The human intermediate-affinity interleukin 2 receptor consists of two distinct, partially homologous glycoproteins (Q44491218)

3 December 2017

title

The human intermediate-affinity interleukin 2 receptor consists of two distinct, partially homologous glycoproteins (English)

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3 December 2017

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3 December 2017

Diamantstein T

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3 December 2017

language of work or name

English

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publication date

1 July 1988

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European Journal of Immunology

3 December 2017

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inferred from page(s)

published in

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3 December 2017

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3 December 2017

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3 December 2017

page(s)

1051-1057

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The mouse high affinity IL 2 receptor complex. I. Evidence for a third molecule, the putative gamma-chain, associated with the alpha- and/or beta-chain of the receptor

3 December 2017

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Interleukin 2 high-affinity receptor expression requires two distinct binding proteins

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Interleukin 2 binding molecule distinct from the Tac protein: analysis of its role in formation of high-affinity receptors

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A second human interleukin-2 binding protein that may be a component of high-affinity interleukin-2 receptors

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Internalization of interleukin 2 is mediated by the beta chain of the high-affinity interleukin 2 receptor

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The two-chain structure of high-affinity IL-2 receptors

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Novel interleukin-2 receptor subunit detected by cross-linking under high-affinity conditions

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Expression of functional interleukin-2 receptors in human light chain/Tac ransgenic mice

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Low and high affinity cellular receptors for interleukin 2. Implications for the level of Tac antigen

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N-hydroxysulfosuccinimide active esters: bis(N-hydroxysulfosuccinimide) esters of two dicarboxylic acids are hydrophilic, membrane-impermeant, protein cross-linkers

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Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F.

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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16 Peptide mapping in one dimension by limited proteolysis of sodium dodecyl sulfate-solubilized proteins

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Characterization of the human receptor for T-cell growth factor

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Identifiers

DOI

10.1002/EJI.1830180713

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3 December 2017

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