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Proceedings of the National Academy of Sciences of the United States of America
|
October 15, 1996
Interplay of structure and disorder in cochaperonin mobile loops
S J Landry, A Taher, C Georgopoulos, et al.
The Journal of Biological Chemistry
|
August 18, 1995
ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates
A Wawrzynów, B Banecki, D Wall, et al.
Nucleic Acids Research
|
June 25, 1984
The nucleotide sequence of the Escherichia coli K12 nusB (groNB) gene
J Swindle, J Ajioka, D Dawson, et al.
American Journal of Speech-Language Pathology
|
April 27, 2016
Postextubation Dysphagia in Critical Patients: A First Report From the Largest Step-Down Intensive Care Unit in Greece
Georgia A Malandraki, Vasiliki Markaki, Voula C Georgopoulos, et al.
The Journal of Biological Chemistry
|
February 25, 1990
Physical interactions between bacteriophage and Escherichia coli proteins required for initiation of lambda DNA replication
K Liberek, J Osipiuk, M Zylicz, et al.
The Journal of Biological Chemistry
|
December 5, 1993
Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity
A Ziemienowicz, D Skowyra, J Zeilstra-Ryalls, et al.
Nature
|
July 15, 1993
Characterization of a functionally important mobile domain of GroES
S J Landry, J Zeilstra-Ryalls, O Fayet, et al.
The Journal of Biological Chemistry
|
December 16, 2000
Pseudo-T-even bacteriophage RB49 encodes CocO, a cochaperonin for GroEL, which can substitute for Escherichia coli's GroES and bacteriophage T4's Gp31
D Ang, A Richardson, M P Mayer, et al.
Gene
|
November 1, 1982
Mutants in the y region of bacteriophage lambda constitutive for repressor synthesis: their isolation and the characterization of the Hyp phenotype
H Eisen, P Barrand, W Spiegelman, et al.
Nature Structural Biology
|
November 10, 1998
The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding
F Weber, F Keppel, C Georgopoulos, et al.
Page
of 15
Search research articles
Search
Showing results (121-130 of 146) with videos related to
Sort By:
Page
of 15
Proceedings of the National Academy of Sciences of the United States of America
|
October 15, 1996
Interplay of structure and disorder in cochaperonin mobile loops
S J Landry, A Taher, C Georgopoulos, et al.
The Journal of Biological Chemistry
|
August 18, 1995
ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates
A Wawrzynów, B Banecki, D Wall, et al.
Nucleic Acids Research
|
June 25, 1984
The nucleotide sequence of the Escherichia coli K12 nusB (groNB) gene
J Swindle, J Ajioka, D Dawson, et al.
American Journal of Speech-Language Pathology
|
April 27, 2016
Postextubation Dysphagia in Critical Patients: A First Report From the Largest Step-Down Intensive Care Unit in Greece
Georgia A Malandraki, Vasiliki Markaki, Voula C Georgopoulos, et al.
The Journal of Biological Chemistry
|
February 25, 1990
Physical interactions between bacteriophage and Escherichia coli proteins required for initiation of lambda DNA replication
K Liberek, J Osipiuk, M Zylicz, et al.
The Journal of Biological Chemistry
|
December 5, 1993
Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity
A Ziemienowicz, D Skowyra, J Zeilstra-Ryalls, et al.
Nature
|
July 15, 1993
Characterization of a functionally important mobile domain of GroES
S J Landry, J Zeilstra-Ryalls, O Fayet, et al.
The Journal of Biological Chemistry
|
December 16, 2000
Pseudo-T-even bacteriophage RB49 encodes CocO, a cochaperonin for GroEL, which can substitute for Escherichia coli's GroES and bacteriophage T4's Gp31
D Ang, A Richardson, M P Mayer, et al.
Gene
|
November 1, 1982
Mutants in the y region of bacteriophage lambda constitutive for repressor synthesis: their isolation and the characterization of the Hyp phenotype
H Eisen, P Barrand, W Spiegelman, et al.
Nature Structural Biology
|
November 10, 1998
The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding
F Weber, F Keppel, C Georgopoulos, et al.
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of 15