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Hsp90 and Co. - A holding for folding
Johannes Buchner
Chair of Biotechnology
Research output
:
Contribution to journal
›
Review article
›
peer-review
591
Scopus citations
Overview
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Dive into the research topics of 'Hsp90 and Co. - A holding for folding'. Together they form a unique fingerprint.
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Keyphrases
Heat Shock Protein 90 (Hsp90)
100%
Chaperone
33%
Recent Advances
16%
Signaling Molecules
16%
High Affinity
16%
In Vitro Experiment
16%
Binding Site
16%
N-terminal Domain
16%
Molecular Chaperone
16%
Co-chaperone
16%
ATP Binding Site
16%
Non-native
16%
Protein Folding
16%
Native Protein
16%
Steroid Receptors
16%
Defined Substrates
16%
Helper Protein
16%
Substrate-dependent
16%
Neuroscience
Chaperone
100%
Binding Site
66%
In Vivo
33%
Adenosine Triphosphate
33%
Protein Folding
33%
Hormone Receptor
33%
In Vitro
33%
Amino Terminal Sequence
33%
Steroid Hormone
33%
Biochemistry, Genetics and Molecular Biology
Hsp90
100%
Binding Site
33%
N-Terminus
16%
Protein Folding
16%
Adenosine Triphosphate
16%
Hormone Receptor
16%