| Year |
Citation |
Score |
| 2013 |
Mukhopadhyay A, Wei B, Weiner H. Mitochondrial NAD dependent aldehyde dehydrogenase either from yeast or human replaces yeast cytoplasmic NADP dependent aldehyde dehydrogenase for the aerobic growth of yeast on ethanol. Biochimica Et Biophysica Acta. 1830: 3391-8. PMID 23454351 DOI: 10.1016/J.Bbagen.2013.02.010 |
0.315 |
|
| 2013 |
González-Segura L, Ho KK, Perez-Miller S, Weiner H, Hurley TD. Catalytic contribution of threonine 244 in human ALDH2. Chemico-Biological Interactions. 202: 32-40. PMID 23295226 DOI: 10.1016/J.Cbi.2012.12.009 |
0.367 |
|
| 2009 |
Long MC, Nagegowda DA, Kaminaga Y, Ho KK, Kish CM, Schnepp J, Sherman D, Weiner H, Rhodes D, Dudareva N. Involvement of snapdragon benzaldehyde dehydrogenase in benzoic acid biosynthesis. The Plant Journal : For Cell and Molecular Biology. 59: 256-65. PMID 19292760 DOI: 10.1111/J.1365-313X.2009.03864.X |
0.31 |
|
| 2008 |
Ho KK, Mukhopadhyay A, Li YF, Mukhopadhyay S, Weiner H. A point mutation produced a class 3 aldehyde dehydrogenase with increased protective ability against the killing effect of cyclophosphamide. Biochemical Pharmacology. 76: 690-6. PMID 18647600 DOI: 10.1016/J.Bcp.2008.06.018 |
0.368 |
|
| 2007 |
Mukhopadhyay A, Yang CS, Wei B, Weiner H. Precursor protein is readily degraded in mitochondrial matrix space if the leader is not processed by mitochondrial processing peptidase. The Journal of Biological Chemistry. 282: 37266-75. PMID 17959599 DOI: 10.1074/Jbc.M706594200 |
0.354 |
|
| 2007 |
Wenzel P, Oelze M, Coldewey M, Hortmann M, Seeling A, Hink U, Mollnau H, Stalleicken D, Weiner H, Lehmann J, Li H, Förstermann U, Münzel T, Daiber A. Heme oxygenase-1: a novel key player in the development of tolerance in response to organic nitrates. Arteriosclerosis, Thrombosis, and Vascular Biology. 27: 1729-35. PMID 17541025 DOI: 10.1161/Atvbaha.107.143909 |
0.313 |
|
| 2007 |
Larson HN, Zhou J, Chen Z, Stamler JS, Weiner H, Hurley TD. Structural and functional consequences of coenzyme binding to the inactive asian variant of mitochondrial aldehyde dehydrogenase: roles of residues 475 and 487. The Journal of Biological Chemistry. 282: 12940-50. PMID 17327228 DOI: 10.1074/Jbc.M607959200 |
0.575 |
|
| 2007 |
Wenzel P, Hink U, Oelze M, Schuppan S, Schaeuble K, Schildknecht S, Ho KK, Weiner H, Bachschmid M, Münzel T, Daiber A. Role of reduced lipoic acid in the redox regulation of mitochondrial aldehyde dehydrogenase (ALDH-2) activity. Implications for mitochondrial oxidative stress and nitrate tolerance. The Journal of Biological Chemistry. 282: 792-9. PMID 17102135 DOI: 10.1074/Jbc.M606477200 |
0.358 |
|
| 2006 |
Mukhopadhyay A, Yang CS, Weiner H. Binding of mitochondrial leader sequences to Tom20 assessed using a bacterial two-hybrid system shows that hydrophobic interactions are essential and that some mutated leaders that do not bind Tom20 can still be imported. Protein Science : a Publication of the Protein Society. 15: 2739-48. PMID 17088320 DOI: 10.1110/Ps.062462006 |
0.324 |
|
| 2006 |
Ho KK, Hurley TD, Weiner H. Selective alteration of the rate-limiting step in cytosolic aldehyde dehydrogenase through random mutagenesis. Biochemistry. 45: 9445-53. PMID 16878979 DOI: 10.1021/Bi060718C |
0.352 |
|
| 2006 |
Rodríguez-Zavala JS, Allali-Hassani A, Weiner H. Characterization of E. coli tetrameric aldehyde dehydrogenases with atypical properties compared to other aldehyde dehydrogenases. Protein Science : a Publication of the Protein Society. 15: 1387-96. PMID 16731973 DOI: 10.1110/Ps.052039606 |
