Complement is activated by IgG hexamers assembled at the cell surface.
about
Engineered IgG1-Fc--one fragment to bind them allMonoclonal antibodies targeting CD38 in hematological malignancies and beyondComplement inhibitors to treat IgM-mediated autoimmune hemolysisHuman IgG4: a structural perspectiveThe perfect storm: HLA antibodies, complement, FcγRs, and endothelium in transplant rejectionCrystal structure of deglycosylated human IgG4-FcThe diverse and expanding role of mass spectrometry in structural and molecular biologyThe Complement System and Antibody-Mediated Transplant RejectionGlobal shape and ligand binding efficiency of the HIV-1-neutralizing antibodies differ from those of antibodies that cannot neutralize HIV-1Leporid immunoglobulin G shows evidence of strong selective pressure on the hinge and CH3 domainsAntibodies That Efficiently Form Hexamers upon Antigen Binding Can Induce Complement-Dependent Cytotoxicity under Complement-Limiting Conditions.CODV-Ig, a universal bispecific tetravalent and multifunctional immunoglobulin format for medical applications.Human IgG is produced in a pro-form that requires clipping of C-terminal lysines for maximal complement activationThe Humoral Theory of Transplantation: Epitope Analysis and the Pathogenicity of HLA Antibodies.Deciphering the fine details of c1 assembly and activation mechanisms: "mission impossible"?Developing the IVIG biomimetic, hexa-Fc, for drug and vaccine applicationsMolecules Great and Small: The Complement System.Complement in disease: a defence system turning offensiveImpact of serum immunoglobulins level and IL-18 promoter gene polymorphism among Egyptian patients with idiopathic thrombocytopenic purpura.Human IgG3 with extended half-life does not improve Fc-gamma receptor-mediated cancer antibody therapies in miceTechnical Limitations of the C1q Single-Antigen Bead Assay to Detect Complement Binding HLA-Specific Antibodies.Fc-Galactosylation of Human Immunoglobulin Gamma Isotypes Improves C1q Binding and Enhances Complement-Dependent CytotoxicityImpact of Antigen Density on the Binding Mechanism of IgG AntibodiesInhibition of the classical pathway of complement by meningococcal capsular polysaccharidesIgG subclasses and allotypes: from structure to effector functions.Complement System Part I - Molecular Mechanisms of Activation and Regulation.Detection of C3d-binding donor-specific anti-HLA antibodies at diagnosis of humoral rejection predicts renal graft loss.The solution structures of two human IgG1 antibodies show conformational stability and accommodate their C1q and FcγR ligands.Prospects for engineering HIV-specific antibodies for enhanced effector function and half-life.Recent advances in renal transplantation: antibody-mediated rejection takes center stageSimultaneous determination of sample thickness, tilt, and electron mean free path using tomographic tilt images based on Beer-Lambert law.A Novel Platform for the Potentiation of Therapeutic Antibodies Based on Antigen-Dependent Formation of IgG Hexamers at the Cell Surface.Antibody Engineering & Therapeutics, the annual meeting of The Antibody Society December 7-10, 2015, San Diego, CA, USA.Cross-reactive and pre-existing antibodies to therapeutic antibodies--Effects on treatment and immunogenicity.An Anti-C1s Monoclonal, TNT003, Inhibits Complement Activation Induced by Antibodies Against HLAComplement activation, regulation, and molecular basis for complement-related diseasesExpression of factor H binding protein in meningococcal strains can vary at least 15-fold and is genetically determined.Complement inhibition prevents oncolytic vaccinia virus neutralization in immune humans and cynomolgus macaquesPre-exposure Prophylaxis With OspA-Specific Human Monoclonal Antibodies Protects Mice Against Tick Transmission of Lyme Disease Spirochetes.The role of Fc receptors in HIV prevention and therapy.
