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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Sterile alpha and TIR motif containing 1

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Top mentioned proteins: fibrillin-1, MyD88, TRAM, Armadillo, CAN
Papers on SARM
SARM modulates MyD88-mediated TLR activation through BB-loop dependent TIR-TIR interactions.
Byrne et al., London, United Kingdom. In Biochim Biophys Acta, Feb 2016
Of the five TIR domain-containing adaptor proteins identified, Sterile α- and armadillo-motif-containing protein (SARM) is functionally unique; suppressing immune signalling instead of promoting it.
In vitro metabolism study of a black market product containing SARM LGD-4033.
Deventer et al., Gent, Belgium. In Drug Test Anal, Feb 2016
A black market product labelled to contain the SARM LGD-4033 was purchased over the Internet.
Proteome-wide muscle protein fractional synthesis rates predict muscle mass gain in response to a selective androgen receptor modulator in rats.
Evans et al., China. In Am J Physiol Endocrinol Metab, Jan 2016
Utilizing Selective Androgen Receptor Modulator (SARM) treatment in the ovariectomized (OVX) rat, we applied an unbiased, dynamic proteomics approach to measure the fractional synthesis rates (FSR) of 167-201 individual skeletal muscle proteins in triceps, EDL and soleus.
Wallerian Degeneration Is Executed by an NMN-SARM1-Dependent Late Ca(2+) Influx but Only Modestly Influenced by Mitochondria.
Conforti et al., Nottingham, United Kingdom. In Cell Rep, Jan 2016
NMN requires the pro-degenerative protein SARM1 to stimulate Ca(2+) influx and axon degeneration.
SARM1, Not MyD88, Mediates TLR7/TLR9-Induced Apoptosis in Neurons.
Peterson et al., Hamilton, United States. In J Immunol, Dec 2015
Instead, apoptosis required the TLR adaptor molecule SARM1, which localized to the mitochondria following TLR activation and was associated with mitochondrial accumulation in neurites.
Selective androgen receptor modulator activity of a steroidal antiandrogen TSAA-291 and its cofactor recruitment profile.
Hara et al., Tokyo, Japan. In Eur J Pharmacol, Nov 2015
In this study, we investigated the SARM activity of TSAA-291, previously known as a steroidal antiandrogen, in mice because TSAA-291 was found to possess partial androgen receptor agonist activity in reporter assays.
SARM1 activation triggers axon degeneration locally via NAD⁺ destruction.
Milbrandt et al., Saint Louis, United States. In Science, May 2015
Sterile alpha and TIR motif-containing 1 (SARM1) protein is an essential mediator of axon degeneration.
Toll/interleukin-1 receptor (TIR) domain-mediated cellular signaling pathways.
Park et al., Kyŏngsan, South Korea. In Apoptosis, Feb 2015
The Toll-like receptor/Interleukin (IL)-1 receptor (TLR/IL-1R) superfamily comprises proteins that contain the phylogenetically conserved Toll/IL-1 receptor (TIR) domain, which is responsible for the propagation of downstream signaling through recruitment of TIR domain containing cytosolic adaptor proteins such as MyD88, TIRAP/MAL, TRIF, TRAM and SARM.
Beyond TLR Signaling—The Role of SARM in Antiviral Immune Defense, Apoptosis & Development.
Ding et al., Singapore, Singapore. In Int Rev Immunol, 2014
SARM (Sterile alpha and armadillo motif-containing protein) is the recently identified TIR domain-containing cytosolic protein.
TLR2 and TLR4 in autoimmune diseases: a comprehensive review.
Lu et al., Changsha, China. In Clin Rev Allergy Immunol, 2014
There are five adaptors to TLRs including MyD88, TRIF, TIRAP/MAL, TRAM, and SARM.
Wallerian degeneration: an emerging axon death pathway linking injury and disease.
Coleman et al., Nottingham, United Kingdom. In Nat Rev Neurosci, 2014
Rapid Wallerian degeneration requires the pro-degenerative molecules SARM1 and PHR1.
Selective androgen receptor modulators for the prevention and treatment of muscle wasting associated with cancer.
Steiner et al., Memphis, United States. In Curr Opin Support Palliat Care, 2013
Enobosarm, a nonsteroidal SARM, is the most well characterized clinically, and has consistently demonstrated increases in lean body mass and better physical function across several populations along with a lower hazard ratio for survival in cancer patients.
Activation of the innate signaling molecule MAVS by bunyavirus infection upregulates the adaptor protein SARM1, leading to neuronal death.
Peterson et al., Hamilton, United States. In Immunity, 2013
By using in vitro studies in primary neurons and in vivo studies in mice, we have shown that LACV infection induced the RNA helicase, RIG-I, and mitochondrial antiviral signaling protein (MAVS) signaling pathway, resulting in upregulation of the sterile alpha and TIR-containing motif 1 (SARM1), an adaptor molecule that we found to be directly involved in neuronal damage.
dSarm/Sarm1 is required for activation of an injury-induced axon death pathway.
Freeman et al., Worcester, United States. In Science, 2012
severed mouse Sarm1 null axons exhibit long-term survival both in vivo and in vitro, indicating Sarm1 prodegenerative signaling is conserved in mammals; results provide direct evidence that axons actively promote their own destruction after injury and identify dSarm/Sarm1 as a member of an ancient axon death signaling pathway
Targeting of pro-apoptotic TLR adaptor SARM to mitochondria: definition of the critical region and residues in the signal sequence.
Ding et al., Singapore, Singapore. In Biochem J, 2012
The N-terminal 27 amino acids (S27) of SARM, which is hydrophobic and polybasic, acts as a mitochondria-targeting signal sequence, associating SARM to the mitochondria. The S27 peptide has an inherent ability to bind to lipids and mitochondria.
Burkholderia pseudomallei-induced expression of a negative regulator, sterile-alpha and Armadillo motif-containing protein, in mouse macrophages: a possible mechanism for suppression of the MyD88-independent pathway.
Utaisincharoen et al., Bangkok, Thailand. In Infect Immun, 2011
Burkholderia pseudomallei modulates macrophage defense mechanisms by upregulating SARM, thus leading to the suppression of IFN-beta and iNOS needed for bacterial elimination
Sarm1, a negative regulator of innate immunity, interacts with syndecan-2 and regulates neuronal morphology.
Hsueh et al., Taipei, Taiwan. In J Cell Biol, 2011
Sarm1, a negative regulator of innate immunity, interacts with syndecan-2 and regulates neuronal morphogenesis.
SARM inhibits both TRIF- and MyD88-mediated AP-1 activation.
Ding et al., Singapore, Singapore. In Eur J Immunol, 2010
SARM-mediated inhibition may not be exclusively directed at TRIF or MyD88, but that SARM may also directly inhibit MAPK phosphorylation
The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling.
Bowie et al., Dublin, Ireland. In Nat Rev Immunol, 2007
Signalling by Toll-like receptors (TLRs) involves five adaptor proteins known as MyD88, MAL, TRIF, TRAM and SARM.
The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling.
Bowie et al., Dublin, Ireland. In Nat Immunol, 2006
TIR adaptor SARM is a negative regulator of Toll-like receptor signaling.
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