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HSP90AA2P gene

Known as: HSP90ALPHA, HSP90AA2P, heat shock protein 90kDa alpha family class A member 2, pseudogene 
National Institutes of Health

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Related topics

2 relations
HSP90AA1 geneHeat Shock Protein HSP 90-Alpha

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2009
Highly Cited
2009
The regulatory mechanism of Hsp90α secretion and its function in tumor malignancy
Heat shock protein 90-α (Hsp90α) is an intracellular molecular chaperone. However, it can also be secreted with the underlying… 
Highly Cited
2008
Highly Cited
2008
The Tale of Two Domains
Very little is known about SET- and MYND-containing protein 2 (SMYD2), a member of the SMYD protein family. However, the interest… 
Highly Cited
2008
Highly Cited
2008
Heat-shock protein 90α1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos
Heat-shock protein 90α (Hsp90α) is a member of the molecular chaperone family involved in protein folding and assembly. The role… 
Highly Cited
2007
Highly Cited
2007
STAT3 and MAPK signaling maintain overexpression of heat shock proteins 90alpha and beta in multiple myeloma cells, which critically contribute to tumor-cell survival.
The combined blockade of the IL-6R/STAT3 and the MAPK signaling pathways has been shown to inhibit bone marrow microenvironment… 
2007
2007
Heat shock protein 90alpha recruits FLIPS to the death-inducing signaling complex and contributes to TRAIL resistance in human glioma.
Heat shock protein 90 (HSP90) is a molecular chaperone that contributes to the proper folding and stability of target proteins… 
Highly Cited
2004
Highly Cited
2004
Development of a Fluorescence Polarization Assay for the Molecular Chaperone Hsp90
Heat shock protein 90 (Hsp90) is a molecular chaperone with essential functions in maintaining transformation, and there is… 
Highly Cited
2003
Highly Cited
2003
JlpA of Campylobacter jejuni interacts with surface‐exposed heat shock protein 90α and triggers signalling pathways leading to the activation of NF‐κB and p38 MAP kinase in epithelial cells
Campylobacter jejuni is a leading cause of acute bacterial gastroenteritis in humans. The mechanism by which C. jejuni interacts… 
2002
2002
A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone.
The alpha isoform of human 90-kDa heat shock protein (HSP90alpha) is composed of three domains: the N-terminal (residues 1-400… 
Highly Cited
2000
Highly Cited
2000
Expression of heat shock proteins in osteosarcoma and its relationship to prognosis.
Highly Cited
1999
Highly Cited
1999
Intron-independent Association of Splicing Factors with Active Genes
The cell nucleus is organized as discrete domains, often associated with specific events involved in chromosome organization… 
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