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1 to 21 of 21  Show
  1. 1
    "Isolation of a cDNA encoding the rat liver S-adenosylmethionine synthetase."
    Horikawa S., Ishikawa M., Ozasa H., Tsukada K.
    Eur. J. Biochem. 184:497-501(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Category: Expression, Sequences.
    Strain: Wistar.
    Tissue: Liver.
    Source: UniProtKB/Swiss-Prot (reviewed).
  2. 2
    "Analysis of the 5' non-coding region of rat liver S-adenosylmethionine synthetase mRNA and comparison of the Mr deduced from the cDNA sequence and the purified enzyme."
    Alvarez L., Asuncion M., Corrales F., Pajares M.A., Mato J.M.
    FEBS Lett. 290:142-146(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  3. 3
    "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Category: Sequences.
    Tissue: Spleen.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 50446 other entries.

  4. 4
    "Modulation of rat liver S-adenosylmethionine synthetase activity by glutathione."
    Pajares M.A., Duran C., Corrales F., Pliego M.M., Mato J.M.
    J. Biol. Chem. 267:17598-17605(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, PATHWAY, TISSUE SPECIFICITY.
    Category: Function, Expression, Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).
  5. 5
    "Nitric oxide inactivates rat hepatic methionine adenosyltransferase In vivo by S-nitrosylation."
    Ruiz F., Corrales F.J., Miqueo C., Mato J.M.
    Hepatology 28:1051-1057(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, PATHWAY.
    Category: Function, PTM / Processing, Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).
  6. 6
    "Methionine adenosyltransferase S-nitrosylation is regulated by the basic and acidic amino acids surrounding the target thiol."
    Perez-Mato I., Castro C., Ruiz F.A., Corrales F.J., Mato J.M.
    J. Biol. Chem. 274:17075-17079(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION AT CYS-121.
    Category: PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).
  7. 7
    "Assignment of a single disulfide bridge in rat liver methionine adenosyltransferase."
    Martinez-Chantar M.L., Pajares M.A.
    Eur. J. Biochem. 267:132-137(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND.
    Category: PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).
  8. 8
    "The crystal structure of tetrameric methionine adenosyltransferase from rat liver reveals the methionine-binding site."
    Gonzalez B., Pajares M.A., Hermoso J.A., Alvarez L., Garrido F., Sufrin J.R., Sanz-Aparicio J.
    J. Mol. Biol. 300:363-375(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) IN COMPLEX WITH METHIONINE ANALOG; POTASSIUM AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, MUTAGENESIS OF ASP-180; LYS-182 AND PHE-251, DISULFIDE BOND.
    Category: Function, Pathology & Biotech, PTM / Processing, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is mapped to 1 other entry.

  9. 9
    "Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism."
    Gonzalez B., Pajares M.A., Hermoso J.A., Guillerm D., Guillerm G., Sanz-Aparicio J.
    J. Mol. Biol. 331:407-416(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEXES WITH ATP; METHIONINE POTASSIUM AND MAGNESIUM, SUBUNIT.
    Category: Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is mapped to 1 other entry.

  10. 10
    "Changes in methionine adenosyltransferase and S-adenosylmethionine homeostasis in alcoholic rat liver."
    Lu S.C., Huang Z.Z., Yang H., Mato J.M., Avila M.A., Tsukamoto H.
    Am. J. Physiol. Gastrointest. Liver Physiol. 279:G178-85(2000) [PubMed] [Europe PMC] [Abstract]
    Category: Function, Subcellular Location.
    Source: RGD:3050.

    This publication is mapped to 5 other entries.

  11. 11
    "Role of an intrasubunit disulfide in the association state of the cytosolic homo-oligomer methionine adenosyltransferase."
    Sanchez-Perez G.F., Gasset M., Calvete J.J., Pajares M.A.
    J. Biol. Chem. 278:7285-7293(2003) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Annotation: role of an intrasubunit disulfide in the association state; residues involved in this disulfide have been identified by mass spectrometry and using a set of single cysteine mutants as cysteines 35 and 61.
    Source: GeneRIF:25331.
  12. 12
    "Proteomics reveal a concerted upregulation of methionine metabolic pathway enzymes, and downregulation of carbonic anhydrase-III, in betaine supplemented ethanol-fed rats."
    Kharbanda K.K., Vigneswara V., McVicker B.L., Newlaczyl A.U., Bailey K., Tuma D., Ray D.E., Carter W.G.
    Biochem. Biophys. Res. Commun. 381:523-527(2009) [PubMed] [Europe PMC] [Abstract]
    Category: Subcellular Location.
    Source: RGD:3050.

