Binding of a Diphosphorylated-ITAM peptide to spleen tyrosine kinase (Syk) induces distal conformational changes: A hydrogen exchange mass spectrometry study-Reference-Cited by-同舟云学术

Binding of a Diphosphorylated-ITAM peptide to spleen tyrosine kinase (Syk) induces distal conformational changes: A hydrogen exchange mass spectrometry study

Published:2005-07-01 Issue:7 Volume:16 Page:1039-1051
ISSN:1044-0305
Container-title:Journal of the American Society for Mass Spectrometry
language:en
Short-container-title:J. Am. Soc. Mass Spectrom.

Author:

Catalina M. Isabel¹,Fischer Marcel J. E.²,Dekker Frank J.²,Liskamp Rob M. J.²,Heck Albert J. R.¹

Affiliation:

1. Department of Biomolecular Mass Spectrometry, Utrecht Institute for Pharmaceutical Sciences (UIPS) and Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands

2. Department of Medicinal Chemistry, Utrecht Institute for Pharmaceutical Sciences (UIPS), Utrecht University, Utrecht, The Netherlands

Publisher

American Chemical Society (ACS)

Subject

Spectroscopy,Structural Biology

Link

https://pubs.acs.org/doi/pdf/10.1016/j.jasms.2005.02.011

Reference51 articles.

1. Tyrosine kinase SYK: essential functions for immunoreceptor signalling

2. Syk Expression and Novel Function in a Wide Variety of Tissues

3. Antigen receptor tail clue

4. Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation.

5. Signal Transduction by the B Cell Antigen Receptor and its Coreceptors

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