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

Histidyl-tRNA synthetase

Histidine-tRNA Ligase, histidyl-tRNA synthetase, HARS
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, Phosphogluconate Dehydrogenase, GCN2
Papers on Histidine-tRNA Ligase
Long-term effects of cognitive therapy on biological rhythms and depressive symptoms: A randomized clinical trial.
Silva et al., Pelotas, Brazil. In J Affect Disord, Dec 2015
Severity of depressive and anxious symptoms was assessed by the Hamilton Depression Rating Scale (HDRS) and the Hamilton Anxiety Rating Scale (HARS), respectively.
Genome-wide association study identifies HLA 8.1 ancestral haplotype alleles as major genetic risk factors for myositis phenotypes.
Myositis Genetics Consortium et al., Bethesda, United States. In Genes Immun, Oct 2015
To identify genetic risk factors in patients of European ancestry, we conducted a genome-wide association study (GWAS) of the major myositis phenotypes in a total of 1710 cases, which included 705 adult dermatomyositis, 473 juvenile dermatomyositis, 532 polymyositis and 202 adult dermatomyositis, juvenile dermatomyositis or polymyositis patients with anti-histidyl-tRNA synthetase (anti-Jo-1) autoantibodies, and compared them with 4724 controls.
Role of Jo-1 in the Immunopathogenesis of the Anti-synthetase Syndrome.
Ascherman, Miami, United States. In Curr Rheumatol Rep, Sep 2015
Histidyl-tRNA synthetase (HRS = Jo-1) represents a key autoantibody target in the anti-synthetase syndrome that is marked by myositis as well as extra-muscular organ complications including interstitial lung disease (ILD).
Loss of function mutations in HARS cause a spectrum of inherited peripheral neuropathies.
Baets et al., Praha, Czech Republic. In Brain, Aug 2015
Recently, a mutation in histidyl-tRNA synthetase (HARS) was identified in a single patient with a late-onset, sensory-predominant peripheral neuropathy; however, the genetic evidence was lacking, making the significance of the finding unclear.
A binding hotspot in Trypanosoma cruzi histidyl-tRNA synthetase revealed by fragment-based crystallographic cocktail screens.
Hol et al., Seattle, United States. In Acta Crystallogr D Biol Crystallogr, Aug 2015
The structure of T. cruzi histidyl-tRNA synthetase (HisRS), a validated drug target, has previously been reported.
Differential effect of soil and environment on metabolic expression of turmeric (Curcuma longa cv. Roma).
Sujata et al., In Indian J Exp Biol, Jun 2015
A high curcumin yielding cultivar i.e., Roma was collected from high altitude research station, Koraput (HARS) and planted in nine agroclimatic regions of Odisha.
Structural basis for recognition of G-1-containing tRNA by histidyl-tRNA synthetase.
Xie et al., Guangzhou, China. In Nucleic Acids Res, Apr 2015
Among all the tRNAs, only tRNA(His) bears a guanine base at position -1 (G-1), and it serves as a major recognition element for histidyl-tRNA synthetase (HisRS).
An 8-Week Randomized, Double-Blind Trial Comparing Efficacy, Safety, and Tolerability of 3 Vilazodone Dose-Initiation Strategies Following Switch From SSRIs and SNRIs in Major Depressive Disorder.
Patkar et al., Pusan, South Korea. In Prim Care Companion Cns Disord, 2014
The secondary efficacy measures were changes in Clinical Global Impressions-Severity (CGI-S), CGI-Improvement (CGI-I), and Hamilton Anxiety Rating Scale (HARS) scores.
Recent advances in Charcot-Marie-Tooth disease.
Timmerman et al., Antwerp, Belgium. In Curr Opin Neurol, 2014
RECENT FINDINGS: Several new Charcot-Marie-Tooth disease-causing genes have been recently identified, further enlarging the genetic diversity and phenotypic variability, including: SBF1, DHTKD1, TFG, MARS, HARS, HINT1, TRIM1, AIFM1, PDK3 and GNB4.
Idiopathic inflammatory myopathies and the anti-synthetase syndrome: a comprehensive review.
Fritzler et al., San Diego, United States. In Autoimmun Rev, 2014
Although several research methods and commercial tests are available, routine testing for anti-ARS autoantibodies (other than anti-Jo-1/histidyl-tRNA synthetase) is not widely available, sometimes leading to delays in diagnosis and poor disease outcomes.
Comparison of long-term outcome between anti-Jo1- and anti-PL7/PL12 positive patients with antisynthetase syndrome.
Jouen et al., Rouen, France. In Autoimmun Rev, 2012
Although anti-Jo1 positive patients with antisynthetase syndrome share features of patients with anti-PL7/PL12 antibody, they exhibit many differences regarding clinical phenotype and long-term outcome.
Genetic mapping and exome sequencing identify variants associated with five novel diseases.
Strauss et al., United States. In Plos One, 2011
Study identified sequence variants in the known disease-causing genes SLC6A3 and FLVCR1, and present evidence to strongly support the pathogenicity of variants identified in TUBGCP6, BRAT1, SNIP1, CRADD, and HARS.
High altitude renal syndrome (HARS).
Escudero et al., Lima, Peru. In J Am Soc Nephrol, 2011
The frequent presentation of systemic hypertension and microalbuminuria with relatively preserved GFR coupled with the presence of polycythemia and hyperuricemia suggests a new clinical syndrome we term high altitude renal syndrome (HARS).
Development of antisynthetase syndrome in a patient with rheumatoid arthritis.
Park et al., Kwangju, South Korea. In Rheumatol Int, 2011
The patient was diagnosed with ASS based on; positivity for anti-histidyl-tRNA synthetase (Jo-1) antibody, interstitial lung disease, polyarthritis, and mechanic's hands.
Novel conformation of histidyl-transfer RNA synthetase in the lung: the target tissue in Jo-1 autoantibody-associated myositis.
Casciola-Rosen et al., Baltimore, United States. In Arthritis Rheum, 2007
A proteolytically sensitive conformation of HisRS exists in the lung, the target tissue associated with this autoantibody response.
Clinical significance of anti-histidyl-tRNA synthetase (Jo1) autoantibodies.
Rousset et al., Lyon, France. In Ann N Y Acad Sci, 2007
clinical and prognostic profiles of 45 patients displaying anti-histidyl-tRNA synthetase autoantibodies were determined
HIV-associated adipose redistribution syndrome as a selective autonomic neuropathy.
Buijs et al., Amsterdam, Netherlands. In Lancet, 2003
Abnormal body-fat distribution in HIV-1-associated adipose redistribution syndrome (HARS) remains unexplained at present.
TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation.
Cohen et al., Stanford, United States. In Proc Natl Acad Sci U S A, 2003
the TSG101 interaction with HRS is a crucial step in endocytic down-regulation of mitogenic signaling and this interaction may have a role in linking the functions of early and late endosomes
Polymyositis and molecular mimicry, a mechanism of autoimmunity.
Jeffrey et al., In Lancet, 1986
The amino acid sequences of Escherichia coli histidyl-tRNA synthetase and alanyl-tRNA synthetase, two proteins recently identified as autoantigens in polymyositis, were compared by a computer alignment procedure with those of the 3600 proteins tabulated in the National Biomedical Research Foundation protein sequence database.
Myositis autoantibody inhibits histidyl-tRNA synthetase: a model for autoimmunity.
Bernstein et al., In Nature, 1983
The protein is immunoprecipitated with tRNA His and appears to be histidyl-tRNA synthetase.
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