P2860
Q26766715-CDA6A1E7-E48D-4780-B578-91924FA9C25FQ26766718-55231857-2A05-4CA1-BD86-2AF621DD1490Q26777628-24F371FD-C47B-4455-93C9-4956A3FBC6CEQ26779758-42EE3F92-0304-4B09-9CE2-4E81C4448540Q26862195-40C05AB3-85E9-41FA-B3BB-F69028729063Q27684440-C9E647D3-995E-464E-A62A-6143D5836853Q28080243-081DEDAD-626A-46A2-9A0D-3B561BBE02C2Q28087773-4F75B329-D081-489E-81EF-853AB1EC13E8Q28250040-718D6A91-6054-4037-90CD-242C52F66709Q28655035-5CD45BCE-9CD8-47CC-B183-8E1476B18500Q30276243-98CDCB14-1013-4DC2-8D0F-97F6B0A631E1Q30360904-96EC80DF-2C61-445B-9E89-80E38C989B4AQ30360964-A38925D3-4398-4A00-BAD2-BD711F29B18BQ30397251-C88E132B-0CE0-459D-BCEF-955E51E3124EQ30596999-7FBBE830-27EC-4E2D-97B2-5D768C232604Q30834514-67527CA0-F4F9-4454-9A91-2967D0C77582Q33419651-43BF94D0-7D24-4F4A-B961-6303EA3C8451Q33432423-5EF938AE-B093-413E-A6E0-CBB95B8085CBQ33435188-7E34FDD0-3830-4705-8492-AD595C3E1802Q33707941-39842318-E713-472B-BB26-7F5A8A115F0BQ33760357-2F193560-C16D-4663-95E2-6FBDFE8137D4Q33766365-0027EF1F-88E5-41DD-B544-A9509AEAB513Q33812798-98CD05AB-7D0C-4058-9BDD-335E4DD233C4Q33992223-464E1DC3-23CD-4DE3-985F-090DA1E2DB6DQ34368678-8EEB9D55-9C96-45A4-B95F-B933C0E4B1F0Q34481071-4B0EB98C-9A6C-4C13-9966-1EB22223F9B5Q35027253-4A82C0DF-C48F-456D-8A9B-05874734EF84Q35221593-16274BB2-E815-4653-ADFB-76AB6ECA7267Q35569901-F44C452D-EB44-4EEA-99EF-BF4436C36D3CQ35659332-328A2788-7888-4DF8-87FA-61021B7D651DQ35798092-3B2EAD06-94D8-4F5E-9B0E-CDA16D7DFDF2Q35886917-6877948F-8BD3-4F64-84F2-4B504FE14912Q35933820-F6377A4D-813D-492B-AD1E-9231900327BBQ36214720-33C9283A-E0B2-4EF8-8B20-7E72E59343C3Q36302476-173E0772-EE0B-49C9-9ECC-4EEF4C969C91Q36380682-7656FAE8-6077-48F7-80DC-726624EA2898Q36684761-7CFD78A8-D656-4255-BE01-BBCB9FE00C52Q36756690-16C8F0FB-4FB9-4A1A-8622-FFC3F5A841F6Q37033087-9DB6AF79-E197-4A38-BCCD-B8A200CB96A2Q37113972-232CAB9F-8F0F-4273-91B6-3E3D22D56F1A
P2860
Complement is activated by IgG hexamers assembled at the cell surface.
description
2014 nî lūn-bûn
@nan
2014 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի մարտին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Complement is activated by IgG hexamers assembled at the cell surface.
@ast
Complement is activated by IgG hexamers assembled at the cell surface.
@en
type
label
Complement is activated by IgG hexamers assembled at the cell surface.
@ast
Complement is activated by IgG hexamers assembled at the cell surface.
@en
prefLabel
Complement is activated by IgG hexamers assembled at the cell surface.
@ast
Complement is activated by IgG hexamers assembled at the cell surface.
@en
P2093
P2860
P50
P356
P1433
P1476
Complement is activated by IgG hexamers assembled at the cell surface.
@en
P2093
Deniz Ugurlar
Dennis R Burton
Frank J Beurskens
Jan G J van de Winkel
Janine Schuurman
Kristin Strumane
Margaret A Lindorfer
Marleen Voorhorst
Ronald P Taylor
P2860
P304
P356
10.1126/SCIENCE.1248943
P407
P50
P577
2014-03-01T00:00:00Z