| Year |
Citation |
Score |
| 2009 |
Garza JA, Ilangovan U, Hinck AP, Barnes LD. Kinetic, dynamic, ligand binding properties, and structural models of a dual-substrate specific nudix hydrolase from Schizosaccharomyces pombe. Biochemistry. 48: 6224-39. PMID 19462967 DOI: 10.1021/Bi802266G |
0.368 |
|
| 2009 |
Pichiorri F, Okumura H, Nakamura T, Garrison PN, Gasparini P, Suh SS, Druck T, McCorkell KA, Barnes LD, Croce CM, Huebner K. Correlation of fragile histidine triad (Fhit) protein structural features with effector interactions and biological functions. The Journal of Biological Chemistry. 284: 1040-9. PMID 19004824 DOI: 10.1074/Jbc.M806638200 |
0.378 |
|
| 2006 |
Semba S, Trapasso F, Fabbri M, McCorkell KA, Volinia S, Druck T, Iliopoulos D, Pekarsky Y, Ishii H, Garrison PN, Barnes LD, Croce CM, Huebner K. Fhit modulation of the Akt-survivin pathway in lung cancer cells: Fhit-tyrosine 114 (Y114) is essential. Oncogene. 25: 2860-72. PMID 16407838 DOI: 10.1038/Sj.Onc.1209323 |
0.332 |
|
| 2005 |
Garrison PN, Robinson AK, Pekarsky Y, Croce CM, Barnes LD. Phosphorylation of the human Fhit tumor suppressor on tyrosine 114 in Escherichia coli and unexpected steady state kinetics of the phosphorylated forms. Biochemistry. 44: 6286-92. PMID 15835917 DOI: 10.1021/Bi047670S |
0.372 |
|
| 2004 |
Pekarsky Y, Garrison PN, Palamarchuk A, Zanesi N, Aqeilan RI, Huebner K, Barnes LD, Croce CM. Fhit is a physiological target of the protein kinase Src. Proceedings of the National Academy of Sciences of the United States of America. 101: 3775-9. PMID 15007172 DOI: 10.1073/Pnas.0400481101 |
0.334 |
|
| 2003 |
Hua LV, Hidaka K, Pesesse X, Barnes LD, Shears SB. Paralogous murine Nudt10 and Nudt11 genes have differential expression patterns but encode identical proteins that are physiologically competent diphosphoinositol polyphosphate phosphohydrolases. The Biochemical Journal. 373: 81-9. PMID 12689335 DOI: 10.1042/Bj20030142 |
0.352 |
|
| 2003 |
Ingram SW, Safrany ST, Barnes LD. Disruption and overexpression of the Schizosaccharomyces pombe aps1 gene, and effects on growth rate, morphology and intracellular diadenosine 5',5"'-P1,P5-pentaphosphate and diphosphoinositol polyphosphate concentrations. The Biochemical Journal. 369: 519-28. PMID 12387729 DOI: 10.1042/Bj20020733 |
0.722 |
|
| 2002 |
Hidaka K, Caffrey JJ, Hua L, Zhang T, Falck JR, Nickel GC, Carrel L, Barnes LD, Shears SB. An adjacent pair of human NUDT genes on chromosome X are preferentially expressed in testis and encode two new isoforms of diphosphoinositol polyphosphate phosphohydrolase. The Journal of Biological Chemistry. 277: 32730-8. PMID 12105228 DOI: 10.1074/Jbc.M205476200 |
0.407 |
|
| 2002 |
Bieganowski P, Garrison PN, Hodawadekar SC, Faye G, Barnes LD, Brenner C. Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3. The Journal of Biological Chemistry. 277: 10852-60. PMID 11805111 DOI: 10.1074/Jbc.M111480200 |
0.407 |
|
| 2001 |
McLennan AG, Barnes LD, Blackburn GM, Brenner C, Guranowski A, Miller AD, Rovira JM, Rotllán P, Soria B, Tanner JA, Sillero A. Recent progress in the study of the intracellular functions of diadenosine polyphosphates Drug Development Research. 52: 249-259. DOI: 10.1002/Ddr.1122 |
0.405 |
|
| 2000 |
Ingram SW, Barnes LD. Disruption and overexpression of the Schizosaccharomyces pombe aph1 gene and the effects on intracellular diadenosine 5',5'''-P1, P4-tetraphosphate (Ap4A), ATP and ADP concentrations. The Biochemical Journal. 350: 663-9. PMID 10970777 DOI: 10.1042/Bj3500663 |
0.729 |
|
| 1999 |
Chaudhuri AR, Khan IA, Prasad V, Robinson AK, Ludueña RF, Barnes LD. The tumor suppressor protein Fhit. A novel interaction with tubulin. The Journal of Biological Chemistry. 274: 24378-82. PMID 10446217 DOI: 10.1074/Jbc.274.34.24378 |