0.384 |
|
| 2006 |
Mukhopadhyay A, Zullo SJ, Weiner H. Factors that might affect the allotopic replacement of a damaged mitochondrial DNA-encoded protein. Rejuvenation Research. 9: 182-90. PMID 16706640 DOI: 10.1089/Rej.2006.9.182 |
0.303 |
|
| 2005 |
Ho KK, Allali-Hassani A, Hurley TD, Weiner H. Differential effects of Mg2+ ions on the individual kinetic steps of human cytosolic and mitochondrial aldehyde dehydrogenases. Biochemistry. 44: 8022-9. PMID 15924421 DOI: 10.1021/Bi050038U |
0.302 |
|
| 2005 |
Ho KK, Weiner H. Isolation and characterization of an aldehyde dehydrogenase encoded by the aldB gene of Escherichia coli. Journal of Bacteriology. 187: 1067-73. PMID 15659684 DOI: 10.1128/Jb.187.3.1067-1073.2005 |
0.417 |
|
| 2005 |
Oyama T, Isse T, Kagawa N, Kinaga T, Kim YD, Morita M, Sugio K, Weiner H, Yasumoto K, Kawamoto T. Tissue-distribution of aldehyde dehydrogenase 2 and effects of the ALDH2 gene-disruption on the expression of enzymes involved in alcohol metabolism. Frontiers in Bioscience : a Journal and Virtual Library. 10: 951-60. PMID 15569633 DOI: 10.2741/1589 |
0.317 |
|
| 2004 |
Mukhopadhyay A, Ni L, Weiner H. A co-translational model to explain the in vivo import of proteins into HeLa cell mitochondria. The Biochemical Journal. 382: 385-92. PMID 15153070 DOI: 10.1042/Bj20040065 |
0.331 |
|
| 2003 |
Wei B, Mays DC, Lipsky JJ, Weiner H. Chemical modifications to study mutations that affect the ability of the general base (E268) to function in human liver mitochondrial aldehyde dehydrogenase. Chemico-Biological Interactions. 143: 85-91. PMID 12604192 DOI: 10.1016/S0009-2797(02)00177-1 |
0.432 |
|
| 2003 |
Mukhopadhyay A, Heard TS, Wen X, Hammen PK, Weiner H. Location of the actual signal in the negatively charged leader sequence involved in the import into the mitochondrial matrix space. The Journal of Biological Chemistry. 278: 13712-8. PMID 12551941 DOI: 10.1074/Jbc.M212743200 |
0.301 |
|
| 2002 |
Mukhopadhyay A, Wei B, Zullo SJ, Wood LV, Weiner H. In vitro evidence of inhibition of mitochondrial protease processing by HIV-1 protease inhibitors in yeast: a possible contribution to lipodystrophy syndrome. Mitochondrion. 1: 511-8. PMID 16120303 DOI: 10.1016/S1567-7249(02)00042-9 |
0.332 |
|
| 2002 |
Rodriguez-Zavala JS, Weiner H. Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation. Biochemistry. 41: 8229-37. PMID 12081471 DOI: 10.1021/Bi012081X |
0.381 |
|
| 2002 |
Hammen PK, Allali-Hassani A, Hallenga K, Hurley TD, Weiner H. Multiple conformations of NAD and NADH when bound to human cytosolic and mitochondrial aldehyde dehydrogenase. Biochemistry. 41: 7156-68. PMID 12033950 DOI: 10.1021/Bi012197T |
0.403 |
|
| 2002 |
Mukhopadhyay A, Hammen P, Waltner-Law M, Weiner H. Timing and structural consideration for the processing of mitochondrial matrix space proteins by the mitochondrial processing peptidase (MPP). Protein Science : a Publication of the Protein Society. 11: 1026-35. PMID 11967360 DOI: 10.1110/Ps.3760102 |
0.356 |
|
| 2002 |
Yang CS, Weiner H. Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol. Archives of Biochemistry and Biophysics. 400: 105-10. PMID 11913976 DOI: 10.1006/Abbi.2002.2778 |
0.316 |
|
| 2002 |
Mukhopadhyay A, Avramova LV, Weiner H. Tom34 unlike Tom20 does not interact with the leader sequences of mitochondrial precursor proteins. Archives of Biochemistry and Biophysics. 400: 97-104. PMID 11913975 DOI: 10.1006/Abbi.2002.2777 |
0.344 |
|
| 2001 |
