P. Hu

发表

Vav: A potential link between tyrosine kinases and Ras‐like GTPases in hematopoietic cell signaling

B. Margolis, J. Schlessinger, P. Hu, 1993, BioEssays : news and reviews in molecular, cellular and developmental biology.

Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs

A. Ullrich, B. Margolis, J. Schlessinger, 1992, Nature.

The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors

J. Schlessinger, E. Skolnik, A. Ullrich, 1992 .

The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors

A. Ullrich, J. Schlessinger, E. Skolnik, 1992, Molecular and cellular biology.

Direct association of p110 beta phosphatidylinositol 3-kinase with p85 is mediated by an N-terminal fragment of p110 beta

J. Schlessinger, P. Hu, 1994, Molecular and cellular biology.

Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85

J. Schlessinger, A. Mondino, E. Skolnik, 1993 .

Phosphatidylinositol 3-kinase mediates epidermal growth factor-induced activation of the c-Jun N-terminal kinase signaling pathway

J. Schlessinger, S. Logan, M. Falasca, 1997, Molecular and cellular biology.

TheSH2andSH3Domain-Containing NckProtein Is Oncogenic andaCommonTarget forPhosphorylation byDifferent Surface Receptors

A. Ullrich, A. Schlessinger, E. Skolnik, 1992 .

Phosphatidylinositol 3′‐kinase is activated by association with IRS‐1 during insulin stimulation.

B. Margolis, M. White, J. Schlessinger, 1992, The EMBO journal.

Phosphatidylinositol 3-kinase p85 SH2 domain specificity defined by direct phosphopeptide/SH2 domain binding.

J. Schlessinger, S. Shoelson, M. Chaudhuri, 1993, Biochemistry.

SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange

J Ureña, A. Ullrich, M. White, 1993, Molecular and cellular biology.

IRS-1 activates phosphatidylinositol 3'-kinase by associating with src homology 2 domains of p85.

M. White, J. Schlessinger, S. Shoelson, 1992, Proceedings of the National Academy of Sciences of the United States of America.

Interaction of phosphatidylinositol 3-kinase-associated p85 with epidermal growth factor and platelet-derived growth factor receptors

A. Ullrich, B. Margolis, J. Schlessinger, 1992, Molecular and cellular biology.

Point mutation in the fibroblast growth factor receptor eliminates phosphatidylinositol hydrolysis without affecting neuronal differentiation of PC12 cells.

M. Jaye, I. Lax, J. Schlessinger, 1994, The Journal of biological chemistry.

Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85

J. Schlessinger, A. Mondino, E. Skolnik, 1993, Molecular and cellular biology.

Specific phosphopeptide binding regulates a conformational change in the PI 3‐kinase SH2 domain associated with enzyme activation.

J. Schlessinger, S. Shoelson, M. Weiss, 1993, The EMBO journal.