The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins-Reference-Cited by-同舟云学术

The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins

Published:2017-04-08 Issue:4 Volume:22 Page:627-638
ISSN:1355-8145
Container-title:Cell Stress and Chaperones
language:en
Short-container-title:Cell Stress and Chaperones

Author:

Carver John A.,Grosas Aidan B.,Ecroyd Heath,Quinlan Roy A.

Funder

National Health and Medical Research Council

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Biochemistry

Link

http://link.springer.com/article/10.1007/s12192-017-0789-6/fulltext.html

Reference130 articles.

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3. Almeida-Souza L, Asselbergh B, d'Ydewalle C et al (2011) Small heat-shock protein HSPB1 mutants stabilize microtubules in Charcot-Marie-Tooth neuropathy. J Neurosci 31(43):15320–15328. doi: 10.1523/JNEUROSCI.3266-11.2011

4. Aquilina JA, Benesch JL, Bateman OA, Slingsby C, Robinson CV (2003) Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in αB-crystallin. Proc Natl Acad Sci U S A 100(19):10611–10616. doi: 10.1073/pnas.1932958100

5. Asomugha C, Gupta R, Srivastava O (2011) Structural and functional roles of deamidation of N146 and/or truncation of NH2- or COOH-termini in human αB-crystallin. Mol Vis 17(262):2407–2420

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