Zhou J, Weiner H. The N-terminal portion of mature aldehyde dehydrogenase affects protein folding and assembly. Protein Science : a Publication of the Protein Society. 10: 1490-7. PMID 11468345 DOI: 10.1110/Ps.5301 |
0.562 |
|
| 2001 |
Liu F, Cui X, Horner HT, Weiner H, Schnable PS. Mitochondrial aldehyde dehydrogenase activity is required for male fertility in maize. The Plant Cell. 13: 1063-78. PMID 11340182 DOI: 10.1105/Tpc.13.5.1063 |
0.308 |
|
| 2001 |
Wei B, Weiner H. Making an Oriental equivalent of the yeast cytosolic aldehyde dehydrogenase as well as making one with positive cooperativity in coenzyme binding by mutations of glutamate 492 and arginine 480. Chemico-Biological Interactions. 173-9. PMID 11306041 DOI: 10.1016/S0009-2797(00)00232-5 |
0.395 |
|
| 2001 |
Rodriguez-Zavala J, Weiner H. Role of the C-terminal tail on the quaternary structure of aldehyde dehydrogenases. Chemico-Biological Interactions. 151-60. PMID 11306039 DOI: 10.1016/S0009-2797(00)00230-1 |
0.327 |
|
| 2001 |
Allali-Hassani A, Weiner H. Interaction of human aldehyde dehydrogenase with aromatic substrates and ligands. Chemico-Biological Interactions. 125-33. PMID 11306037 DOI: 10.1016/S0009-2797(00)00228-3 |
0.37 |
|
| 2001 |
Weiner H, Wei B, Zhou J. Subunit communication in tetrameric class 2 human liver aldehyde dehydrogenase as the basis for half-of-the-site reactivity and the dominance of the oriental subunit in a heterotetramer. Chemico-Biological Interactions. 130: 47-56. PMID 11306030 DOI: 10.1016/S0009-2797(00)00221-0 |
0.555 |
|
| 2000 |
Zhou J, Weiner H. Basis for half-of-the-site reactivity and the dominance of the K487 oriental subunit over the E487 subunit in heterotetrameric human liver mitochondrial aldehyde dehydrogenase. Biochemistry. 39: 12019-24. PMID 11009616 DOI: 10.1021/Bi001221K |
0.586 |
|
| 2000 |
Wei B, Ni L, Hurley TD, Weiner H. Cooperativity in nicotinamide adenine dinucleotide binding induced by mutations of arginine 475 located at the subunit interface in the human liver mitochondrial class 2 aldehyde dehydrogenase Biochemistry. 39: 5295-5302. PMID 10819999 DOI: 10.1021/Bi000028N |
0.4 |
|
| 2000 |
Hammen PK, Weiner H. Structure of the cytosolic domain of TOM5, a mitochondrial import protein. Febs Letters. 468: 101-104. PMID 10683449 DOI: 10.1016/S0014-5793(00)01160-1 |
0.305 |
|
| 2000 |
Mann CJ, Weiner H. Differences in the roles of conserved glutamic acid residues in the active site of human class 3 and class 2 aldehyde dehydrogenases. Protein Science : a Publication of the Protein Society. 8: 1922-9. PMID 10548037 DOI: 10.1110/Ps.8.10.1922 |
0.393 |
|
| 1999 |
Ni L, Zhou J, Hurley TD, Weiner H. Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Science : a Publication of the Protein Society. 8: 2784-90. PMID 10631996 DOI: 10.1110/Ps.8.12.2784 |
0.596 |
|
| 1999 |
Hurley TD, Weiner H. Evaluation of the roles of the conserved residues of aldehyde dehydrogenase Advances in Experimental Medicine and Biology. 463: 45-52. PMID 10352668 DOI: 10.1007/978-1-4615-4735-8_6 |
0.383 |
|
| 1999 |
Hurley TD, Steinmetz CG, Weiner H. Three-dimensional structure of mitochondrial aldehyde dehydrogenase: Mechanistic implications Advances in Experimental Medicine and Biology. 463: 15-25. PMID 10352665 DOI: 10.1007/978-1-4615-4735-8_3 |
0.386 |
|
| 1999 |
Ni L, Heard TS, Weiner H. In vivo mitochondrial import. A comparison of leader sequence charge and structural relationships with the in vitro model resulting in evidence for co-translational import. The Journal of Biological Chemistry. 274: 12685-91. PMID 10212250 DOI: 10.1074/Jbc.274.18.12685 |
0.345 |
|
