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U Hartl

Showing results (31-40 of 133) with videos related to

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Nature|July 24, 1997
Recombination of protein domains facilitated by co-translational folding in eukaryotesW J Netzer, F U Hartl
Trends in Biochemical Sciences|April 16, 1998
Protein folding in the cytosol: chaperonin-dependent and -independent mechanismsW J Netzer, F U Hartl
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
Pageof 14

Showing results (31-40 of 133) with videos related to

Sort By:
Pageof 14
Nature|July 24, 1997
Recombination of protein domains facilitated by co-translational folding in eukaryotesW J Netzer, F U Hartl
Trends in Biochemical Sciences|April 16, 1998
Protein folding in the cytosol: chaperonin-dependent and -independent mechanismsW J Netzer, F U Hartl
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
Pageof 14