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F U Hartl

Showing results (81-90 of 128) with videos related to

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Nature|January 26, 2000
Identification of in vivo substrates of the chaperonin GroELW A Houry, D Frishman, C Eckerskorn, et al.
FEBS Letters|June 22, 1992
Formation and quantification of protein complexes between peroxisomal alcohol oxidase and GroELM E Evers, T Langer, W Harder, et al.
Cell|August 8, 1997
In vivo observation of polypeptide flux through the bacterial chaperonin systemK L Ewalt, J P Hendrick, W A Houry, et al.
Science (New York, N.Y.)|February 27, 2001
Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factorsH Sondermann, C Scheufler, C Schneider, et al.
The Journal of Cell Biology|October 1, 1989
Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sitesJ Rassow, B Guiard, U Wienhues, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 25, 1994
The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpEA Szabo, T Langer, H Schröder, 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.
The Journal of Biological Chemistry|September 25, 1990
Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondriaN Pfanner, J Rassow, B Guiard, et al.
Cell|June 3, 1988
Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing proteinG Hawlitschek, H Schneider, B Schmidt, et al.
Pageof 13

Showing results (81-90 of 128) with videos related to

Sort By:
Pageof 13
Nature|January 26, 2000
Identification of in vivo substrates of the chaperonin GroELW A Houry, D Frishman, C Eckerskorn, et al.
FEBS Letters|June 22, 1992
Formation and quantification of protein complexes between peroxisomal alcohol oxidase and GroELM E Evers, T Langer, W Harder, et al.
Cell|August 8, 1997
In vivo observation of polypeptide flux through the bacterial chaperonin systemK L Ewalt, J P Hendrick, W A Houry, et al.
Science (New York, N.Y.)|February 27, 2001
Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factorsH Sondermann, C Scheufler, C Schneider, et al.
The Journal of Cell Biology|October 1, 1989
Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sitesJ Rassow, B Guiard, U Wienhues, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 25, 1994
The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpEA Szabo, T Langer, H Schröder, 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.
The Journal of Biological Chemistry|September 25, 1990
Energy requirements for unfolding and membrane translocation of precursor proteins during import into mitochondriaN Pfanner, J Rassow, B Guiard, et al.
Cell|June 3, 1988
Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing proteinG Hawlitschek, H Schneider, B Schmidt, et al.
Pageof 13