A S52P mutation in the ‘α-crystallin domain’ ofMycobacterium lepraeHSP18 reduces its oligomeric size and chaperone function-Reference-Cited by-同舟云学术

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A S52P mutation in the ‘α-crystallin domain’ ofMycobacterium lepraeHSP18 reduces its oligomeric size and chaperone function

Published:2013-09-30 Issue:23 Volume:280 Page:5994-6009
ISSN:1742-464X
Container-title:FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Nandi Sandip K.¹,Rehna Elengikal A. A.²,Panda Alok K.¹,Shiburaj Sugathan³,Dharmalingam Kuppamuthu²,Biswas Ashis¹

Affiliation:

1. School of Basic Sciences; Indian Institute of Technology Bhubaneswar; Orissa India

2. Department of Genetic Engineering; School of Biotechnology; Madurai Kamraj University; Tamilnadu India

3. Jawaharlal Nehru Tropical Botanic Garden and Research Institute; Palode Thiruvananthapuram Kerala India

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/febs.12519/fullpdf

Reference70 articles.

1. New puffing pattern induced by temperature shock and DNP in Drosophila;Ritossa;Experientia,1962

2. Molecular chaperones in the cytosol: from nascent chain to folded protein;Hartl;Science,2002

3. Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network;Narberhaus;Microbiol Mol Biol Rev,2002

4. Small heat-shock proteins and their potential role in human disease;Clark;Curr Opin Struct Biol,2000

5. Small heat shock proteins are molecular chaperones;Jakob;J Biol Chem,1993

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