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Search results 201 to 254 out of 254 for Msra

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Type Details Score
Publication
- | J:155856
       
First Author: The Gene Ontology Consortium
Year: 2014
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
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Publication
- | J:342604
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
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Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
21677750 | J:173534
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
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Publication
- | J:141210
     
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
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Publication
- | J:326541
       
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Protein Domain
IPR002569 | Met_Sox_Rdtase_MsrA_dom
Type: Domain
Description: Peptide methionine sulphoxide reductase (Msr) reverses the inactivation of many proteins due to the oxidation of critical methionine residues by reducing methionine sulphoxide, Met(O), to methionine []. It is present in most living organisms, and the cognate structural gene belongs to the so-called minimum gene set [, ].The domains MsrA and MsrB reduce different epimeric forms of methionine sulphoxide. This group represent MsrA, the crystal structure of which has been determined in a number of organisms. In Mycobacterium tuberculosis, the MsrA structure has been determined to 1.5 Angstrom resolution []. In contrast to the three catalytic cysteine residues found in previously characterised MsrA structures, M. tuberculosis MsrA represents a class containing only two functional cysteine residues. The overall structure shows no resemblance to the structures of MsrB () from other organisms; though the active sites show approximate mirror symmetry. In each case, conserved amino acid motifs mediate the stereo-specific recognition and reduction of the substrate. In a number of pathogenic bacteria including Neisseria gonorrhoeae, the MsrA and MsrB domains are fused; the MsrA being N-terminal to MsrB. This arrangement is reversed in Treponema pallidum. In N. gonorrhoeae and Neisseria meningitidis a thioredoxin domain is fused to the N terminus. This may function to reduce the active sites of the downstream MsrA and MsrB domains.
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Protein Domain
IPR036509 | Met_Sox_Rdtase_MsrA_sf
Type: Homologous_superfamily
Description: Peptide methionine sulphoxide reductase (Msr) reverses the inactivation of many proteins due to the oxidation of critical methionine residues by reducing methionine sulphoxide, Met(O), to methionine []. It is present in most living organisms, and the cognate structural gene belongs to the so-called minimum gene set [, ].The domains MsrA and MsrB reduce different epimeric forms of methionine sulphoxide. This group represent MsrA, the crystal structure of which has been determined in a number of organisms. In Mycobacterium tuberculosis, the MsrA structure has been determined to 1.5 Angstrom resolution []. In contrast to the three catalytic cysteine residues found in previously characterised MsrA structures, M. tuberculosis MsrA represents a class containing only two functional cysteine residues. The overall structure shows no resemblance to the structures of MsrB () from other organisms; though the active sites show approximate mirror symmetry. In each case, conserved amino acid motifs mediate the stereo-specific recognition and reduction of the substrate. In a number of pathogenic bacteria including Neisseria gonorrhoeae, the MsrA and MsrB domains are fused; the MsrA being N-terminal to MsrB. This arrangement is reversed in Treponema pallidum. In N. gonorrhoeae and Neisseria meningitidis a thioredoxin domain is fused to the N terminus. This may function to reduce the active sites of the downstream MsrA and MsrB domains.
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Protein
Q9D6Y7
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
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Protein
A0A1B0GT40
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: false
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Publication
12837786 | -
First Author: Taylor AB
Year: 2003
Journal: J Bacteriol
Title: Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine.
Volume: 185
Issue: 14
Pages: 4119-26
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Publication
10841552 | J:62723
First Author: Lowther WT
Year: 2000
Journal: Proc Natl Acad Sci U S A
Title: Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase.
Volume: 97
Issue: 12
Pages: 6463-8
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Publication
8994848 | -
First Author: Koonin EV
Year: 1996
Journal: Curr Opin Genet Dev
Title: Complete genome sequences of cellular life forms: glimpses of theoretical evolutionary genomics.
Volume: 6
Issue: 6
Pages: 757-62
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Publication
8816789 | -
First Author: Mushegian AR
Year: 1996
Journal: Proc Natl Acad Sci U S A
Title: A minimal gene set for cellular life derived by comparison of complete bacterial genomes.
Volume: 93
Issue: 19
Pages: 10268-73
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GO Term
GO:0008113 | peptide-methionine (S)-S-oxide reductase activity
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Protein Domain
IPR002579 | Met_Sox_Rdtase_MsrB_dom
Type: Domain