| 1999 |
Hammen PK, Heard TS, Waltner M, Weiner H. The loss in hydrophobic surface area resulting from a Leu to Val mutation at the N-terminus of the aldehyde dehydrogenase presequence prevents import of the protein into mitochondria. Protein Science : a Publication of the Protein Society. 8: 890-6. PMID 10211835 DOI: 10.1110/Ps.8.4.890 |
0.361 |
|
| 1998 |
Hammen PK, Weiner H. Mitochondrial leader sequences: structural similarities and sequence differences. The Journal of Experimental Zoology. 282: 280-3. PMID 9723185 DOI: 10.1002/(Sici)1097-010X(199809/10)282:1/2<280::Aid-Jez30>3.0.Co;2-V |
0.327 |
|
| 1998 |
Wang X, Mann CJ, Bai Y, Ni L, Weiner H. Molecular Cloning, Characterization, and Potential Roles of Cytosolic and Mitochondrial Aldehyde Dehydrogenases in Ethanol Metabolism in Saccharomyces cerevisiae Journal of Bacteriology. 180: 822-830. DOI: 10.1128/Jb.180.4.822-830.1998 |
0.386 |
|
| 1997 |
Ni L, Sheikh S, Weiner H. Involvement of glutamate 399 and lysine 192 in the mechanism of human liver mitochondrial aldehyde dehydrogenase. The Journal of Biological Chemistry. 272: 18823-6. PMID 9228057 DOI: 10.1074/Jbc.272.30.18823 |
0.395 |
|
| 1997 |
Steinmetz CG, Xie P, Weiner H, Hurley TD. Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol aversion Structure. 5: 701-711. PMID 9195888 DOI: 10.1016/S0969-2126(97)00224-4 |
0.402 |
|
| 1997 |
Zhou J, Weiner H. Binding of thyroxine analogs to human liver aldehyde dehydrogenases. European Journal of Biochemistry / Febs. 245: 123-8. PMID 9128732 DOI: 10.1111/J.1432-1033.1997.00123.X |
0.579 |
|
| 1997 |
Sheikh S, Weiner H. Allosteric inhibition of human liver aldehyde dehydrogenase by the isoflavone prunetin Biochemical Pharmacology. 53: 471-478. PMID 9105397 DOI: 10.1016/S0006-2952(96)00837-4 |
0.424 |
|
| 1997 |
Wang X, Bai Y, Ni L, Weiner H. Saccharomyces cerevisiae aldehyde dehydrogenases. Identification and expression. Advances in Experimental Medicine and Biology. 414: 277-80. PMID 9059631 DOI: 10.1007/978-1-4615-5871-2_32 |
0.307 |
|
| 1997 |
Sheikh S, Ni L, Weiner H. Mutation of the conserved amino acids of mitochondria aldehyde dehydrogenase: Role of the conserved residues in the mechanism of reaction Advances in Experimental Medicine and Biology. 414: 195-200. PMID 9059621 DOI: 10.1007/978-1-4615-5871-2_22 |
0.339 |
|
| 1997 |
Weiner H, Sheikh S, Zhou J, Wang X. Subunit interactions in mammalian liver aldehyde dehydrogenases. Advances in Experimental Medicine and Biology. 414: 181-5. PMID 9059619 DOI: 10.1007/978-1-4615-5871-2_20 |
0.562 |
|
| 1997 |
Sjöling S, Waltner M, Kalousek F, Glaser E, Weiner H. Studies on protein processing for membrane-bound spinach leaf mitochondrial processing peptidase integrated into the cytochrome bc1 complex and the soluble rat liver matrix mitochondrial processing peptidase. European Journal of Biochemistry. 242: 114-21. PMID 8954161 DOI: 10.1111/J.1432-1033.1996.0114R.X |
0.353 |
|
| 1997 |
Wang X, Sheikh S, Saigal D, Robinson L, Weiner H. Heterotetramers of human liver mitochondrial (class 2) aldehyde dehydrogenase expressed in Escherichia coli. A model to study the heterotetramers expected to be found in Oriental people. The Journal of Biological Chemistry. 271: 31172-8. PMID 8940116 DOI: 10.1074/Jbc.271.49.31172 |
0.411 |
|
| 1997 |
Xiao Q, Weiner H, Crabb DW. The mutation in the mitochondrial aldehyde dehydrogenase (ALDH2) gene responsible for alcohol-induced flushing increases turnover of the enzyme tetramers in a dominant fashion. The Journal of Clinical Investigation. 98: 2027-32. PMID 8903321 DOI: 10.1172/Jci119007 |
