Malat dehidrogenase (Malay Wikipedia)

Analysis of information sources in references of the Wikipedia article "Malat dehidrogenase" in Malay language version.

refsWebsite

Global rank Malay rank

22nih.gov

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14^th place

16doi.org

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8^th place

2jbc.org

4,455^th place

4,879^th place

1harvard.edu

18^th place

46^th place

doi.org

"Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD". Journal of Molecular Biology. 285 (2): 703–12. January 1999. doi:10.1006/jmbi.1998.2357. PMID 10075524.
"Molecular evolution within the L-malate and L-lactate dehydrogenase super-family". Journal of Molecular Evolution. 54 (6): 825–40. June 2002. Bibcode:2002JMolE..54..825M. doi:10.1007/s00239-001-0088-8. PMID 12029364.
"Malate dehydrogenase: a model for structure, evolution, and catalysis". Protein Science. 3 (10): 1883–8. October 1994. doi:10.1002/pro.5560031027. PMC 2142602. PMID 7849603.
"Evolutionary relationships among the malate dehydrogenases". Trends in Biochemical Sciences. 13 (5): 178–81. May 1988. doi:10.1016/0968-0004(88)90146-6. PMID 3076279.
"Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui". Biochemistry. 32 (16): 4308–13. April 1993. doi:10.1021/bi00067a020. PMID 8476859.
"Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87 A resolution". Journal of Molecular Biology. 226 (3): 867–82. August 1992. doi:10.1016/0022-2836(92)90637-Y. PMID 1507230.
"Dehydrogenation through the looking-glass". Nature Structural Biology. 1 (5): 281–2. May 1994. doi:10.1038/nsb0594-281. PMID 7664032.
"Studies on the mechanism of the malate dehydrogenase reaction" (PDF). The Journal of Biological Chemistry. 253 (24): 8702–7. December 1978. doi:10.1016/S0021-9258(17)34234-5. PMID 31361.
"The use of genetically engineered tryptophan to identify the movement of a domain of B. stearothermophilus lactate dehydrogenase with the process which limits the steady-state turnover of the enzyme". Biochemical and Biophysical Research Communications. 150 (2): 752–9. January 1988. doi:10.1016/0006-291X(88)90455-X. PMID 3422557.
"Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events". The Journal of Biological Chemistry. 279 (47): 49138–50. November 2004. doi:10.1074/jbc.M404544200. PMID 15358789.
"Mitochondrial malate dehydrogenase and malic enzyme: Mendelian inherited electrophoretic variants in the mouse". Biochemical Genetics. 4 (6): 707–18. December 1970. doi:10.1007/BF00486384. PMID 5496232.
"Subunit interactions in mitochondrial malate dehydrogenase. Kinetics and mechanism of reassociation". The Journal of Biological Chemistry. 256 (5): 2377–82. March 1981. doi:10.1016/S0021-9258(19)69790-5. PMID 7462244.
"Determination of the catalytic mechanism for mitochondrial malate dehydrogenase". Biophysical Journal. 108 (2): 408–19. January 2015. doi:10.1016/j.bpj.2014.11.3467. PMC 4302198. PMID 25606688.
"Malate dehydrogenase of the cytosol. A kinetic investigation of the reaction mechanism and a comparison with lactate dehydrogenase". The Biochemical Journal. 175 (3): 987–98. December 1978. doi:10.1042/bj1750987. PMC 1186162. PMID 217361.
"Kinetic studies of the regulation of mitochondrial malate dehydrogenase by citrate". The Biochemical Journal. 283 ( Pt 1) (Pt 1): 289–97. April 1992. doi:10.1042/bj2830289. PMC 1131027. PMID 1567375.
"Regulation of malate dehydrogenase activity by glutamate, citrate, alpha-ketoglutarate, and multienzyme interaction" (PDF). The Journal of Biological Chemistry. 263 (22): 10687–97. August 1988. doi:10.1016/S0021-9258(18)38026-8. PMID 2899080.

harvard.edu

ui.adsabs.harvard.edu

"Molecular evolution within the L-malate and L-lactate dehydrogenase super-family". Journal of Molecular Evolution. 54 (6): 825–40. June 2002. Bibcode:2002JMolE..54..825M. doi:10.1007/s00239-001-0088-8. PMID 12029364.

jbc.org

"Studies on the mechanism of the malate dehydrogenase reaction" (PDF). The Journal of Biological Chemistry. 253 (24): 8702–7. December 1978. doi:10.1016/S0021-9258(17)34234-5. PMID 31361.
"Regulation of malate dehydrogenase activity by glutamate, citrate, alpha-ketoglutarate, and multienzyme interaction" (PDF). The Journal of Biological Chemistry. 263 (22): 10687–97. August 1988. doi:10.1016/S0021-9258(18)38026-8. PMID 2899080.

