7C64-45D0-443C-8D33-57868317D39D Q38927751-20A23384-2E56-4ADF-86DF-5176014BC14E Q39037824-284A9A07-E4F1-465F-8D28-409BFF5E62F8 Q39088502-2F07133A-3588-4226-9E86-F655A5EEC755 Q39361301-EF5209D5-7568-492D-A531-064DAD6FC420 Q39401108-EFEF2A35-A6F6-4C9B-868F-AAD5318FEAB5 Q39661732-8D294A49-6A51-492C-B388-2B91E5337228 Q40672146-4369E11E-126C-4DF0-AB2C-5BEB9F890AC3 Q41366211-E61C44EB-4B6D-4CB0-B741-17C0E5E301D2 Q41495558-40091E72-F824-405E-966F-FB92CB656A2B Q42075218-951CA0B4-041F-40E4-B99C-E9DEF6E2EAD1 Q42171615-16CC6A8A-63EA-4C90-AE71-6C615BCCEAC0 Q42381251-1EC57810-B708-43A3-ACE5-031D76EE79F5 Q42390676-48DACE84-6F65-4614-AE7A-BF1D75FED1A7 Q42971141-2064FE60-E48D-4CC5-A2A6-CF26E65D42CB Q44852748-827B9C21-20EF-49B2-8B63-91F2C458B0A3 Q47445247-2CFF81D0-E134-4BB1-AA50-C68F8F21A2FF Q55335781-4A35A978-7A4B-4128-B2BC-22398B58E338 Q55510375-B5AD00D9-FE9E-4335-8CCD-A874F73759B6

P2860

Revisiting the role of glycosylation in the structure of human IgG Fc.

http://www.wikidata.org/entity/Q36252642

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

Revisiting the role of glycosylation in the structure of human IgG Fc.

@ast

Revisiting the role of glycosylation in the structure of human IgG Fc.

@en

type

label

Revisiting the role of glycosylation in the structure of human IgG Fc.

@ast

Revisiting the role of glycosylation in the structure of human IgG Fc.

@en

prefLabel

Revisiting the role of glycosylation in the structure of human IgG Fc.

@ast

Revisiting the role of glycosylation in the structure of human IgG Fc.

@en

P1433

Q36252642-A2523009-D4C5-4421-82F4-02B4538AFFB8

P1476

Q36252642-30006EE6-2E4C-4437-83E3-63589468CA99

P2093

Q36252642-6228C861-F35C-4757-9610-D4EE0E9CF520

Q36252642-865DF68C-9909-496A-A19E-7C869DDC426E

Q36252642-9D3CEED1-4050-495B-AFA3-1925C6E2427B

Q36252642-C58B61A6-4648-458E-AAE2-59349AFB04C9

Q36252642-EEAB2DED-466B-421B-B7B1-6AA613EA2462

P2860

Q36252642-048D8DBD-897E-4FB5-9B65-B3C340E0698F

Q36252642-0598C26E-718F-445A-8856-D44CEA699DD2

Q36252642-09FE9FCC-D54D-43B2-A1F0-A134C6CFDB0A

Q36252642-11EAA5FB-F683-4D84-B6E0-00F6346261D4

Q36252642-16A4A018-331C-4C17-83CA-1DBB3CBA5549

Q36252642-2082AA1D-B30C-4418-9BE1-D28CD66AB3C6

Q36252642-23753707-7FFB-482B-A2DE-EB3B53E9927F

Q36252642-26300266-CFFC-4B9C-956C-067D059D592D

Q36252642-272BEF72-CC35-433E-8474-53868D2F9B80

Q36252642-304350B5-773F-4FFA-876C-ABF7F3C6EEB2

P304

Q36252642-C6C86281-F0BF-451E-9AF9-F8DE2F1883BE

P31

Q36252642-A805FE52-FBBB-430C-9ADA-459B968D499D

P356

Q36252642-B34F1FB9-FBA9-4E1A-B647-DD40E7C45B15

P433

Q36252642-42AB3BA6-CE4C-4CA4-8907-5DEF047577DD

P478

Q36252642-1E17A11E-1958-449B-ABE4-E63A47EA6522

P577

Q36252642-77F83003-3B33-4948-89D2-D535A4C42915

P5875

Q36252642-038FDEB4-1B38-4F9F-9DBE-8A3086E06A0F

P698

Q36252642-B9FAD5D6-EBBA-4290-A6D6-E4033AEBD5E0

P921

Q36252642-89651B4C-DBE7-43AE-89E3-6FDD18BF35F9

P932

Q36252642-FC6BD37E-247C-4DD5-B1A3-438CC478F909

P356

P1433

ACS Chemical Biology

P1476

Revisiting the role of glycosylation in the structure of human IgG Fc.

@en

P2093

Arthur F Monzingo

http://www.w3.org/2001/XMLSchema#string

George Georgiou

http://www.w3.org/2001/XMLSchema#string

M Jack Borrok

http://www.w3.org/2001/XMLSchema#string

Sang Taek Jung

http://www.w3.org/2001/XMLSchema#string

Tae Hyun Kang

http://www.w3.org/2001/XMLSchema#string

P2860

Role of oligosaccharide residues of IgG1-Fc in Fc gamma RIIb binding

Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing

The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex

Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design

Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity

Structural comparison of fucosylated and nonfucosylated Fc fragments of human immunoglobulin G1

Structural characterization of a mutated, ADCC-enhanced human Fc fragment

Structure of an isolated unglycosylated antibody CH2 domain

Structure-based design of a periplasmic binding protein antagonist that prevents domain closure

Structure of the murine unglycosylated IgG1 Fc fragment

P304

1596-1602

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/CB300130K

http://www.w3.org/2001/XMLSchema#string

P433

9

http://www.w3.org/2001/XMLSchema#string

P478

7

http://www.w3.org/2001/XMLSchema#string

P577

2012-07-10T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

228099163

http://www.w3.org/2001/XMLSchema#string

P698

22747430

http://www.w3.org/2001/XMLSchema#string

P921

P932

3448853

http://www.w3.org/2001/XMLSchema#string