Skip to search formSkip to main contentSkip to account menu

HYPK gene

Known as: HYPK, HSPC136, HUNTINGTIN YEAST 2-HYBRID PROTEIN K 
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2016
2016
Trans-activation of small EDRK-rich factor 2 (SERF2) promoter by Heat Shock Factor 1
2016
2016
L11 A novel approach for treatment of huntington’s disease by genistein-mediated stimulation of autophagy
Background Expansions of CAG codons in the first exon of the HTT gene, encoding huntingtin, result in production of the protein… 
2014
2014
Heat shock transcription factor HSF1 regulates the expression of the Huntingtin-interacting protein HYPK.
2014
2014
Conserved C-terminal nascent peptide binding domain of HYPK facilitates its chaperone-like activity
Human HYPK (Huntingtin Yeast-two-hybrid Protein K) is an intrinsically unstructured chaperone-like protein with no sequence… 
Review
2010
Review
2010
Interfering with Huntington
60 Introduction Pathophysiology. Symptoms such as chorae and psychological changes have led to Huntington’s disease’s reputation… 
2008
2008
A Regulatory Role of the Rnq1 Nonprion Domain for Prion Propagation and Polyglutamine Aggregates
ABSTRACT Prions are infectious, self-propagating protein conformations. Rnq1 is required for the yeast Saccharomyces cerevisiae… 
2008
2008
Biophysical and biological characterization of Huntingtin interacting protein HYPK
2007
2007
Huntingtin-InteractingProtein1InfluencesWormand MousePresynapticFunctionandProtectsCaenorhabditis elegansNeuronsagainstMutantPolyglutamineToxicity
2005
2005
CHARACTERIZATION OF THE EFFECTS OF REDUCED MUTANT HUNTINGTIN IN THE R6/1 MODEL OF HUNTINGTON'S DISEASE
of Dissertation Presented to the Graduate School of the University of Florida in Partial Fulfillment of the Requirements for the… 
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)