Amino acid sequence and post-translational modification of human interleukin 2.
about
Cloning, sequence, and expression of bovine interleukin 2Identification of specific residues of human interleukin 2 that affect binding to the 70-kDa subunit (p70) of the interleukin 2 receptor.The first alpha helix of interleukin (IL)-2 folds as a homotetramer, acts as an agonist of the IL-2 receptor beta chain, and induces lymphokine-activated killer cellsSequence analysis of carcinoembryonic antigen: identification of glycosylation sites and homology with the immunoglobulin supergene familyGlycoproteomics: past, present and future.Design, synthesis and expression of a human interleukin-2 gene incorporating the codon usage bias found in highly expressed Escherichia coli genes.Modification and secretion of human interleukin 2 produced in insect cells by a baculovirus expression vector.Folding and Purification of Insoluble (Inclusion Body) Proteins from Escherichia coli.Structural analysis and modeling of a synthetic interleukin-2 mimetic and its interleukin-2Rbeta2 receptor.Intermolecular cystine-bonding of murine interleukin 2 indicates that ligand dimerization is important for the formation of the high-affinity receptor complex.Amino acid distributions around O-linked glycosylation sites.Purification and renaturation of recombinant human interleukin-2.Size polymorphisms due to changes in the number of O-glycosylated tandem repeats in the Dictyostelium discoideum glycoprotein PsA.Prediction of O-glycosylation of mammalian proteins: specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferaseIdentification of a human non-interferon lymphokine activating monocyte complement biosynthesis.Characterization of recombinant glycosylated human interleukin 2 produced by a recombinant plasmid transformed CHO cell line.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.The isolation and sequence of canine interleukin-2.Prediction of mucin-type O-glycosylation sites by a two-staged strategy.Folding and purification of insoluble (inclusion body) proteins from Escherichia coli.Improving Immunotherapy Through Glycodesign
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P2860
Amino acid sequence and post-translational modification of human interleukin 2.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on October 1984
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Amino acid sequence and post-translational modification of human interleukin 2.
@en
Amino acid sequence and post-translational modification of human interleukin 2.
@nl
type
label
Amino acid sequence and post-translational modification of human interleukin 2.
@en
Amino acid sequence and post-translational modification of human interleukin 2.
@nl
prefLabel
Amino acid sequence and post-translational modification of human interleukin 2.
@en
Amino acid sequence and post-translational modification of human interleukin 2.
@nl
P2093
P2860
P356
P1476
Amino acid sequence and post-translational modification of human interleukin 2.
@en
P2093
P2860
P304
P356
10.1073/PNAS.81.20.6486
P407
P577
1984-10-01T00:00:00Z