Literature DB >> 8527837

Inhibitors of protein tyrosine kinases.

D W Fry1, A J Bridges.   

Abstract

The description in the past year of several novel protein tyrosine kinase inhibitors, which exhibit dramatic improvements in potency and specificity over earlier agents, will be considered a major turning point in the field. These compounds appear to have the necessary pharmacological properties to finally allow clarification of whether suppression of specific tyrosine kinases is of therapeutic benefit in certain disease states.

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Year:  1995        PMID: 8527837     DOI: 10.1016/0958-1669(95)80109-x

Source DB:  PubMed          Journal:  Curr Opin Biotechnol        ISSN: 0958-1669            Impact factor:   9.740


  3 in total

1.  Protein phosphorylation during coconut zygotic embryo development

Authors: 
Journal:  Plant Physiol       Date:  1998-09       Impact factor: 8.340

2.  The structure of mitogen-activated protein kinase p38 at 2.1-A resolution.

Authors:  Z Wang; P C Harkins; R J Ulevitch; J Han; M H Cobb; E J Goldsmith
Journal:  Proc Natl Acad Sci U S A       Date:  1997-03-18       Impact factor: 11.205

3.  Specific, irreversible inactivation of the epidermal growth factor receptor and erbB2, by a new class of tyrosine kinase inhibitor.

Authors:  D W Fry; A J Bridges; W A Denny; A Doherty; K D Greis; J L Hicks; K E Hook; P R Keller; W R Leopold; J A Loo; D J McNamara; J M Nelson; V Sherwood; J B Smaill; S Trumpp-Kallmeyer; E M Dobrusin
Journal:  Proc Natl Acad Sci U S A       Date:  1998-09-29       Impact factor: 11.205

  3 in total

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