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149 related items for PubMed ID: 23954635
1. The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase. Miyanaga A, Fujisawa S, Furukawa N, Arai K, Nakajima M, Taguchi H. Biochem Biophys Res Commun; 2013 Sep 13; 439(1):109-14. PubMed ID: 23954635 [Abstract] [Full Text] [Related]
2. A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases. Wada Y, Iwai S, Tamura Y, Ando T, Shinoda T, Arai K, Taguchi H. Biosci Biotechnol Biochem; 2008 Apr 13; 72(4):1087-94. PubMed ID: 18391442 [Abstract] [Full Text] [Related]
3. The ternary complex structure of d-mandelate dehydrogenase with NADH and anilino(oxo)acetate. Furukawa N, Miyanaga A, Nakajima M, Taguchi H. Biochem Biophys Res Commun; 2017 May 06; 486(3):665-670. PubMed ID: 28327357 [Abstract] [Full Text] [Related]
4. Crystal structure of Escherichia coli ketopantoate reductase at 1.7 A resolution and insight into the enzyme mechanism. Matak-Vinković D, Vinković M, Saldanha SA, Ashurst JL, von Delft F, Inoue T, Miguel RN, Smith AG, Blundell TL, Abell C. Biochemistry; 2001 Dec 04; 40(48):14493-500. PubMed ID: 11724562 [Abstract] [Full Text] [Related]
5. Identification and characterization of an archaeal ketopantoate reductase and its involvement in regulation of coenzyme A biosynthesis. Tomita H, Imanaka T, Atomi H. Mol Microbiol; 2013 Oct 04; 90(2):307-21. PubMed ID: 23941541 [Abstract] [Full Text] [Related]
6. Crystal structure of Escherichia coli ketopantoate reductase in a ternary complex with NADP+ and pantoate bound: substrate recognition, conformational change, and cooperativity. Ciulli A, Chirgadze DY, Smith AG, Blundell TL, Abell C. J Biol Chem; 2007 Mar 16; 282(11):8487-97. PubMed ID: 17229734 [Abstract] [Full Text] [Related]
7. Structural insights into the enzyme mechanism of a new family of d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate reductase. Mondal S, Mizuguchi K. Genome Inform; 2009 Oct 16; 23(1):98-105. PubMed ID: 20180265 [Abstract] [Full Text] [Related]
8. A new D-2-hydroxyacid dehydrogenase with dual coenzyme-specificity from Haloferax mediterranei, sequence analysis and heterologous overexpression. Domenech J, Ferrer J. Biochim Biophys Acta; 2006 Nov 16; 1760(11):1667-74. PubMed ID: 17049749 [Abstract] [Full Text] [Related]
9. Evidence of Kinetic Cooperativity in Dimeric Ketopantoate Reductase from Staphylococcus aureus. Sanchez JE, Gross PG, Goetze RW, Walsh RM, Peeples WB, Wood ZA. Biochemistry; 2015 Jun 02; 54(21):3360-3369. PubMed ID: 25946571 [Abstract] [Full Text] [Related]
10. The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound. Lobley CM, Ciulli A, Whitney HM, Williams G, Smith AG, Abell C, Blundell TL. Biochemistry; 2005 Jun 28; 44(25):8930-9. PubMed ID: 15966718 [Abstract] [Full Text] [Related]
11. Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase. Zhang T, Koshland DE. Protein Sci; 1995 Jan 28; 4(1):84-92. PubMed ID: 7773180 [Abstract] [Full Text] [Related]
12. Crystal structure of archaeal ketopantoate reductase complexed with coenzyme a and 2-oxopantoate provides structural insights into feedback regulation. Aikawa Y, Nishitani Y, Tomita H, Atomi H, Miki K. Proteins; 2016 Mar 28; 84(3):374-82. PubMed ID: 26757028 [Abstract] [Full Text] [Related]
13. Detecting subtle functional differences in ketopantoate reductase and related enzymes using a rule-based approach with sequence-structure homology recognition scores. Mondal S, Nagao C, Mizuguchi K. Protein Eng Des Sel; 2010 Nov 28; 23(11):859-69. PubMed ID: 20876192 [Abstract] [Full Text] [Related]