An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation - Wikidata - wikimedia - TriplyDB

An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation

An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation

http://www.wikidata.org/entity/Q27765986

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The human interleukin-6 (IL-6) receptor exists as a preformed dimer in the plasma membrane Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system Topological requirements and signaling properties of T cell-activating, anti-CD28 antibody superagonists A common model for cytokine receptor activation: combined scissor-like rotation and self-rotation of receptor dimer induced by class I cytokine Atomic structure of the GCSF-receptor complex showing a new cytokine-receptor recognition scheme Crystal structure of human cytomegalovirus IL-10 bound to soluble human IL-10R1.Evidence for plasticity and structural mimicry at the immunoglobulin light chain-protein L interface Structural Organization of a Full-Length gp130/LIF-R Cytokine Receptor Transmembrane Complex Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21 Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation Immunoglobulin Fc Heterodimer Platform Technology: From Design to Applications in Therapeutic Antibodies and Proteins Shared and unique determinants of the erythropoietin (EPO) receptor are important for binding EPO and EPO mimetic peptide Disabling of receptor activator of nuclear factor-kappaB (RANK) receptor complex by novel osteoprotegerin-like peptidomimetics restores bone loss in vivo A new agonist of the erythropoietin receptor, Epobis, induces neurite outgrowth and promotes neuronal survival Phage display of random peptide libraries: applications, limits, and potential.Exploring protein-protein interactions with phage display.The SCHOOL of nature: I. Transmembrane signaling.A ligand peptide motif selected from a cancer patient is a receptor-interacting site within human interleukin-11.Construction and genetic selection of small transmembrane proteins that activate the human erythropoietin receptor.Loss of Forkhead box M1 promotes erythropoiesis through increased proliferation of erythroid progenitors.Insulin receptor activation with transmembrane domain ligands.Selection of antibodies that regulate phenotype from intracellular combinatorial antibody libraries.HER2/neu: mechanisms of dimerization/oligomerization.Contribution of the Box 1 and Box 2 motifs of cytokine receptors to Jak1 association and activation.Nerve growth factor signals via preexisting TrkA receptor oligomers Evidence for ligand-independent multimerization of the IL-17 receptor.Mechanism of activation of protein kinase JAK2 by the growth hormone receptor.Diversity-oriented approaches for interrogating T-cell receptor repertoire, ligand recognition, and function The SCHOOL of nature: III. From mechanistic understanding to novel therapies Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase.Thrombopoietin receptor activation: transmembrane helix dimerization, rotation, and allosteric modulation A novel EPO receptor agonist improves glucose tolerance via glucose uptake in skeletal muscle in a mouse model of diabetes A point mutation in the extracellular domain of KIT promotes tumorigenesis of mast cells via ligand-independent auto-dimerization Emerging EPO and EPO receptor regulators and signal transducers.Nonnatural protein-protein interaction-pair design by key residues grafting.Mechanistic diversity of cytokine receptor signaling across cell membranes.GDF-5 can act as a context-dependent BMP-2 antagonist.The molecular basis of IL-10 function: from receptor structure to the onset of signaling.Macromolecular docking of a three-body system: the recognition of human growth hormone by its receptor Understanding cytokine and growth factor receptor activation mechanisms.

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P2860

An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation

http://www.wikidata.org/entity/Q27765986

description

1998 nî lūn-bûn

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1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի նոյեմբերին հրատարակված գիտական հոդված

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1998年の論文

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1998年学术文章

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1998年学术文章

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1998年学术文章

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name

An antagonist peptide-EPO rece ...... not sufficient for activation

@ast

An antagonist peptide-EPO rece ...... not sufficient for activation

@en

An antagonist peptide-EPO rece ...... not sufficient for activation

@nl

type

label

An antagonist peptide-EPO rece ...... not sufficient for activation

@ast

An antagonist peptide-EPO rece ...... not sufficient for activation

@en

An antagonist peptide-EPO rece ...... not sufficient for activation

@nl

prefLabel

An antagonist peptide-EPO rece ...... not sufficient for activation

@ast

An antagonist peptide-EPO rece ...... not sufficient for activation

@en

An antagonist peptide-EPO rece ...... not sufficient for activation

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Nature structural biology

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An antagonist peptide-EPO rece ...... not sufficient for activation

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P2093

C D Krause

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

D L Johnson

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

F P Barbone

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

F X Farrell

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I A Wilson

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K D Liu

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L K Jolliffe

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M A Goldsmith

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O Livnah

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S Pestka

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P2860

Efficiency of signalling through cytokine receptors depends critically on receptor orientation

Identification and sequence of an accessory factor required for activation of the human interferon gamma receptor

PROCHECK: a program to check the stereochemical quality of protein structures

Processing of X-ray diffraction data collected in oscillation mode

NMR structure of human erythropoietin and a comparison with its receptor bound conformation

Interaction between the components of the interferon gamma receptor complex

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993-1004

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3103261

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10.1038/2965

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11

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5

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13478588

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9808045

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