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Journal article

The molecular chaperone Hsp90 is required for signal transduction by wild-type Hck and maintenance of its constitutively active counterpart

GM Scholz, SD Hartson, K Cartledge, L Volk, RL Matts, AR Dunn

Cell Growth and Differentiation | AMER ASSOC CANCER RESEARCH | Published : 2001

University of Melbourne Researchers

Ashley Dunn's Profile Picture
Ashley Dunn Author Surgery - Royal Melbourne Hospital

Glen Scholz's Profile Picture
Glen Scholz Author Melbourne Dental School

Grants

Awarded by NIGMS NIH HHS


Awarded by NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES


Citation metrics

25Web of Science
28Scopus
19Dimensions

Keywords

Catalytic Domain
Focal Adhesion Kinase 2
Phosphorylation
Tyrosine
Proto-Oncogene Proteins C-Hck
Binding-Site
Signal Transduction
Geldanamycin
Bacterial Lipopolysaccharide
Macrophages
Science & Technology
Tyrosine Kinase
Cell Adhesion
P50(cdc37)
Cell Biology
Hsp90 Heat-Shock Proteins
Protein Folding
Lipopolysaccharide Receptors
Heat-Shock-Protein
Protein-Tyrosine Kinases
Quinones
In-Vivo
Lactams, Macrocyclic
Retroviridae Proteins, Oncogenic
Antigens, Cd14
Cells, Cultured
Enzyme Inhibitors
Terminal Domain
Oncogene Protein V-Cbl
Src-Family Kinases
Mice
Lipopolysaccharides
Proto-Oncogene Proteins
Protein Structure, Tertiary
Life Sciences & Biomedicine
Animals
Toll-Like Receptor-4
Benzoquinones
Macrophage Activation

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