0.409 |
|
| 1996 |
Waltner M, Hammen PK, Weiner H. Influence of the Mature Portion of a Precursor Protein on the Mitochondrial Signal Sequence Journal of Biological Chemistry. 271: 21226-21230. DOI: 10.1074/Jbc.271.35.21226 |
0.322 |
|
| 1996 |
Hammen PK, Waltner M, Hahnemann B, Heard TS, Weiner H. The Role of Positive Charges and Structural Segments in the Presequence of Rat Liver Aldehyde Dehydrogenase in Import into Mitochondria Journal of Biological Chemistry. 271: 21041-21048. DOI: 10.1074/Jbc.271.35.21041 |
0.332 |
|
| 1995 |
Farrés J, Wang TT, Cunningham SJ, Weiner H. Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis. Biochemistry. 34: 2592-8. PMID 7873540 DOI: 10.1021/Bi00008A025 |
0.403 |
|
| 1995 |
Wang X, Weiner H. Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis. Biochemistry. 34: 237-43. PMID 7819202 DOI: 10.1021/Bi00001A028 |
0.423 |
|
| 1995 |
Zhou J, Bai Y, Weiner H. Proteolysis prevents in vivo chimeric fusion protein import into yeast mitochondria. Cytosolic cleavage and subcellular distribution. The Journal of Biological Chemistry. 270: 16689-93. PMID 7622479 DOI: 10.1074/Jbc.270.28.16689 |
0.549 |
|
| 1995 |
Xiao Q, Weiner H, Johnston T, Crabb DW. The aldehyde dehydrogenase ALDH2*2 allele exhibits dominance over ALDH2*1 in transduced HeLa cells. The Journal of Clinical Investigation. 96: 2180-6. PMID 7593603 DOI: 10.1172/Jci118272 |
0.33 |
|
| 1995 |
Waltner M, Weiner H. Conversion of a nonprocessed mitochondrial precursor protein into one that is processed by the mitochondrial processing peptidase. The Journal of Biological Chemistry. 270: 26311-7. PMID 7592841 DOI: 10.1074/Jbc.270.44.26311 |
0.333 |
|
| 1995 |
Pchelintseva O, Pak YK, Weiner H. Identification of protein-receptor components required for the import of prealdehyde dehydrogenase into rat liver mitochondria. Archives of Biochemistry and Biophysics. 323: 54-62. PMID 7487073 DOI: 10.1006/Abbi.1995.0009 |
0.315 |
|
| 1995 |
Weiner H, Farrés J, Rout UJ, Wang X, Zheng CF. Site directed mutagenesis to probe for active site components of liver mitochondrial aldehyde dehydrogenase. Advances in Experimental Medicine and Biology. 372: 1-7. PMID 7484366 DOI: 10.1007/978-1-4615-1965-2_1 |
0.379 |
|
| 1994 |
Rout UK, Weiner H. Involvement of serine 74 in the enzyme-coenzyme interaction of rat liver mitochondrial aldehyde dehydrogenase. Biochemistry. 33: 8955-61. PMID 8043582 DOI: 10.1021/Bi00196A013 |
0.434 |
|
| 1994 |
Hammen PK, Gorenstein DG, Weiner H. Structure of the signal sequences for two mitochondrial matrix proteins that are not proteolytically processed upon import. Biochemistry. 33: 8610-7. PMID 7913339 DOI: 10.1021/Bi00194A028 |
0.343 |
|
| 1993 |
Zheng CF, Weiner H. Attempts to increase the expression of rat liver mitochondrial aldehyde dehydrogenase in E. coli by altering the mRNA. Advances in Experimental Medicine and Biology. 328: 73-9. PMID 8493942 DOI: 10.1007/978-1-4615-2904-0_9 |
0.395 |
|
| 1993 |
Zheng CF, Weiner H. Role of the highly conserved histidine residues in rat liver mitochondrial aldehyde dehydrogenase as studied by site-directed mutagenesis. Archives of Biochemistry and Biophysics. 305: 460-6. PMID 8373184 DOI: 10.1006/Abbi.1993.1447 |
0.419 |
|
| 1993 |
Zheng CF, Wang TT, Weiner H. Cloning and expression of the full-length cDNAS encoding human liver class 1 and class 2 aldehyde dehydrogenase. Alcoholism, Clinical and Experimental Research. 17: 828-31. PMID 8214422 DOI: 10.1111/J.1530-0277.1993.Tb00849.X |
0.384 |
|
| 1993 |