    This publication is mapped to 6 other entries.

  13. 13
    "Conformational signals in the C-terminal domain of methionine adenosyltransferase I/III determine its nucleocytoplasmic distribution."
    Reytor E., Perez-Miguelsanz J., Alvarez L., Perez-Sala D., Pajares M.A.
    FASEB J. 23:3347-3360(2009) [PubMed] [Europe PMC] [Abstract]
    Category: Function, Subcellular Location, Interaction.
    Annotation: In this work methionine adenosyltransferase I/III was identified in most rat tissues both in the cytoplasm and the nucleus. [GeneRIF:25331].
    Source: RGD:3050, GeneRIF:25331.

    This publication is mapped to 2 other entries.

  14. 14
    Category: Expression.
    Annotation: Data support a role for AUF1 and HuR/methyl-HuR in liver de-differentiation and development through the posttranslational regulation of MAT1A and MAT2A mRNAs.
    Source: GeneRIF:25331.

    This publication is mapped to 7 other entries.

  15. 15
    "Role of epigenetic and miR-22 and miR-29b alterations in the downregulation of Mat1a and Mthfr genes in early preneoplastic livers in rats induced by 2-acetylaminofluorene."
    Koturbash I., Melnyk S., James S.J., Beland F.A., Pogribny I.P.
    Mol. Carcinog. 52:318-327(2013) [PubMed] [Europe PMC] [Abstract]
    Category: Expression.
    Annotation: Mat1a and Mthfr genes were downregulated during early stages of rat 2-acetylaminofluorene-induced liver carcinogenesis.
    Source: GeneRIF:25331.

    This publication is mapped to 1 other entry.

  16. 16
    "Role of transcriptional and posttranscriptional regulation of methionine adenosyltransferases in liver cancer progression."
    Frau M., Tomasi M.L., Simile M.M., Demartis M.I., Salis F., Latte G., Calvisi D.F., Seddaiu M.A., Daino L., Feo C.F., Brozzetti S., Solinas G., Yamashita S., Ushijima T., Feo F., Pascale R.M.
    Hepatology 56:165-175(2012) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: we found for the first time a post-transcriptional regulation of MAT1A and MAT2A by AUF1 and HuR in hepatocellular carcinoma.
    Source: GeneRIF:25331.

    This publication is mapped to 9 other entries.

  17. 17
    "The Oncogene PDRG1 Is an Interaction Target of Methionine Adenosyltransferases."
    Perez C., Perez-Zuniga F.J., Garrido F., Reytor E., Portillo F., Pajares M.A.
    PLoS ONE 11:e0161672-e0161672(2016) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Annotation: The oncogene PDRG1 is an interaction target of methionine adenosyltransferases.
    Source: GeneRIF:25331.

    This publication is mapped to 1 other entry.

  18. 18
    "Purification and comparison of two forms of S-adenosyl-L-methionine synthetase from rat liver."
    Cabrero C., Puerta J., Alemany S.
    Eur. J. Biochem. 170:299-304(1987) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Source: BioCyc:MetaCyc:MONOMER-8568.
  19. 19
    "Protein kinase C phosphorylation of rat liver S-adenosylmethionine synthetase: dissociation and production of an active monomer."
    Pajares M.A., Duran C., Corrales F., Mato J.M.
    Biochem. J. 303:949-955(1994) [PubMed] [Europe PMC] [Abstract]
    Category: PTM / Processing.
    Annotation: Phosphorylation. [iPTMnet:P13444].
    Source: iPTMnet:P13444, PhosphoSitePlus:P13444.
  20. 20
    "Expression of rat liver S-adenosylmethionine synthetase in Escherichia coli results in two active oligomeric forms."
    Alvarez L., Mingorance J., Pajares M.A., Mato J.M.
    Biochem. J. 301:557-561(1994) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:1QM4.
  21. 21
    "Recombinant rat liver S-adenosyl-L-methionine synthetase tetramers and dimers are in equilibrium."
    Mingorance J., Alvarez L., Pajares M.A., Mato J.M.
    Int. J. Biochem. Cell Biol. 29:485-491(1997) [PubMed] [Europe PMC] [Abstract]
    Category: Function, Interaction.
    Source: RGD:3050.

    This publication is mapped to 2 other entries.

1 to 21 of 21  Show
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