A kinetic intermediate in the reaction of an antigenic peptide and I-Ek.
about
A step-by-step overview of the dynamic process of epitope selection by major histocompatibility complex class II for presentation to helper T cellsExploration of the P6/P7 region of the peptide-binding site of the human class II major histocompatability complex protein HLA-DR1Structural features of the invariant chain fragment CLIP controlling rapid release from HLA-DR molecules and inhibition of peptide bindingGene Expression Driven by a Strong Viral Promoter in MVA Increases Vaccination Efficiency by Enhancing Antibody Responses and Unmasking CD8⁺ T Cell EpitopesRefolding and reassembly of separate alpha and beta chains of class II molecules of the major histocompatibility complex leads to increased peptide-binding capacity.The invariant chain forms complexes with class II major histocompatibility complex molecules and antigenic peptides "in vivo".Peptide binding to HLA-DR1: a peptide with most residues substituted to alanine retains MHC binding.The kinetic basis of peptide exchange catalysis by HLA-DMHarden M. McConnell: The Science Speaks for Itself.Interpretation of biphasic dissociation kinetics for isomeric class II major histocompatibility complex-peptide complexes.For many but not for all: how the conformational flexibility of the peptide/MHCII complex shapes epitope selectionHLA-DM targets the hydrogen bond between the histidine at position beta81 and peptide to dissociate HLA-DR-peptide complexes.Binding interactions between peptides and proteins of the class II major histocompatibility complex.The convergent roles of tapasin and HLA-DM in antigen presentation.HLA-DO as the optimizer of epitope selection for MHC class II antigen presentation.Kinetic intermediates in the reactions between peptides and proteins of major histocompatibility complex class IIThe utility and limitations of current Web-available algorithms to predict peptides recognized by CD4 T cells in response to pathogen infectionShort-lived complexes between myelin basic protein peptides and IAkStimulation of T cells by antigenic peptide complexed with isolated chains of major histocompatibility complex class II moleculesExpression of a class II major histocompatibility complex (MHC) heterodimer in a lipid-linked form with enhanced peptide/soluble MHC complex formation at low pH.Enhanced binding of peptide antigen to purified class II major histocompatibility glycoproteins at acidic pH.Biochemical evidence for the rapid assembly and disassembly of processed antigen-major histocompatibility complex class II complexes in acidic vesicles of B cellsRegulation of antigen presentation by acidic pH.An insulin peptide that binds an alternative site in class II major histocompatibility complex.HLA-DM recognizes the flexible conformation of major histocompatibility complex class II.Enhancement of peptide antigen presentation by a second peptide.Specific T cell recognition of kinetic isomers in the binding of peptide to class II major histocompatibility complexThe cell biology of antigen processing.Solution binding of an antigenic peptide to a major histocompatibility complex class I molecule and the role of beta 2-microglobulin.Availability of autoantigenic epitopes controls phenotype, severity, and penetrance in TCR Tg autoimmune gastritisHLA-DM mediates peptide exchange by interacting transiently and repeatedly with HLA-DR1.Kinetics of antigenic peptide binding to the class II major histocompatibility molecule I-AdSpecific binding of antigenic peptides to separate alpha and beta chains of class II molecules of the major histocompatibility complex.Conformational heterogeneity of MHC class II induced upon binding to different peptides is a key regulator in antigen presentation and epitope selection.Phospholipids enhance the binding of peptides to class II major histocompatibility moleculesCellular mechanisms of antigen processing and the function of class I and II major histocompatibility complex molecules.Identification of the lateral interaction surfaces of human histocompatibility leukocyte antigen (HLA)-DM with HLA-DR1 by formation of tethered complexes that present enhanced HLA-DM catalysisModeling Functional Motions of Biological Systems by Customized Natural Moves.Membrane interactions influence the peptide binding behavior of DR1.Single-chain recombinant HLA-DQ2.5/peptide molecules block α2-gliadin-specific pathogenic CD4+ T-cell proliferation and attenuate production of inflammatory cytokines: a potential therapy for celiac disease.
