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Binding sites for Hsp70 molecular chaperones in natural proteins
M. J. Gething
, S. Blond-Elguindi
,
J. Buchner
, A. Fourie
, G. Knarr
, S. Modrow
, L. Nanu
, M. Segal
, J. Sambrook
University of Melbourne
UIC ECE-CSN-Lab
University of Regensburg
The R.W. Johnson Pharmaceutical Research Institute
Klinikum der Universität Regensburg und Medizinische Fakultät
UT Southwestern Medical Center
Peter Maccallum Cancer Centre
Research output
:
Contribution to journal
›
Article
›
peer-review
36
Scopus citations
Overview
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Keyphrases
Binding Site
100%
Natural Proteins
100%
Hsp70 Molecular Chaperone
100%
High Affinity
42%
Family Members
28%
Immunoglobulin
28%
Peptide Binding
28%
Trimer
28%
Chaperone
28%
DnaK
28%
Hsc70
28%
Computer Program
14%
Protein Function
14%
Heavy Chain
14%
Hydrophobicity
14%
Current Form
14%
Glycoprotein
14%
Precise Location
14%
Binding Capacity
14%
Cysteine Residues
14%
Peptide Sequencing
14%
Disulfide Bond
14%
Light Chain
14%
Hsp70 Chaperone
14%
Heat Shock Protein 70 (HSP70)
14%
Protein Folding
14%
Binding Specificity
14%
Tumor Protein p53 (TP53)
14%
Hsp70 Family
14%
DNA-binding Domain
14%
Influenza Virus
14%
P53 Protein
14%
Disulfide Bond Formation
14%
Mutant Protein
14%
Hydrophobic Surface
14%
Specific Sequences
14%
Folded Molecule
14%
Sequence Preference
14%
P53 Peptide
14%
Subunit Assembly
14%
Binding Data
14%
Stalk Domain
14%
Long Peptides
14%
Bacteriophage
14%
Tumor Suppressor Activity
14%
Biochemistry, Genetics and Molecular Biology
Hsp70
100%
Chaperone Protein
100%
Binding Site
100%
P53
42%
Disulfide Bond
28%
Intravenous Immunoglobulin
28%
Peptide Sequence
14%
Tumor Suppressor Protein
14%
Heavy Chain
14%
Glycoprotein
14%
Hydrophobicity
14%
DNA-binding Domain
14%
Protein Folding
14%
Light Chain
14%
Influenza Virus
14%
Mutant Protein
14%
Cysteine
14%
Bacteriophage
14%