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Definition and spatial location of mouse interleukin-2 residues that interact with its heterotrimeric receptorThe structure of granulocyte-colony-stimulating factor and its relationship to other growth factorsStructure of the active core of human stem cell factor and analysis of binding to its receptor KitBinding of small molecules to an adaptive protein-protein interfaceSmall-molecule inhibitors of protein-protein interactions: progressing towards the dreamBuffalo (Bubalus bubalis) interleukin-2: sequence analysis reveals high nucleotide and amino acid identity with interleukin-2 of cattle and other ruminants.Specific human granulocyte-macrophage colony-stimulating factor antagonists.Nitric oxide and thiol redox regulation of Janus kinase activityIdentification of a direct interaction between interleukin 2 and the p64 interleukin 2 receptor gamma chain.Saturation mutagenesis of the human interleukin 6 receptor-binding site: implications for its three-dimensional structure.Homology modelling and 1H NMR studies of human leukaemia inhibitory factor.Folding and Purification of Insoluble (Inclusion Body) Proteins from Escherichia coli.Receptors for interleukin-13 and interleukin-4 are complex and share a novel component that functions in signal transductionComputational solvent mapping in structure-based drug design.Generation of interleukin-6 receptor antagonists by molecular-modeling guided mutagenesis of residues important for gp130 activation.Two distinct functional sites of human interleukin 4 are identified by variants impaired in either receptor binding or receptor activation.Predicting the conformation of proteins. Man versus machine.Receptor binding properties of four-helix-bundle growth factors deduced from electrostatic analysis.An interleukin 4 (IL-4) mutant protein inhibits both IL-4 or IL-13-induced human immunoglobulin G4 (IgG4) and IgE synthesis and B cell proliferation: support for a common component shared by IL-4 and IL-13 receptorsBalancing target flexibility and target denaturation in computational fragment-based inhibitor discovery.NMR characterization of interleukin-2 in complexes with the IL-2Ralpha receptor component, and with low molecular weight compounds that inhibit the IL-2/IL-Ralpha interaction.Rational design of a mouse granulocyte macrophage-colony-stimulating factor receptor antagonist.Insufficient (sub-native) helix content in soluble/solid aggregates of recombinant and engineered forms of IL-2 throws light on how aggregated IL-2 is biologically active.Folding and purification of insoluble (inclusion body) proteins from Escherichia coli.
P2860
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P2860
description
1992 nî lūn-bûn
@nan
1992 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Response.
@nl
type
label
Response.
@nl
prefLabel
Response.
@nl
P1433
P1476
Response
@en
P2093
P356
10.1126/SCIENCE.257.5068.412
P407
P577
1992-07-17T00:00:00Z