Ghenbot G, Weiner H. Purification of liver aldehyde dehydrogenase by p-hydroxyacetophenone-sepharose affinity matrix and the coelution of chloramphenicol acetyl transferase from the same matrix with recombinantly expressed aldehyde dehydrogenase. Protein Expression and Purification. 3: 470-8. PMID 1486275 DOI: 10.1016/1046-5928(92)90064-4 |
0.376 |
|
| 1991 |
Wang TT, Wang Y, Weiner H. Effects of protein size on the rate of import of the precursors of aldehyde dehydrogenase and ornithine transcarbamylase into rat liver mitochondria. Alcoholism, Clinical and Experimental Research. 15: 286-90. PMID 2058806 DOI: 10.1111/J.1530-0277.1991.Tb01870.X |
0.356 |
|
| 1991 |
Weiner H, Farrés J, Wang TT, Cunningham SJ, Zheng CF, Ghenbot G. Probing the active site of aldehyde dehydrogenase by site directed mutagenesis. Advances in Experimental Medicine and Biology. 284: 13-7. PMID 2053473 DOI: 10.1007/978-1-4684-5901-2_3 |
0.363 |
|
| 1991 |
Jeng J, Weiner H. Purification and characterization of catalytically active precursor of rat liver mitochondrial aldehyde dehydrogenase expressed in Escherichia coli Archives of Biochemistry and Biophysics. 289: 214-222. PMID 1898068 DOI: 10.1016/0003-9861(91)90464-T |
0.353 |
|
| 1990 |
Wang TT, Pak YK, Weiner H. Effects of alcohol on the import of aldehyde dehydrogenase precursor into rat liver mitochondria. Alcoholism, Clinical and Experimental Research. 14: 600-4. PMID 2221289 DOI: 10.1111/J.1530-0277.1990.Tb01209.X |
0.366 |
|
| 1990 |
Guan K, Weiner H. Sequence of the precursor of bovine liver mitochondrial aldehyde dehydrogenase as determined from its cDNA, its gene, and its functionality Archives of Biochemistry and Biophysics. 277: 351-360. PMID 1689984 DOI: 10.1016/0003-9861(90)90590-U |
0.363 |
|
| 1989 |
Cao QN, Tu GC, Weiner H. Mitochondria as the primary site of acetaldehyde metabolism in beef and pig liver slices. Alcoholism, Clinical and Experimental Research. 12: 720-4. PMID 3067622 DOI: 10.1111/J.1530-0277.1988.Tb00271.X |
0.406 |
|
| 1989 |
Guan KL, Pak YK, Tu GC, Cao QN, Weiner H. Purification and characterization of beef and pig liver aldehyde dehydrogenases. Alcoholism, Clinical and Experimental Research. 12: 713-9. PMID 3067621 DOI: 10.1111/J.1530-0277.1988.Tb00270.X |
0.425 |
|
| 1989 |
Cao QN, Tu GC, Weiner H. Presence of cytosolic aldehyde dehydrogenase isozymes in adult and fetal rat liver. Biochemical Pharmacology. 38: 77-83. PMID 2910309 DOI: 10.1016/0006-2952(89)90152-4 |
0.367 |
|
| 1989 |
Wang TT, Farrés J, Weiner H. Liver mitochondrial aldehyde dehydrogenase: in vitro expression, in vitro import, and effect of alcohols on import. Archives of Biochemistry and Biophysics. 272: 440-9. PMID 2751310 DOI: 10.1016/0003-9861(89)90238-5 |
0.337 |
|
| 1989 |
Farrés J, Guan KL, Weiner H. Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences. European Journal of Biochemistry. 180: 67-74. PMID 2540003 DOI: 10.1111/J.1432-1033.1989.Tb14616.X |
0.396 |
|
| 1988 |
Farrés J, Guan KL, Weiner H. Sequence of the signal peptide for rat liver mitochondrial aldehyde dehydrogenase. Biochemical and Biophysical Research Communications. 150: 1083-7. PMID 3342060 DOI: 10.1016/0006-291X(88)90740-1 |
0.313 |
|
| 1986 |
McMichael M, Hellström-Lindahl E, Weiner H. Identification and selective precipitation of human aldehyde dehydrogenase isozymes using antibodies raised to horse liver aldehyde dehydrogenase isozymes. Alcoholism, Clinical and Experimental Research. 10: 323-9. PMID 3526958 DOI: 10.1111/J.1530-0277.1986.Tb05098.X |
0.366 |
|
| 1986 |