nih.gov

pubmed.ncbi.nlm.nih.gov

"Malate dehydrogenases--structure and function". General Physiology and Biophysics. 21 (3): 257–65. September 2002. PMID 12537350.
"Malate dehydrogenase: distribution, function and properties". General Physiology and Biophysics. 17 (3): 193–210. September 1998. PMID 9834842.
"Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD". Journal of Molecular Biology. 285 (2): 703–12. January 1999. doi:10.1006/jmbi.1998.2357. PMID 10075524.
"Molecular evolution within the L-malate and L-lactate dehydrogenase super-family". Journal of Molecular Evolution. 54 (6): 825–40. June 2002. Bibcode:2002JMolE..54..825M. doi:10.1007/s00239-001-0088-8. PMID 12029364.
"Malate dehydrogenase: a model for structure, evolution, and catalysis". Protein Science. 3 (10): 1883–8. October 1994. doi:10.1002/pro.5560031027. PMC 2142602. PMID 7849603.
"Evolutionary relationships among the malate dehydrogenases". Trends in Biochemical Sciences. 13 (5): 178–81. May 1988. doi:10.1016/0968-0004(88)90146-6. PMID 3076279.
"Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui". Biochemistry. 32 (16): 4308–13. April 1993. doi:10.1021/bi00067a020. PMID 8476859.
"Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87 A resolution". Journal of Molecular Biology. 226 (3): 867–82. August 1992. doi:10.1016/0022-2836(92)90637-Y. PMID 1507230.
"Dehydrogenation through the looking-glass". Nature Structural Biology. 1 (5): 281–2. May 1994. doi:10.1038/nsb0594-281. PMID 7664032.
"Studies on the mechanism of the malate dehydrogenase reaction" (PDF). The Journal of Biological Chemistry. 253 (24): 8702–7. December 1978. doi:10.1016/S0021-9258(17)34234-5. PMID 31361.
"The use of genetically engineered tryptophan to identify the movement of a domain of B. stearothermophilus lactate dehydrogenase with the process which limits the steady-state turnover of the enzyme". Biochemical and Biophysical Research Communications. 150 (2): 752–9. January 1988. doi:10.1016/0006-291X(88)90455-X. PMID 3422557.
"Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events". The Journal of Biological Chemistry. 279 (47): 49138–50. November 2004. doi:10.1074/jbc.M404544200. PMID 15358789.
"Mitochondrial malate dehydrogenase and malic enzyme: Mendelian inherited electrophoretic variants in the mouse". Biochemical Genetics. 4 (6): 707–18. December 1970. doi:10.1007/BF00486384. PMID 5496232.
"Subunit interactions in mitochondrial malate dehydrogenase. Kinetics and mechanism of reassociation". The Journal of Biological Chemistry. 256 (5): 2377–82. March 1981. doi:10.1016/S0021-9258(19)69790-5. PMID 7462244.
"Determination of the catalytic mechanism for mitochondrial malate dehydrogenase". Biophysical Journal. 108 (2): 408–19. January 2015. doi:10.1016/j.bpj.2014.11.3467. PMC 4302198. PMID 25606688.
"Malate dehydrogenase of the cytosol. A kinetic investigation of the reaction mechanism and a comparison with lactate dehydrogenase". The Biochemical Journal. 175 (3): 987–98. December 1978. doi:10.1042/bj1750987. PMC 1186162. PMID 217361.
"Kinetic studies of the regulation of mitochondrial malate dehydrogenase by citrate". The Biochemical Journal. 283 ( Pt 1) (Pt 1): 289–97. April 1992. doi:10.1042/bj2830289. PMC 1131027. PMID 1567375.
"Regulation of malate dehydrogenase activity by glutamate, citrate, alpha-ketoglutarate, and multienzyme interaction" (PDF). The Journal of Biological Chemistry. 263 (22): 10687–97. August 1988. doi:10.1016/S0021-9258(18)38026-8. PMID 2899080.

ncbi.nlm.nih.gov

"Malate dehydrogenase: a model for structure, evolution, and catalysis". Protein Science. 3 (10): 1883–8. October 1994. doi:10.1002/pro.5560031027. PMC 2142602. PMID 7849603.
"Determination of the catalytic mechanism for mitochondrial malate dehydrogenase". Biophysical Journal. 108 (2): 408–19. January 2015. doi:10.1016/j.bpj.2014.11.3467. PMC 4302198. PMID 25606688.
"Malate dehydrogenase of the cytosol. A kinetic investigation of the reaction mechanism and a comparison with lactate dehydrogenase". The Biochemical Journal. 175 (3): 987–98. December 1978. doi:10.1042/bj1750987. PMC 1186162. PMID 217361.
"Kinetic studies of the regulation of mitochondrial malate dehydrogenase by citrate". The Biochemical Journal. 283 ( Pt 1) (Pt 1): 289–97. April 1992. doi:10.1042/bj2830289. PMC 1131027. PMID 1567375.