Amanote Research
Register
Sign In
Exploiting Protein Conformational Change to Optimize Adenosine-Derived Inhibitors of HSP70
doi 10.1021/acs.jmedchem.5b02001.s002
Full Text
Open PDF
Abstract
Available in
full text
Date
Unknown
Authors
Unknown
Publisher
American Chemical Society (ACS)
Related search
Exploiting Barriers to Optimize Power Consumption of CMPs
Poly Adenosine Diphosphate-Ribose Polymerase Inhibitors and Heat Shock Protein 90 Inhibitors
Journal of Thoracic Oncology
Medicine
Oncology
Respiratory Medicine
Pulmonary
Early Amyloid Β-Protein Aggregation Precedes Conformational Change
Chemical Communications
Surfaces
Alloys
Materials Chemistry
Coatings
Metals
Optical
Magnetic Materials
Films
Catalysis
Chemistry
Electronic
Composites
Ceramics
An Analysis of Conformational Change of a Protein Upon Binding to Ligand by Multicanonical MD
Seibutsu Butsuri
Proteasome and Heat Shock Protein 70 (HSP70) Inhibitors as Therapeutic Alternative in Multiple Myeloma
Oncotarget
Oncology
A Heat Shock Protein Gene inGiardia Lambliaunrelated to HSP70
Nucleic Acids Research
Genetics
Modeling Hsp70-Mediated Protein Folding
Biophysical Journal
Biophysics
Conformational Analyses of Thiirane-Based Gelatinase Inhibitors
Bioorganic and Medicinal Chemistry Letters
Organic Chemistry
Molecular Medicine
Molecular Biology
Biochemistry
Clinical Biochemistry
Pharmaceutical Science
Drug Discovery
Mechanism of Specific G Protein Coupling to Adenosine Receptors
Biophysical Journal
Biophysics