A. Harpur

发表

Polypeptide signalling to the nucleus through tyrosine phosphorylation of Jak and Stat proteins

Andrew Ziemiecki, James E. Darnell, Henry B. Sadowski, 1993, Nature.

The protein tyrosine kinase JAK1 complements defects in interferon-alpha/beta and -gamma signal transduction.

C. Schindler, O. Silvennoinen, G. Barbieri, 1993, Nature.

Cutting edge: KAP10, a novel transmembrane adapter protein genetically linked to DAP12 but with unique signaling properties.

Michael J. Wilson, J. Trowsdale, M. Colonna, 1999, Journal of immunology.

Tyrosine kinase JAK1 is associated with the granulocyte-colony-stimulating factor receptor and both become tyrosine-phosphorylated after receptor activation.

A. Oates, A. Wilks, A. Ziemiecki, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Class of Protein Kinase

A. Wilks, A. Ziemiecki, A. Harpur, 2003 .

Colony-stimulating factor 1-induced STAT1 and STAT3 activation is accompanied by phosphorylation of Tyk2 in macrophages and Tyk2 and JAK1 in fibroblasts.

A. Wilks, U. Novak, J. Hamilton, 1995, Blood.

Intermolecular Interactions of the p85a Regulatory Subunit of Phosphatidylinositol 3-Kinase*

G. Panayotou, M. Waterfield, M. Layton, 1999 .

Mutant cell lines unresponsive to alpha/beta and gamma interferon are defective in tyrosine phosphorylation of ISGF-3 alpha components

R. Flavell, C. Schindler, A. Wilks, 1994, Molecular and cellular biology.

Imaging FRET between spectrally similar GFP molecules in single cells

Fred S. Wouters, F. Wouters, P. Bastiaens, 2001, Nature Biotechnology.

The JAK Family of Protein Tyrosine Kinases

A. Wilks, A. Harpur, 1996 .

Colony-stimulating factor 1-induced STAT1 and STAT3 activation is accompanied by phosphorylation of Tyk2 in macrophages and Tyk2 and JAK1 in fibroblasts

A. Wilks, U. Novak, J. Hamilton, 1995 .

Association of transcription factor APRF and protein kinase Jak1 with the interleukin-6 signal transducer gp130.

C. Schindler, A. Wilks, K. Yasukawa, 1994, Science.

JAK2, a third member of the JAK family of protein tyrosine kinases.

A. Andres, A. Wilks, A. Ziemiecki, 1992, Oncogene.

Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase

A. Wilks, A. Ziemiecki, A. Harpur, 1991, Molecular and cellular biology.

RYK, a receptor tyrosine kinase-related molecule with unusual kinase domain motifs.

C. Hovens, A. Andres, A. Wilks, 1992, Proceedings of the National Academy of Sciences of the United States of America.

Identification of JAK protein tyrosine kinases as signaling molecules for prolactin. Functional analysis of prolactin receptor and prolactin‐erythropoietin receptor chimera expressed in lymphoid cells.

A. Wilks, I. Dusanter-Fourt, A. Ziemiecki, 1994, The EMBO journal.

Binding of a Diphosphotyrosine-containing Peptide That Mimics Activated Platelet-derived Growth Factor Receptor β Induces Oligomerization of Phosphatidylinositol 3-Kinase*

P. Bastiaens, G. Panayotou, M. Waterfield, 1998, The Journal of Biological Chemistry.

Cytokine signal transduction and the JAK family of protein tyrosine kinases

A. Wilks, A. Harpur, Andrew F. Wilks, 1994, BioEssays : news and reviews in molecular, cellular and developmental biology.

The protein tyrosine kinase JAK1 complements defects in interferon-α/β and -γ signal transduction

G. Stark, C. Schindler, O. Silvennoinen, 1993, Nature.

JAK protein tyrosine kinases: their role in cytokine signalling.

A. Wilks, A. Ziemiecki, A. Harpur, 1994, Trends in cell biology.

Kinase‐negative mutants of JAK1 can sustain interferon‐gamma‐inducible gene expression but not an antiviral state.

G. Stark, I. Kerr, J. Ihle, 1996, The EMBO journal.

Differentiation-regulated serine phosphorylation of STAT1 promotes GAF activation in macrophages

C. Schindler, D. Georgellis, A. Wilks, 1995, Molecular and cellular biology.

A prominent natural H-2 Kd ligand is derived from protein tyrosine kinase JAK1.

H. Rammensee, A. Wilks, A. Harpur, 1993, Immunology letters.

Interferon-gamma induces tyrosine phosphorylation of interferon-gamma receptor and regulated association of protein tyrosine kinases, Jak1 and Jak2, with its receptor.

A. Wilks, A. Ziemiecki, A. Harpur, 1994, The Journal of biological chemistry.

Biomolecular interaction analysis of IFN gamma-induced signaling events in whole-cell lysates: prevalence of latent STAT1 in high-molecular weight complexes.

G. Stark, I. Kerr, M. Lackmann, 1998, Growth factors.

Imaging protein interactions by FRET microscopy: FRET measurements by acceptor photobleaching.

P. Verveer, P. Bastiaens, A. Harpur, 2006, CSH protocols.

Measuring FRET by sensitized emission.

P. Verveer, P. Bastiaens, A. Harpur, 2006, CSH protocols.

Intracellular Signal Transduction: The JAK-STAT Pathway

A. Wilks, A. Harpur, 2013, Molecular Biology Intelligence Unit.

Measuring FRET by acceptor photobleaching.

P. Verveer, P. Bastiaens, A. Harpur, 2006, Cold Spring Harbor Protocols.

Intermolecular Interactions of the p85α Regulatory Subunit of Phosphatidylinositol 3-Kinase*

G. Panayotou, M. Waterfield, M. Layton, 1999, The Journal of Biological Chemistry.

Imaging protein interactions by FRET microscopy: FLIM measurements.

P. Verveer, P. Bastiaens, A. Harpur, 2006, CSH protocols.