Description: Peptide methionine sulphoxide reductase (Msr) reverses the inactivation of many proteins due to the oxidation of critical methionine residues by reducing methionine sulphoxide, Met(O), to methionine []. It is present in most living organisms, and the cognate structural gene belongs to the so-called minimum gene set [, ].The domains: MsrA and MsrB, reduce different epimeric forms of methionine sulphoxide. This group represents MsrB, the crystal structure of which has been determined to 1.8A []. The overall structure shows no resemblance to the structures of MsrA () from other organisms; though the active sites show approximate mirror symmetry. In each case, conserved amino acid motifs mediate the stereo-specific recognition and reduction of the substrate. Unlike the MsrA domain, the MsrB domain activates the cysteine or selenocysteine nucleophile through a unique Cys-Arg-Asp/Glu catalytic triad. The collapse of the reaction intermediate most likely results in the formation of a sulphenic or selenenic acid moiety. Regeneration of the active site occurs through a series of thiol-disulphide exchange steps involving another active site Cys residue and thioredoxin.In a number of pathogenic bacteria, including Neisseria gonorrhoeae, the MsrA and MsrB domains are fused; the MsrA being N-terminal to MsrB. This arrangement is reversed in Treponema pallidum. In N. gonorrhoeae and Neisseria meningitidis, a thioredoxin domain is fused to the N terminus. This may function to reduce the active sites of the downstream MsrA and MsrB domains.
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Protein
Q78J03
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: false
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Protein
Q8BU85
Organism: Mus musculus/domesticus
Length: 253  
Fragment?: false
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Protein
A0A0R4J139
Organism: Mus musculus/domesticus
Length: 186  
Fragment?: false
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Protein
D3YUC9
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: false
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Protein
Q9JLC3
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
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Protein
B2RUH3
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
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Publication
11938352 | -
First Author: Lowther WT
Year: 2002
Journal: Nat Struct Biol
Title: The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB.
Volume: 9
Issue: 5
Pages: 348-52
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Publication
27551953 | -
First Author: Han AR
Year: 2016
Journal: Biochemistry
Title: Essential Role of the Linker Region in the Higher Catalytic Efficiency of a Bifunctional MsrA-MsrB Fusion Protein.
Volume: 55
Issue: 36
Pages: 5117-27
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Protein Domain
IPR028427 | Met_Sox_Rdtase_MsrB
Type: Family
Description: The oxidation of methionine residues in proteins is considered to be one of the consequences of oxidative damage to cells, which in many cases leads to the loss of biological activity. Peptide methionine sulphoxide reductase (Msr) reverses the inactivation of many proteins due to the oxidation of critical methionine residues by reducing methionine sulphoxide, (MetO), to methionine []. Methionine (Met) can be oxidised to the R and S diastereomers of methionine sulfoxide (MetO). Methionine sulfoxide reductases A (MsrA) and B (MsrB) reduce MetO back to Met in a stereospecific manner, acting on the S and R forms, respectively. Msr is present in most living organisms [, ].Many bacteria, particularly pathogens, possess methionine sulfoxide reductase MsrA and MsrB as a fusion form (MsrAB) []. This entry includes MsrB and the fusion form of these enzymes.
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Publication
35752173 | J:354665
First Author: He D
Year: 2022
Journal: Mol Cell
Title: Methionine oxidation activates pyruvate kinase M2 to promote pancreatic cancer metastasis.
Volume: 82
Issue: 16
Pages: 3045-3060.e11
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Publication
26318157 | J:226165
First Author: Xu YY
Year: 2015
Journal: J Lipid Res
Title: Hepatic overexpression of methionine sulfoxide reductase A reduces atherosclerosis in apolipoprotein E-deficient mice.
Volume: 56
Issue: 10
Pages: 1891-900
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Publication
33241629 | J:325237
First Author: Wu Y
Year: 2021
Journal: J Cell Mol Med
Title: Acacetin exerts antioxidant potential against atherosclerosis through Nrf2 pathway in apoE-/- Mice.
Volume: 25
Issue: 1
Pages: 521-534
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Publication
18990697 | J:147916
First Author: Fomenko DE
Year: 2009
Journal: J Biol Chem
Title: MsrB1 (methionine-R-sulfoxide reductase 1) knock-out mice: roles of MsrB1 in redox regulation and identification of a novel selenoprotein form.
Volume: 284
Issue: 9
Pages: 5986-93
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Publication
30322141 | J:272366
 
First Author: Marimoutou M
Year: 2018
Journal: Antioxidants (Basel)
Title: Oxidation of Methionine 77 in Calmodulin Alters Mouse Growth and Behavior.
Volume: 7
Issue: 10
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Publication
17105189 | J:116484
First Author: Kim HY
Year: 2006
Journal: Biochemistry
Title: Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases.
Volume: 45
Issue: 46
Pages: 13697-704
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Publication
27838938 | J:318386
First Author: Heo JY
Year: 2017
Journal: Free Radic Res
Title: Methionine sulfoxide reductase B1 deficiency does not increase high-fat diet-induced insulin resistance in mice.
Volume: 51
Issue: 1
Pages: 24-37
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Publication
14699060 | J:90051
First Author: Kim HY
Year: 2004
Journal: Mol Biol Cell
Title: Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases.
Volume: 15
Issue: 3
Pages: 1055-64
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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