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Trends in Cell Biology|May 1, 1995
Partner proteins determine multiple functions of Hsp70J Rassow, W Voos, N PfannerMolecular and Cellular Biology|September 21, 2001
Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteinsA Geissler, J Rassow, N Pfanner, et al.The Journal of Biological Chemistry|June 20, 1998
The import route of ADP/ATP carrier into mitochondria separates from the general import pathway of cleavable preproteins at the trans side of the outer membraneM Kübrich, J Rassow, W Voos, et al.Journal of Molecular Biology|December 8, 1995
The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial functionM Moczko, B Schönfisch, W Voos, et al.Molecular and Cellular Biology|July 27, 2000
Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory roleT Krimmer, J Rassow, W H Kunau, et al.The Journal of Cell Biology|June 3, 1999
The J-related segment of tim44 is essential for cell viability: a mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocationA Merlin, W Voos, A C Maarse, et al.The EMBO Journal|June 3, 1996
Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteinsW Voos, O von Ahsen, H Müller, et al.Traffic (Copenhagen, Denmark)|February 24, 2001
The protein import machinery of the mitochondrial membranesJ Rassow, N PfannerCurrent Biology : CB|February 1, 1996
Protein biogenesis: chaperones for nascent polypeptidesJ Rassow, N PfannerFEBS Letters|November 18, 1991
Mitochondrial preproteins en route from the outer membrane to the inner membrane are exposed to the intermembrane spaceJ Rassow, N PfannerPageof 18