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David Cowburn

Researcher at Albert Einstein College of Medicine

Publications -  223
Citations -  12923

David Cowburn is an academic researcher from Albert Einstein College of Medicine. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & SH3 domain. The author has an hindex of 55, co-authored 218 publications receiving 12386 citations. Previous affiliations of David Cowburn include National Institutes of Health & VU University Amsterdam.

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Accurate quantitation of protein expression and site-specific phosphorylation

TL;DR: The present method is general and affords a quantitative description of cellular differences at the level of protein expression and modification, thus providing information that is critical to the understanding of complex biological phenomena.
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Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions.

TL;DR: It is reported here that the inactive Stat91 in the cytoplasm of untreated cells is a monomer and that upon IFN-gamma-induced phosphorylation it forms a stable homodimer.
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Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms

TL;DR: The crystal structure of the Src SH2 domain complexed with a high affinity 11-residue phosphopeptide has been determined at 2.7 A resolution by X-ray diffraction, and comparison with the structure with the high affinity complex reveals only localized and relatively small changes.
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Modular peptide recognition domains in eukaryotic signaling.

TL;DR: The structural bases of the specificities of recognition by SH2, SH3, and PTB domains have been elucidated by X-ray crystallography and NMR, and the mechanism of cooperative interactions between these domains is discussed.