Mechanism of substrate recognition by Hsp70 chaperones

2004 ◽  
Vol 32 (4) ◽  
pp. 617-621 ◽  
Author(s):  
A. Erbse ◽  
M.P. Mayer ◽  
B. Bukau

The role of Hsp70 (heat-shock protein 70) chaperones in assisting protein-folding processes relies on their ability to associate with short peptide stretches of protein substrates in a transient and ATP-controlled manner. In the present study, we review the molecular details of the mechanism behind substrate recognition by Hsp70 proteins.

2004 ◽  
Vol 32 (6) ◽  
pp. 1425-1426 ◽  
Author(s):  
Martin Westphal ◽  
Perenlei Enkhbaatar ◽  
Daniel L. Traber

Author(s):  
Jose Rey-Ladino ◽  
Abiola Senok ◽  
Abdullah Sarkar ◽  
Ahlam Al Shedoukhy

FEBS Letters ◽  
2004 ◽  
Vol 561 (1-3) ◽  
pp. 144-148 ◽  
Author(s):  
Samideh Khoei ◽  
Bahram Goliaei ◽  
Ali Neshasteh-Riz ◽  
Abdolkhalegh Deizadji

2011 ◽  
Vol 27 (8) ◽  
pp. 802-810 ◽  
Author(s):  
Doris Helbig ◽  
Jan C. Simon ◽  
Uwe Paasch

2015 ◽  
Vol 368 (2) ◽  
pp. 179-184 ◽  
Author(s):  
Gabriele Multhoff ◽  
Alan G. Pockley ◽  
Thomas E. Schmid ◽  
Daniela Schilling

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