Structure of the SLy1 SAM homodimer reveals a new interface for SAM domain self-association-Reference-Cited by-同舟云学术

Structure of the SLy1 SAM homodimer reveals a new interface for SAM domain self-association

Published:2019-01-10 Issue:1 Volume:9 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Kukuk Laura^ORCID,Dingley Andrew J.^ORCID,Granzin Joachim^ORCID,Nagel-Steger Luitgard^ORCID,Thiagarajan-Rosenkranz Pallavi,Ciupka Daniel,Hänel Karen^ORCID,Batra-Safferling Renu^ORCID,Pacheco Victor,Stoldt Matthias^ORCID,Pfeffer Klaus^ORCID,Beer-Hammer Sandra^ORCID,Willbold Dieter^ORCID,Koenig Bernd W.^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/s41598-018-37185-3.pdf

Reference75 articles.

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2. Astoul, E. et al. Approaches to define antigen receptor-induced serine kinase signal transduction pathways. J. Biol. Chem. 278, 9267–9275 (2003).

3. Beer, S. et al. Impaired immune responses and prolonged allograft survival in Sly1 mutant mice. Molecular and cellular biology 25, 9646–9660 (2005).

4. Reis, B., Pfeffer, K. & Beer-Hammer, S. The orphan adapter protein SLY1 as a novel anti-apoptotic protein required for thymocyte development. BMC Immunology 10, 38, https://doi.org/10.1186/1471-2172-10-38 (2009).

5. Schäll, D., Schmitt, F., Reis, B., Brandt, S. & Beer-Hammer, S. SLy1 regulates T-cell proliferation during Listeria monocytogenes infection in a Foxo1-dependent manner. European J. of Immunol. 45, 3087–3097 (2015).

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