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F U Hartl

Showing results (31-40 of 128) with videos related to

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The EMBO Journal|November 4, 2000
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23J C Young, F U Hartl
Annual Review of Biochemistry|January 1, 1993
Molecular chaperone functions of heat-shock proteinsJ P Hendrick, F U Hartl
Biochemical Society Symposium|September 28, 2001
Contribution of molecular chaperones to protein folding in the cytoplasm of prokaryotic and eukaryotic cellsD J Naylor, F U Hartl
Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie|November 1, 1983
Rat liver peroxisomes, II. Stimulation of peroxisomal fatty-acid beta-oxidation by thyroid hormonesW W Just, F U Hartl
Nature Structural Biology|July 1, 1995
Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein foldingR Hlodan, P Tempst, F U Hartl
Cell|November 17, 1995
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycleJ Höhfeld, Y Minami, F U Hartl
Annual Review of Biophysics and Biomolecular Structure|January 1, 1992
Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60F U Hartl, J Martin, W Neupert
Trends in Biochemical Sciences|January 1, 1994
Molecular chaperones in protein folding: the art of avoiding sticky situationsF U Hartl, R Hlodan, T Langer
FEBS Letters|March 29, 1993
A comment on: 'The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60): evidence for the presence of a single tryptophan', by N.C. Price, S.M. Kelly, S. Wood and A. auf der Mauer (1991) FEBS Lett. 292, 9-12M K Hayer-Hartl, F U Hartl
European Journal of Biochemistry|August 1, 1988
Import of proteins into mitochondria: a multi-step processN Pfanner, F U Hartl, W Neupert
Pageof 13

Showing results (31-40 of 128) with videos related to

Sort By:
Pageof 13
The EMBO Journal|November 4, 2000
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23J C Young, F U Hartl
Annual Review of Biochemistry|January 1, 1993
Molecular chaperone functions of heat-shock proteinsJ P Hendrick, F U Hartl
Biochemical Society Symposium|September 28, 2001
Contribution of molecular chaperones to protein folding in the cytoplasm of prokaryotic and eukaryotic cellsD J Naylor, F U Hartl
Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie|November 1, 1983
Rat liver peroxisomes, II. Stimulation of peroxisomal fatty-acid beta-oxidation by thyroid hormonesW W Just, F U Hartl
Nature Structural Biology|July 1, 1995
Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein foldingR Hlodan, P Tempst, F U Hartl
Cell|November 17, 1995
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycleJ Höhfeld, Y Minami, F U Hartl
Annual Review of Biophysics and Biomolecular Structure|January 1, 1992
Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60F U Hartl, J Martin, W Neupert
Trends in Biochemical Sciences|January 1, 1994
Molecular chaperones in protein folding: the art of avoiding sticky situationsF U Hartl, R Hlodan, T Langer
FEBS Letters|March 29, 1993
A comment on: 'The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60): evidence for the presence of a single tryptophan', by N.C. Price, S.M. Kelly, S. Wood and A. auf der Mauer (1991) FEBS Lett. 292, 9-12M K Hayer-Hartl, F U Hartl
European Journal of Biochemistry|August 1, 1988
Import of proteins into mitochondria: a multi-step processN Pfanner, F U Hartl, W Neupert
Pageof 13