A lock on phosphotyrosine signaling

Kathryn E. Muratore; Philip A. Cole

doi:10.1021/cb7001285

A lock on phosphotyrosine signaling

Kathryn E. Muratore, Philip A. Cole

School of Medicine

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

Protein phosphorylation plays a major role in cell signaling and human disease, so understanding the effects of tyrosine phosphorylation on protein structure and function is an area of intense investigation. A new technique allows site-specific incorporation of a nonhydrolyzable phosphotyrosine analogue into recombinant proteins, providing a new strategy for research in this important area.

Original language	English (US)
Pages (from-to)	454-456
Number of pages	3
Journal	ACS chemical biology
Volume	2
Issue number	7
DOIs	https://doi.org/10.1021/cb7001285
State	Published - Jul 2007

ASJC Scopus subject areas

Biochemistry
Molecular Medicine

Access to Document

10.1021/cb7001285

Cite this

@article{39e1216570f64404b4c7fd46833cbe68,

title = "A lock on phosphotyrosine signaling",

abstract = "Protein phosphorylation plays a major role in cell signaling and human disease, so understanding the effects of tyrosine phosphorylation on protein structure and function is an area of intense investigation. A new technique allows site-specific incorporation of a nonhydrolyzable phosphotyrosine analogue into recombinant proteins, providing a new strategy for research in this important area.",

author = "Muratore, {Kathryn E.} and Cole, {Philip A.}",

year = "2007",

month = jul,

doi = "10.1021/cb7001285",

language = "English (US)",

volume = "2",

pages = "454--456",

journal = "ACS chemical biology",

issn = "1554-8929",

publisher = "American Chemical Society",

number = "7",

}

TY - JOUR

T1 - A lock on phosphotyrosine signaling

AU - Muratore, Kathryn E.

AU - Cole, Philip A.

PY - 2007/7

Y1 - 2007/7

N2 - Protein phosphorylation plays a major role in cell signaling and human disease, so understanding the effects of tyrosine phosphorylation on protein structure and function is an area of intense investigation. A new technique allows site-specific incorporation of a nonhydrolyzable phosphotyrosine analogue into recombinant proteins, providing a new strategy for research in this important area.

AB - Protein phosphorylation plays a major role in cell signaling and human disease, so understanding the effects of tyrosine phosphorylation on protein structure and function is an area of intense investigation. A new technique allows site-specific incorporation of a nonhydrolyzable phosphotyrosine analogue into recombinant proteins, providing a new strategy for research in this important area.

UR - http://www.scopus.com/inward/record.url?scp=34548619123&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34548619123&partnerID=8YFLogxK

U2 - 10.1021/cb7001285

DO - 10.1021/cb7001285

M3 - Article

C2 - 17649969

AN - SCOPUS:34548619123

SN - 1554-8929

VL - 2

SP - 454

EP - 456

JO - ACS chemical biology

JF - ACS chemical biology

IS - 7

ER -

A lock on phosphotyrosine signaling

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this