(Q27740654)

2

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W Fenderson

3

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S Y Shaw

4

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K L Constantine

5

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J Naemura

6

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G Leytze

7

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R J Peach

8

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T B Lavoie

9

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L Mueller

10

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P S Linsley

Nature structural biology

11

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publication date

July 1997

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published in

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volume

4

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issue

7

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page(s)

527-31

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cites work

CTLA-4 can function as a negative regulator of T cell activation

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Differential recognition by CD28 of its cognate counter receptors CD80 (B7.1) and B70 (B7.2): analysis by site directed mutagenesis

21 April 2017

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The B7 and CD28 receptor families

21 April 2017

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Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue destruction, revealing a critical negative regulatory role of CTLA-4

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Binding stoichiometry of the cytotoxic T lymphocyte-associated molecule-4 (CTLA-4). A disulfide-linked homodimer binds two CD86 molecules

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Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations

21 January 2018

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CD28 and CTLA-4 have opposing effects on the response of T cells to stimulation

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Enhancement of antitumor immunity by CTLA-4 blockade

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Lymphoproliferative disorders with early lethality in mice deficient in Ctla-4

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Covalent dimerization of CD28/CTLA-4 and oligomerization of CD80/CD86 regulate T cell costimulatory interactions

31 March 2020

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CTLA-4 is a second receptor for the B cell activation antigen B7

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Treatment of murine lupus with CTLA4Ig

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Conformation and function of the N-linked glycan in the adhesion domain of human CD2

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Domain association in immunoglobulin molecules. The packing of variable domains

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Complementarity determining region 1 (CDR1)- and CDR3-analogous regions in CTLA-4 and CD28 determine the binding to B7-1.

31 March 2020

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Multidimensional heteronuclear nuclear magnetic resonance of proteins

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Precise vicinal coupling constants 3JHN alpha in proteins from nonlinear fits of J-modulated [15N,1H]-COSY experiments.

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Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods

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Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases

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