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M K Hayer-Hartl

Showing results (1-10 of 11) with videos related to

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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
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 15, 1996
Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysisM K Hayer-Hartl, F Weber, F U Hartl
Biological Chemistry|June 29, 1999
On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein foldingM K Hayer-Hartl, K L Ewalt, F U Hartl
Nature Structural Biology|January 1, 1995
What is the molten globule?J J Ewbank, T E Creighton, M K Hayer-Hartl, et al.
The EMBO Journal|July 1, 1994
Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbuminM K Hayer-Hartl, J J Ewbank, T E Creighton, et al.
Nature Structural Biology|November 10, 1998
The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein foldingF Weber, F Keppel, C Georgopoulos, et al.
Nitric Oxide : Biology and Chemistry|August 4, 2001
Nitric oxide inhibits the cochaperone activity of the RING finger-like protein DnaJK D Kröncke, H Haase, D Beyersmann, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 22, 2000
Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrilsP J Muchowski, G Schaffar, A Sittler, et al.
Human Molecular Genetics|June 19, 2001
Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's diseaseA Sittler, R Lurz, G Lueder, et al.
Pageof 2

Showing results (1-10 of 11) with videos related to

Sort By:
Pageof 2
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
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 15, 1996
Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysisM K Hayer-Hartl, F Weber, F U Hartl
Biological Chemistry|June 29, 1999
On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein foldingM K Hayer-Hartl, K L Ewalt, F U Hartl
Nature Structural Biology|January 1, 1995
What is the molten globule?J J Ewbank, T E Creighton, M K Hayer-Hartl, et al.
The EMBO Journal|July 1, 1994
Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbuminM K Hayer-Hartl, J J Ewbank, T E Creighton, et al.
Nature Structural Biology|November 10, 1998
The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein foldingF Weber, F Keppel, C Georgopoulos, et al.
Nitric Oxide : Biology and Chemistry|August 4, 2001
Nitric oxide inhibits the cochaperone activity of the RING finger-like protein DnaJK D Kröncke, H Haase, D Beyersmann, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 22, 2000
Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrilsP J Muchowski, G Schaffar, A Sittler, et al.
Human Molecular Genetics|June 19, 2001
Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's diseaseA Sittler, R Lurz, G Lueder, et al.
Pageof 2