0.389 |
|
| 1999 |
Safrany ST, Ingram SW, Cartwright JL, Falck JR, McLennan AG, Barnes LD, Shears SB. The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein. The Journal of Biological Chemistry. 274: 21735-40. PMID 10419486 DOI: 10.1074/Jbc.274.31.21735 |
0.727 |
|
| 1999 |
Abend A, Garrison PN, Barnes LD, Frey PA. Stereochemical retention of the configuration in the action of Fhit on phosphorus-chiral substrates. Biochemistry. 38: 3668-76. PMID 10090754 DOI: 10.1021/Bi981895J |
0.426 |
|
| 1999 |
Ingram SW, Stratemann SA, Barnes LD. Schizosaccharomyces pombe Aps1, a diadenosine 5',5' "-P1, P6-hexaphosphate hydrolase that is a member of the nudix (MutT) family of hydrolases: cloning of the gene and characterization of the purified enzyme. Biochemistry. 38: 3649-55. PMID 10090752 DOI: 10.1021/Bi982951J |
0.737 |
|
| 1998 |
Huebner K, Garrison PN, Barnes LD, Croce CM. The role of the FHIT/FRA3B locus in cancer. Annual Review of Genetics. 32: 7-31. PMID 9928473 DOI: 10.1146/Annurev.Genet.32.1.7 |
0.318 |
|
| 1998 |
Pace HC, Garrison PN, Robinson AK, Barnes LD, Draganescu A, Rösler A, Blackburn GM, Siprashvili Z, Croce CM, Huebner K, Brenner C. Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit. Proceedings of the National Academy of Sciences of the United States of America. 95: 5484-9. PMID 9576908 DOI: 10.1073/Pnas.95.10.5484 |
0.454 |
|
| 1998 |
Guranowski A, Starzyńska E, Barnes LD, Robinson AK, Liu S. Adenosine 5'-tetraphosphate phosphohydrolase activity is an inherent property of soluble exopolyphosphatase from yeast Saccharomyces cerevisiae. Biochimica Et Biophysica Acta. 1380: 232-8. PMID 9565693 DOI: 10.1016/S0304-4165(97)00147-5 |
0.365 |
|
| 1997 |
Brenner C, Pace HC, Garrison PN, Robinson AK, Rosler A, Liu XH, Blackburn GM, Croce CM, Huebner K, Barnes LD. Purification and crystallization of complexes modeling the active state of the fragile histidine triad protein. Protein Engineering. 10: 1461-3. PMID 9543008 DOI: 10.1093/Protein/10.12.1461 |
0.385 |
|
| 1997 |
Siprashvili Z, Sozzi G, Barnes LD, McCue P, Robinson AK, Eryomin V, Sard L, Tagliabue E, Greco A, Fusetti L, Schwartz G, Pierotti MA, Croce CM, Huebner K. Replacement of Fhit in cancer cells suppresses tumorigenicity. Proceedings of the National Academy of Sciences of the United States of America. 94: 13771-6. PMID 9391102 DOI: 10.1073/Pnas.94.25.13771 |
0.376 |
|
| 1997 |
Ingrain SW, Barnes LD. Ap4a degradative enzymes in the fission yeast schizosaccharomyces pombe Faseb Journal. 11. |
0.314 |
|
| 1996 |
Barnes LD, Garrison PN, Siprashvili Z, Guranowski A, Robinson AK, Ingram SW, Croce CM, Ohta M, Huebner K. Fhit, a putative tumor suppressor in humans, is a dinucleoside 5',5"'-P1,P3-triphosphate hydrolase. Biochemistry. 35: 11529-35. PMID 8794732 DOI: 10.1021/Bi961415T |
0.726 |
|
| 1995 |
Huang Y, Garrison PN, Barnes LD. Cloning of the Schizosaccharomyces pombe gene encoding diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) asymmetrical hydrolase: sequence similarity with the histidine triad (HIT) protein family. The Biochemical Journal. 312: 925-32. PMID 8554540 DOI: 10.1042/Bj3120925 |
0.428 |
|
| 1993 |
Robinson AK, de la Peña CE, Barnes LD. Isolation and characterization of diadenosine tetraphosphate (Ap4A) hydrolase from Schizosaccharomyces pombe. Biochimica Et Biophysica Acta. 1161: 139-48. PMID 8381667 DOI: 10.1016/0167-4838(93)90207-8 |
0.474 |
|
| 1993 |
Garrison PN, de la Peña CE, Barnes LD. Synthesis and use of a chromogenic substrate analog for Ap4A catabolic enzymes. Analytical Biochemistry. 210: 226-30. PMID 7685562 DOI: 10.1006/Abio.1993.1187 |
