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Sterile Alpha Motif

Known as: Motifs, Sterile Alpha, Sterile Alpha Domain, Motif, Sterile Alpha 
The approximately 70 amino acid SAM (Sterile Alpha Motif) domain has been identified in over 400 different proteins with diverse cellular function… 
National Institutes of Health

Related topics

Related topics

11 relations
SAM Domain and HD Domain-Containing Protein 1SAMD11 geneSAMD12 geneSAMD3 gene

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2019
2019
Endothelial Sash1 Is Required for Lung Maturation through Nitric Oxide Signaling.
2013
2013
Nucleotide embargo by SAMHD1: a strategy to block retroviral infection.
2009
2009
NMR structural studies of the Ste11 SAM domain in the dodecyl phosphocholine micelle
The sterile α‐motif (SAM), a relatively small (∼70 amino acids) interaction domain, is found in a variety of proteins involved in… 
2009
2009
Structures of the tumor necrosis factor α inducing protein Tipα: A novel virulence factor from Helicobacter pylori
2006
2006
Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-tail SAM domain interaction.
2005
2005
The C-terminal sterile alpha motif and the extreme C terminus regulate the transcriptional activity of the alpha isoform of p73.
p73, a member of the p53 family, is expressed from two separate promoters, generating TA and DeltaN variants. Each variant… 
2005
2005
The scaffold protein CNK1 interacts with the angiotensin II type 2 receptor.
Highly Cited
2003
Highly Cited
2003
Risk factors for spontaneous bacterial empyema in cirrhotic patients with hydrothorax.
BACKGROUND Spontaneous bacterial empyema (SBEM) is a rare complication of portal hypertension. The characteristics and risk… 
Highly Cited
2001
Highly Cited
2001
Identification of a Novel Human Tankyrase through Its Interaction with the Adaptor Protein Grb14*
Tankyrase is an ankyrin repeat-containing poly(ADP-ribose) polymerase originally isolated as a binding partner for the telomeric… 
2001
2001
Molecular cloning and characterization of a novel SH3 protein (SLY) preferentially expressed in lymphoid cells.
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