P2860
Q26747063-1FDB5AFA-6BE5-4F0D-85DC-560D6F2D4E19Q27641946-65B5D2C2-D640-4219-835F-833C73E9BCDAQ28612873-F72517E2-83F2-423E-86AD-53C3558B3EEDQ28647428-7B2762F9-73D5-4E8E-8E2C-91D33A25E103Q33606693-D0F916F4-2D45-4039-A958-287FE0FF36EDQ33796819-9C904F89-DDB3-4EF9-A5EF-D76614DFF0C3Q33920167-A8043876-87C6-4F51-9668-2DCD487B215FQ33947777-F1DAB2E7-2A1B-4C6F-935F-9FE1C1E04924Q34092147-F6B11A59-00F5-4331-BA16-FBDA4BF03EE2Q34171654-E1FBDE7D-9E88-4F98-A7B8-02149491B0FDQ34338884-4A2741CA-C930-4A88-A878-DF7C84C1A380Q34483195-F34CDED6-7FE3-481D-BCC2-C6A262DE6437Q34540061-5535DFB1-B30D-48E9-8505-5E14ABE2A2E6Q34784992-54AE7B40-A91A-4D89-9614-27B6B1D3DA16Q34948997-942F1FED-8C19-4B4F-B6FD-7A42F6F9E3D4Q35750583-6ECAC074-3D08-465B-B4B9-426764C1DED8Q35903181-3508E6E9-2799-41F7-95EB-DA9FD9B7E9F7Q35985828-8C5DC5EF-79B3-4D9D-905A-E7674B88FDACQ36117295-218412CE-7129-4468-A18B-D991E07176ACQ36230148-01CD5ADE-BDA0-4A3E-9AF9-8D341B579730Q36230523-ABA7ABE8-5A5D-4E38-98EB-8425DAA3C346Q36230883-7677BE24-B03A-48B6-A0E7-4435052F2AEBQ36351024-A1C601C7-1CD7-4DAB-A501-FC2A54BCFCA0Q36365961-043364EA-DC8D-4322-A8DE-654956BA2F56Q36404572-7FAD874D-A9B6-4697-A562-B99D41298BB5Q36554333-DAEB51C1-2F1F-43A1-A630-E7F4DE16F3BBQ36555812-F9931472-739F-4156-A059-A6139DA7E929Q36707417-5EF9BDCE-698C-427B-BCE2-0921351F4560Q36890441-8F93F179-18DD-4866-8C6D-336C581DCE12Q37267230-B563614A-0289-499F-A294-3C4678A3381EQ37345643-069F4EA6-81FB-4F81-A74B-F5E635B74A77Q37519795-0255E2D6-89CF-4066-AC75-F1C9D3F03C94Q37666665-DD234C05-4375-45ED-B50F-429820D034BAQ37672424-29FE20DB-8A18-4CFF-9CD8-862421965DB3Q37707645-B2AFEF7D-66E6-4527-9D15-D559E8A1A7E3Q37803532-D589D61C-6961-4067-93A4-9C548EDF36DBQ40718052-84F0239C-72B9-49CE-9889-ABBD1B371763Q40960143-B7E04557-2F53-48D4-B1E3-948C2C0F0F7EQ41497170-9AEDA4E4-F92B-4FE7-8425-777DA2F51F66Q41549575-4AF08501-F8EA-45AF-9414-2E5C29733360
P2860
A kinetic intermediate in the reaction of an antigenic peptide and I-Ek.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh-hant
name
A kinetic intermediate in the reaction of an antigenic peptide and I-Ek.
@en
A kinetic intermediate in the reaction of an antigenic peptide and I-Ek.
@nl
type
label
A kinetic intermediate in the reaction of an antigenic peptide and I-Ek.
@en
A kinetic intermediate in the reaction of an antigenic peptide and I-Ek.
@nl
prefLabel
A kinetic intermediate in the reaction of an antigenic peptide and I-Ek.
@en
A kinetic intermediate in the reaction of an antigenic peptide and I-Ek.
@nl
P2860
P356
P1433
P1476
A kinetic intermediate in the reaction of an antigenic peptide and I-Ek.
@en
P2093
McConnell HM
Sadegh-Nasseri S
P2860
P2888
P304
P356
10.1038/337274A0
P407
P577
1989-01-01T00:00:00Z
P5875
P6179
1006901896