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U Hartl

Showing results (51-60 of 133) with videos related to

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Annual Review of Biochemistry|January 1, 1991
The enzymology of protein translocation across the Escherichia coli plasma membraneW Wickner, A J Driessen, F U Hartl
The EMBO Journal|January 15, 1996
A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substratesA Szabo, R Korszun, F U Hartl, et al.
Nature|July 14, 1994
Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperonesJ Frydman, E Nimmesgern, K Ohtsuka, et al.
European Journal of Biochemistry|December 1, 1987
Mitochondrial precursor proteins are imported through a hydrophilic membrane environmentN Pfanner, F U Hartl, B Guiard, et al.
Cell|December 24, 1987
Successive translocation into and out of the mitochondrial matrix: targeting of proteins to the intermembrane space by a bipartite signal peptideF U Hartl, J Ostermann, B Guiard, et al.
Science (New York, N.Y.)|August 11, 1995
Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein foldingM K Hayer-Hartl, J Martin, F U Hartl
The EMBO Journal|November 1, 1993
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damageH Schröder, T Langer, F U Hartl, et al.
Nature|November 18, 1993
The reaction cycle of GroEL and GroES in chaperonin-assisted protein foldingJ Martin, M Mayhew, T Langer, et al.
Nature|November 18, 1993
Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroESJ Martin, S Geromanos, P Tempst, et al.
Biological Chemistry|May 1, 1998
Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein foldingN Heyrovská, J Frydman, J Höhfeld, et al.
Pageof 14

Showing results (51-60 of 133) with videos related to

Sort By:
Pageof 14
Annual Review of Biochemistry|January 1, 1991
The enzymology of protein translocation across the Escherichia coli plasma membraneW Wickner, A J Driessen, F U Hartl
The EMBO Journal|January 15, 1996
A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substratesA Szabo, R Korszun, F U Hartl, et al.
Nature|July 14, 1994
Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperonesJ Frydman, E Nimmesgern, K Ohtsuka, et al.
European Journal of Biochemistry|December 1, 1987
Mitochondrial precursor proteins are imported through a hydrophilic membrane environmentN Pfanner, F U Hartl, B Guiard, et al.
Cell|December 24, 1987
Successive translocation into and out of the mitochondrial matrix: targeting of proteins to the intermembrane space by a bipartite signal peptideF U Hartl, J Ostermann, B Guiard, et al.
Science (New York, N.Y.)|August 11, 1995
Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein foldingM K Hayer-Hartl, J Martin, F U Hartl
The EMBO Journal|November 1, 1993
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damageH Schröder, T Langer, F U Hartl, et al.
Nature|November 18, 1993
The reaction cycle of GroEL and GroES in chaperonin-assisted protein foldingJ Martin, M Mayhew, T Langer, et al.
Nature|November 18, 1993
Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroESJ Martin, S Geromanos, P Tempst, et al.
Biological Chemistry|May 1, 1998
Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein foldingN Heyrovská, J Frydman, J Höhfeld, et al.
Pageof 14