0.48 |
|
| 1991 |
Avila DM, Robinson AK, Kaushal V, Barnes LD. A paradoxical increase of a metabolite upon increased expression of its catabolic enzyme: the case of diadenosine tetraphosphate (Ap4A) and Ap4A phosphorylase I in Saccharomyces cerevisiae. Journal of Bacteriology. 173: 7875-80. PMID 1660456 DOI: 10.1128/Jb.173.24.7875-7880.1991 |
0.462 |
|
| 1991 |
Robinson AK, Barnes LD. Chemical modification of a functional arginine residue in diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) phosphorylase I from Saccharomyces cerevisiae. The Biochemical Journal. 279: 135-9. PMID 1656937 DOI: 10.1042/Bj2790135 |
0.48 |
|
| 1990 |
Kaushal V, Avila DM, Hardies SC, Barnes LD. Sequencing and enhanced expression of the gene encoding diadenosine 5',5'''-P1, P4-tetraphosphate (Ap4A) phosphorylase in Saccharomyces cerevisiae. Gene. 95: 79-84. PMID 2174812 DOI: 10.1016/0378-1119(90)90416-O |
0.392 |
|
| 1990 |
Avila DM, Kaushal V, Barnes LD. Immunoaffinity chromatography of diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase from Saccharomyces cerevisiae. Biotechnology and Applied Biochemistry. 12: 276-83. PMID 2163260 DOI: 10.1111/J.1470-8744.1990.Tb00100.X |
0.406 |
|
| 1986 |
Robinson AK, Barnes LD. Three diadenosine 5',5''-P1,P4-tetraphosphate hydrolytic enzymes from Physarum polycephalum with differential effects by calcium: a specific dinucleoside polyphosphate pyrophosphohydrolase, a nucleotide pyrophosphatase, and a phosphodiesterase. Archives of Biochemistry and Biophysics. 248: 502-15. PMID 3017212 DOI: 10.1016/0003-9861(86)90503-5 |
0.457 |
|
| 1985 |
Barnes LD, Robinson AK, Mumford CH, Garrison PN. Assay of diadenosine tetraphosphate hydrolytic enzymes by boronate chromatography. Analytical Biochemistry. 144: 296-304. PMID 2984957 DOI: 10.1016/0003-2697(85)90120-4 |
0.421 |
|
| 1982 |
Garrison PN, Roberson GM, Culver CA, Barnes LD. Diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase from Physarum polycephalum. Substrate specificity. Biochemistry. 21: 6129-33. PMID 6295457 DOI: 10.1021/Bi00267A016 |
0.454 |
|
| 1982 |
Barnes LD, Culver CA. Isolation and characterization of diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase from Physarum polycephalum. Biochemistry. 21: 6123-8. PMID 6295456 DOI: 10.1021/Bi00267A015 |
0.47 |
|
| 1980 |
Garrison PN, Barnes LD. Cyclic AMP in the cell cycle of Physarum polycephalum. Biochimica Et Biophysica Acta. 633: 114-21. PMID 6256004 DOI: 10.1016/0304-4165(80)90043-4 |
0.303 |
|
| 1979 |
Barnes LD, Roberson GM. Tubulin and microtubules from bovine kidney: purification, properties, and characterization of ligand binding. Archives of Biochemistry and Biophysics. 196: 511-24. PMID 485163 DOI: 10.1016/0003-9861(79)90303-5 |
0.322 |
|
| 1975 |
Barnes LD, Hui YS, Frohnert PP, Dousa TP. Subcellular distribution of the enzymes related to the cellular action of vasopressin in renal medulla. Endocrinology. 96: 119-28. PMID 162875 DOI: 10.1210/endo-96-1-119 |
0.31 |
|
| 1973 |
Stellwagen E, Cronlund MM, Barnes LD. A thermostable enolase from the extreme thermophile Thermus aquaticus YT-1. Biochemistry. 12: 1552-9. PMID 4699989 DOI: 10.1021/Bi00732A014 |
0.304 |
|
| 1972 |
Barnes LD, McGuire JJ, Atkinson DE. Yeast diphosphopyridine nucleotide specific isocitrate dehydrogenase. Regulation of activity and unidirectional catalysis. Biochemistry. 11: 4322-9. PMID 4342903 DOI: 10.1021/Bi00773A019 |
0.372 |
|
| 1971 |
Barnes LD, Kuehn GD, Atkinson DE. Yeast diphosphopyridine nucleotide specific isocitrate dehydrogenase. Purification and some properties. Biochemistry. 10: 3939-44. PMID 4334283 DOI: 10.1021/Bi00797A022 |
0.349 |
|
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