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The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1.

Sbroggiò M, Ferretti R, Percivalle E, Gutkowska M, Zylicz A, Michowski W, Kuznicki J, Accornero F, Pacchioni B, Lanfranchi G, Hamm J, Turco E, Silengo L, Tarone G, Brancaccio M.

FEBS Lett. 2008 Jun 11;582(13):1788-94. doi: 10.1016/j.febslet.2008.04.058. Epub 2008 May 12.


Dynamic nucleotide-dependent interactions of cysteine- and histidine-rich domain (CHORD)-containing Hsp90 cochaperones Chp-1 and melusin with cochaperones PP5 and Sgt1.

Hong TJ, Kim S, Wi AR, Lee P, Kang M, Jeong JH, Hahn JS.

J Biol Chem. 2013 Jan 4;288(1):215-22. doi: 10.1074/jbc.M112.398636. Epub 2012 Nov 26.


Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes: implications for chaperoning of NLR innate immunity receptors.

Zhang M, Kadota Y, Prodromou C, Shirasu K, Pearl LH.

Mol Cell. 2010 Jul 30;39(2):269-81. doi: 10.1016/j.molcel.2010.05.010.


Morgana and melusin: two fairies chaperoning signal transduction.

Ferretti R, Sbroggiò M, Di Savino A, Fusella F, Bertero A, Michowski W, Tarone G, Brancaccio M.

Cell Cycle. 2011 Nov 1;10(21):3678-83. doi: 10.4161/cc.10.21.18202. Epub 2011 Nov 1. Review.


Mammalian CHORD-containing protein 1 is a novel heat shock protein 90-interacting protein.

Wu J, Luo S, Jiang H, Li H.

FEBS Lett. 2005 Jan 17;579(2):421-6.


Sgt1 has co-chaperone properties and is up-regulated by heat shock.

Zabka M, Leśniak W, Prus W, Kuźnicki J, Filipek A.

Biochem Biophys Res Commun. 2008 May 23;370(1):179-83. doi: 10.1016/j.bbrc.2008.03.055. Epub 2008 Mar 19.


ERK1/2 activation in heart is controlled by melusin, focal adhesion kinase and the scaffold protein IQGAP1.

Sbroggiò M, Bertero A, Velasco S, Fusella F, De Blasio E, Bahou WF, Silengo L, Turco E, Brancaccio M, Tarone G.

J Cell Sci. 2011 Oct 15;124(Pt 20):3515-24. doi: 10.1242/jcs.091140.


Sgt1 associates with Hsp90: an initial step of assembly of the core kinetochore complex.

Bansal PK, Abdulle R, Kitagawa K.

Mol Cell Biol. 2004 Sep;24(18):8069-79.


The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones.

Li J, Soroka J, Buchner J.

Biochim Biophys Acta. 2012 Mar;1823(3):624-35. doi: 10.1016/j.bbamcr.2011.09.003. Epub 2011 Sep 16. Review.


Cdc37 is a molecular chaperone with specific functions in signal transduction.

Kimura Y, Rutherford SL, Miyata Y, Yahara I, Freeman BC, Yue L, Morimoto RI, Lindquist S.

Genes Dev. 1997 Jul 15;11(14):1775-85.


Chp-1 and melusin, two CHORD containing proteins in vertebrates.

Brancaccio M, Menini N, Bongioanni D, Ferretti R, De Acetis M, Silengo L, Tarone G.

FEBS Lett. 2003 Sep 11;551(1-3):47-52.


Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37.

Prince T, Matts RL.

J Biol Chem. 2004 Sep 17;279(38):39975-81. Epub 2004 Jul 17.


The Hsp90/Cdc37p chaperone system is a determinant of molybdate resistance in Saccharomyces cerevisiae.

Millson SH, Nuttall JM, Mollapour M, Piper PW.

Yeast. 2009 Jun;26(6):339-47. doi: 10.1002/yea.1670.


Functional specificity of co-chaperone interactions with Hsp90 client proteins.

Riggs DL, Cox MB, Cheung-Flynn J, Prapapanich V, Carrigan PE, Smith DF.

Crit Rev Biochem Mol Biol. 2004 Sep-Dec;39(5-6):279-95. Review.


The Drosophila Dpit47 protein is a nuclear Hsp90 co-chaperone that interacts with DNA polymerase alpha.

Crevel G, Bates H, Huikeshoven H, Cotterill S.

J Cell Sci. 2001 Jun;114(Pt 11):2015-25.


S100A1 is a novel molecular chaperone and a member of the Hsp70/Hsp90 multichaperone complex.

Okada M, Hatakeyama T, Itoh H, Tokuta N, Tokumitsu H, Kobayashi R.

J Biol Chem. 2004 Feb 6;279(6):4221-33. Epub 2003 Nov 24.


Melusin, a muscle-specific integrin beta1-interacting protein, is required to prevent cardiac failure in response to chronic pressure overload.

Brancaccio M, Fratta L, Notte A, Hirsch E, Poulet R, Guazzone S, De Acetis M, Vecchione C, Marino G, Altruda F, Silengo L, Tarone G, Lembo G.

Nat Med. 2003 Jan;9(1):68-75. Epub 2002 Dec 23.


Heat-shock protein 90, a chaperone for folding and regulation.

Picard D.

Cell Mol Life Sci. 2002 Oct;59(10):1640-8. Review.

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