Tank AW, Deitrich RA, Weiner H. Effects of induction of rat liver cytosolic aldehyde dehydrogenase on the oxidation of biogenic aldehydes. Biochemical Pharmacology. 35: 4563-9. PMID 2431694 DOI: 10.1016/0006-2952(86)90779-3 |
0.362 |
|
| 1985 |
Svanas GW, Weiner H. Identification of aldehyde dehydrogenase resistant to cyanamide and disulfiram inhibition. Alcohol (Fayetteville, N.Y.). 1: 347-9. PMID 6536295 DOI: 10.1016/0741-8329(84)90059-4 |
0.315 |
|
| 1985 |
Svanas GW, Weiner H. Use of cyanamide to determine localization of acetaldehyde metabolism in rat liver. Alcohol (Fayetteville, N.Y.). 2: 111-5. PMID 4015825 DOI: 10.1016/0741-8329(85)90026-6 |
0.366 |
|
| 1985 |
Hellström-Lindahl E, Weiner H. Effects of disulfiram on the oxidation of benzaldehyde and acetaldehyde in rat liver. Biochemical Pharmacology. 34: 1529-35. PMID 3994763 DOI: 10.1016/0006-2952(85)90695-1 |
0.385 |
|
| 1985 |
Svanas GW, Weiner H. Enzymatic requirement for cyanamide inactivation of rat liver aldehyde dehydrogenase. Biochemical Pharmacology. 34: 1197-204. PMID 3994742 DOI: 10.1016/0006-2952(85)90495-2 |
0.405 |
|
| 1985 |
Svanas GW, Weiner H. Aldehyde dehydrogenase activity as the rate-limiting factor for acetaldehyde metabolism in rat liver. Archives of Biochemistry and Biophysics. 236: 36-46. PMID 3966800 DOI: 10.1016/0003-9861(85)90603-4 |
0.331 |
|
| 1984 |
Weiner H, Ardelt B. Distribution and properties of aldehyde dehydrogenase in regions of rat brain. Journal of Neurochemistry. 42: 109-15. PMID 6689685 DOI: 10.1111/J.1471-4159.1984.Tb09705.X |
0.366 |
|
| 1983 |
Svanas GW, Weiner H. Rapid purification of dehydrogenases by affinity chromatography with ternary complexes. Analytical Biochemistry. 124: 314-9. PMID 6756204 DOI: 10.1016/0003-2697(82)90045-8 |
0.366 |
|
| 1983 |
Weiner H, Truesdale-Mahoney N, Pelletier AJ. Oxidation of acetaldehyde and presence of aldehyde dehydrogenase in rat erythrocytes. Pharmacology, Biochemistry and Behavior. 18: 167-170. PMID 6634833 DOI: 10.1016/0091-3057(83)90166-1 |
0.385 |
|
| 1983 |
Weiner H, Takahashi K. Effects of magnesium and calcium on mitochondrial and cytosolic liver aldehyde dehydrogenases. Pharmacology, Biochemistry, and Behavior. 109-12. PMID 6634825 DOI: 10.1016/0091-3057(83)90155-7 |
0.372 |
|
| 1982 |
Truesdale-Mahoney N, Doolittle DP, Weiner H. Genetic basis for the polymorphism of rat liver cytosolic aldehyde dehydrogenase. Biochemical Genetics. 19: 1275-82. PMID 7337698 DOI: 10.1007/Bf00484579 |
0.384 |
|
| 1982 |
Takahashi K, Weiner H, Filmer DL. Effects of pH on horse liver aldehyde dehydrogenase: alterations in metal ion activation, number of functioning active sites, and hydrolysis of the acyl intermediate. Biochemistry. 20: 6225-30. PMID 7306510 DOI: 10.1021/Bi00524A049 |
0.354 |
|
| 1981 |
Takahashi K, Weiner H, Hu JH. Increase in the stoichiometry of the functioning active sites of horse liver aldehyde dehydrogenase in the presence of magnesium ions. Archives of Biochemistry and Biophysics. 205: 571-8. PMID 7469426 DOI: 10.1016/0003-9861(80)90140-X |
0.357 |
|
| 1981 |
Takahashi K, Weiner H. Nicotinamide adenine dinucleotide activation of the esterase reaction of horse liver aldehyde dehydrogenase. Biochemistry. 20: 2720-6. PMID 7248246 DOI: 10.1021/Bi00513A003 |
0.373 |
|
| 1981 |
Tank AW, Weiner H, Thurman JA. Enzymology and subcellular localization of aldehyde oxidation in rat liver. Oxidation of 3,4-dihydroxyphenylacetaldehyde derived from dopamine to 3,4-dihydroxyphenylacetic acid. Biochemical Pharmacology. 30: 3265-75. PMID 7034733 DOI: 10.1016/0006-2952(81)90598-0 |
