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U Hartl

Showing results (71-80 of 133) with videos related to

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Biological Chemistry|April 4, 2000
Responses to peroxynitrite in yeast: glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a sensitive intracellular target for nitration and enhancement of chaperone expression and ubiquitinationD P Buchczyk, K Briviba, F U Hartl, et al.
Molecular Microbiology|June 1, 1995
Identification of GroEL as a constituent of an mRNA-protection complex in Escherichia coliD Georgellis, B Sohlberg, F U Hartl, et al.
Biological Chemistry Hoppe-Seyler|September 1, 1994
Topology of the morphological domains of the chaperonin GroEL visualized by immuno-electron microscopyJ Martin, K N Goldie, A Engel, et al.
Biochimica Et Biophysica Acta|January 18, 1989
Mitochondrial protein importF U Hartl, N Pfanner, D W Nicholson, et al.
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|September 14, 1989
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysisJ Ostermann, A L Horwich, W Neupert, et al.
Cell|December 26, 1986
Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductaseF U Hartl, B Schmidt, E Wachter, et al.
Journal of Molecular Biology|July 12, 1996
Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domainY Q Qian, D Patel, F U Hartl, et al.
Antonie Van Leeuwenhoek|October 1, 1990
Stress proteins and mitochondrial protein importN Pfanner, J Ostermann, J Rassow, et al.
The EMBO Journal|December 1, 1992
Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavityT Langer, G Pfeifer, J Martin, et al.
Pageof 14

Showing results (71-80 of 133) with videos related to

Sort By:
Pageof 14
Biological Chemistry|April 4, 2000
Responses to peroxynitrite in yeast: glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a sensitive intracellular target for nitration and enhancement of chaperone expression and ubiquitinationD P Buchczyk, K Briviba, F U Hartl, et al.
Molecular Microbiology|June 1, 1995
Identification of GroEL as a constituent of an mRNA-protection complex in Escherichia coliD Georgellis, B Sohlberg, F U Hartl, et al.
Biological Chemistry Hoppe-Seyler|September 1, 1994
Topology of the morphological domains of the chaperonin GroEL visualized by immuno-electron microscopyJ Martin, K N Goldie, A Engel, et al.
Biochimica Et Biophysica Acta|January 18, 1989
Mitochondrial protein importF U Hartl, N Pfanner, D W Nicholson, et al.
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|September 14, 1989
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysisJ Ostermann, A L Horwich, W Neupert, et al.
Cell|December 26, 1986
Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductaseF U Hartl, B Schmidt, E Wachter, et al.
Journal of Molecular Biology|July 12, 1996
Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domainY Q Qian, D Patel, F U Hartl, et al.
Antonie Van Leeuwenhoek|October 1, 1990
Stress proteins and mitochondrial protein importN Pfanner, J Ostermann, J Rassow, et al.
The EMBO Journal|December 1, 1992
Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavityT Langer, G Pfeifer, J Martin, et al.
Pageof 14