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Items: 1 to 20 of 138

1.

HspB2/myotonic dystrophy protein kinase binding protein (MKBP) as a novel molecular chaperone: structural and functional aspects.

Prabhu S, Raman B, Ramakrishna T, Rao ChM.

PLoS One. 2012;7(1):e29810. doi: 10.1371/journal.pone.0029810. Epub 2012 Jan 17.

2.

The small heat-shock proteins HSPB2 and HSPB3 form well-defined heterooligomers in a unique 3 to 1 subunit ratio.

den Engelsman J, Boros S, Dankers PY, Kamps B, Vree Egberts WT, Böde CS, Lane LA, Aquilina JA, Benesch JL, Robinson CV, de Jong WW, Boelens WC.

J Mol Biol. 2009 Nov 13;393(5):1022-32. doi: 10.1016/j.jmb.2009.08.052. Epub 2009 Aug 26.

PMID:
19715703
4.

Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation.

Sugiyama Y, Suzuki A, Kishikawa M, Akutsu R, Hirose T, Waye MM, Tsui SK, Yoshida S, Ohno S.

J Biol Chem. 2000 Jan 14;275(2):1095-104.

5.

Structural aspects and chaperone activity of human HspB3: role of the "C-terminal extension".

Asthana A, Raman B, Ramakrishna T, Rao ChM.

Cell Biochem Biophys. 2012 Sep;64(1):61-72. doi: 10.1007/s12013-012-9366-x.

PMID:
22610661
6.

Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimics.

Nagaraj RH, Panda AK, Shanthakumar S, Santhoshkumar P, Pasupuleti N, Wang B, Biswas A.

PLoS One. 2012;7(1):e30257. doi: 10.1371/journal.pone.0030257. Epub 2012 Jan 17.

7.

MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase.

Suzuki A, Sugiyama Y, Hayashi Y, Nyu-i N, Yoshida M, Nonaka I, Ishiura S, Arahata K, Ohno S.

J Cell Biol. 1998 Mar 9;140(5):1113-24.

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Structural and functional aspects of hetero-oligomers formed by the small heat shock proteins αB-crystallin and HSP27.

Aquilina JA, Shrestha S, Morris AM, Ecroyd H.

J Biol Chem. 2013 May 10;288(19):13602-9. doi: 10.1074/jbc.M112.443812. Epub 2013 Mar 26.

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14.

Arginine hydrochloride enhances the dynamics of subunit assembly and the chaperone-like activity of alpha-crystallin.

Srinivas V, Raman B, Rao KS, Ramakrishna T, Rao ChM.

Mol Vis. 2005 Apr 1;11:249-55.

15.

HSPB2/MKBP, a novel and unique member of the small heat-shock protein family.

Hu Z, Yang B, Lu W, Zhou W, Zeng L, Li T, Wang X.

J Neurosci Res. 2008 Aug 1;86(10):2125-33. doi: 10.1002/jnr.21682. Review.

PMID:
18615620
16.

Phe71 is essential for chaperone-like function in alpha A-crystallin.

Santhoshkumar P, Sharma KK.

J Biol Chem. 2001 Dec 14;276(50):47094-9. Epub 2001 Oct 11.

17.

Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin.

Plater ML, Goode D, Crabbe MJ.

J Biol Chem. 1996 Nov 8;271(45):28558-66.

18.

Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity.

Chowdary TK, Raman B, Ramakrishna T, Rao CM.

Biochem J. 2004 Jul 15;381(Pt 2):379-87.

19.

Effect of a single AGE modification on the structure and chaperone activity of human alphaB-crystallin.

Bhattacharyya J, Shipova EV, Santhoshkumar P, Sharma KK, Ortwerth BJ.

Biochemistry. 2007 Dec 18;46(50):14682-92. Epub 2007 Nov 21.

PMID:
18027913
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