Sort by

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 90


Role of DnaJ G/F-rich domain in conformational recognition and binding of protein substrates.

Perales-Calvo J, Muga A, Moro F.

J Biol Chem. 2010 Oct 29;285(44):34231-9. doi: 10.1074/jbc.M110.144642.


Unique structural modulation of a non-native substrate by cochaperone DnaJ.

Tiwari S, Kumar V, Jayaraj GG, Maiti S, Mapa K.

Biochemistry. 2013 Feb 12;52(6):1011-8. doi: 10.1021/bi301543g.


Structural insights into the chaperone activity of the 40-kDa heat shock protein DnaJ: binding and remodeling of a native substrate.

Cuéllar J, Perales-Calvo J, Muga A, Valpuesta JM, Moro F.

J Biol Chem. 2013 May 24;288(21):15065-74. doi: 10.1074/jbc.M112.430595.


Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.

Suh WC, Burkholder WF, Lu CZ, Zhao X, Gottesman ME, Gross CA.

Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15223-8.


The role of the DIF motif of the DnaJ (Hsp40) co-chaperone in the regulation of the DnaK (Hsp70) chaperone cycle.

Cajo GC, Horne BE, Kelley WL, Schwager F, Georgopoulos C, Genevaux P.

J Biol Chem. 2006 May 5;281(18):12436-44.


The Hsp40 J-domain stimulates Hsp70 when tethered by the client to the ATPase domain.

Horne BE, Li T, Genevaux P, Georgopoulos C, Landry SJ.

J Biol Chem. 2010 Jul 9;285(28):21679-88. doi: 10.1074/jbc.M110.113118.


Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones.

Laufen T, Mayer MP, Beisel C, Klostermeier D, Mogk A, Reinstein J, Bukau B.

Proc Natl Acad Sci U S A. 1999 May 11;96(10):5452-7.


DnaJ (Hsp40 protein) binding to folded substrate impacts KplE1 prophage excision efficiency.

Puvirajesinghe TM, Elantak L, Lignon S, Franche N, Ilbert M, Ansaldi M.

J Biol Chem. 2012 Apr 20;287(17):14169-77. doi: 10.1074/jbc.M111.331462.


The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70.

Wittung-Stafshede P, Guidry J, Horne BE, Landry SJ.

Biochemistry. 2003 May 6;42(17):4937-44.


Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.

Gässler CS, Buchberger A, Laufen T, Mayer MP, Schröder H, Valencia A, Bukau B.

Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15229-34.


Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones.

Rodriguez F, Arsène-Ploetze F, Rist W, Rüdiger S, Schneider-Mergener J, Mayer MP, Bukau B.

Mol Cell. 2008 Nov 7;32(3):347-58. doi: 10.1016/j.molcel.2008.09.016.


ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates.

Wawrzynów A, Banecki B, Wall D, Liberek K, Georgopoulos C, Zylicz M.

J Biol Chem. 1995 Aug 18;270(33):19307-11.

Items per page

Supplemental Content

Support Center