0.364 |
|
| 1980 |
Takahashi K, Brown CS, Weiner H. Mechanism of the magnesium ion activation of the catalytic activity of horse liver aldehyde dehydrogenase Advances in Experimental Medicine and Biology. 132: 181-188. PMID 7424705 DOI: 10.1007/978-1-4757-1419-7_19 |
0.359 |
|
| 1980 |
Shultz J, Weiner H. Alteration of the enzymology of chloral hydrate reduction in the presence of ethanol. Biochemical Pharmacology. 28: 3379-84. PMID 43731 DOI: 10.1016/0006-2952(79)90076-5 |
0.377 |
|
| 1979 |
Tank AW, Weiner H. Ethanol-induced alteration of dopamine metabolism in rat liver. Biochemical Pharmacology. 28: 3139-47. PMID 518712 DOI: 10.1016/0006-2952(79)90624-5 |
0.368 |
|
| 1977 |
Berger D, Weiner H. Relationship between alcohol preference and biogenic aldehyde metabolizing enzymes in rats. Biochemical Pharmacology. 26: 841-6. PMID 861049 DOI: 10.1016/0006-2952(77)90396-3 |
0.341 |
|
| 1977 |
Berger D, Weiner H. Effects of disulfiram and chloral hydrate on the metabolism of catecholamines in rat liver and brain. Biochemical Pharmacology. 26: 741-7. PMID 856206 DOI: 10.1016/0006-2952(77)90218-0 |
0.321 |
|
| 1972 |
Coleman PL, Iweibo I, Weiner H. Role of zinc in horse liver alcohol dehydrogenase. Influence on structure and conformational changes. Biochemistry. 11: 1010-8. PMID 4335286 DOI: 10.1021/Bi00756A010 |
0.395 |
|
| 1972 |
Iweibo I, Weiner H. Role of zinc in horse liver alcohol dehydrogenase. Coenzyme and substrate binding. Biochemistry. 11: 1003-10. PMID 4335285 DOI: 10.1021/Bi00756A009 |
0.418 |
|
| 1968 |
Weiner H. A polarization of fluorescence study of alcohol dehydrogenase and its binary and ternary complexes. Archives of Biochemistry and Biophysics. 126: 692-9. PMID 4299687 DOI: 10.1016/0003-9861(68)90456-6 |
0.333 |
|
| 1966 |
Weiner H, White WN, Hoare DG, Koshland DE. The formation of anhydrochymotrypsin by removing the elements of water from the serine at the active site. Journal of the American Chemical Society. 88: 3851-9. PMID 5916376 DOI: 10.1021/ja00968a033 |
0.419 |
|
| 1966 |
Weiner H, Koshland DE. Conformational studies on the interaction of chymotrypsin with substrates and inhibitors. Journal of Molecular Biology. 12: 881-91. PMID 5858434 DOI: 10.1016/S0022-2836(65)80335-7 |
0.483 |
|
| 1965 |
Weiner H, Sneen RA. Substitution at a Saturated Carbon Atom. IV. A Clarification of the Mechanism of Solvolyses of 2-Octyl Sulfonates. Stereochemical Considerations1 Journal of the American Chemical Society. 87: 287-291. DOI: 10.1021/ja01080a026 |
0.23 |
|
| 1965 |
Weiner H, Sneen RA. Substitution at a saturated carbon atom. IV. A clarification of the mechanism of solvolyses of 2-octyl sulfonates. Stereochemical considerations Journal of the American Chemical Society. 87: 287-291. DOI: 10.1021/Ja01080A026 |
0.628 |
|
| 1963 |
Weiner H, Sneen RA. Acetone as a Nucleophile Journal of the American Chemical Society. 85: 2181-2181. DOI: 10.1021/Ja00897A042 |
0.645 |
|
| 1963 |
Weiner H, Sneen RA. Identification of intermediates in solvolyses of 2-octyl sulfonates Tetrahedron Letters. 4: 1309-1316. DOI: 10.1016/S0040-4039(01)90823-8 |
0.282 |
|
| 1963 |
Weiner H, Sneen RA. Identification of intermediates in solvolyses of 2-octyl sulfonates Tetrahedron Letters. 4: 1309-1316. DOI: 10.1016/S0040-4039(01)90823-8 |
0.65 |
|
| 1962 |
Weiner H, Sneen RA. Evidence for Dual and Distinct Mechanisms in the Solvolysis of 2-Octyl Brosylate in Aqueous Dioxane Journal of the American Chemical Society. 84: 3599-3599. DOI: 10.1021/ja00877a048 |
0.242 |
|
| 1962 |
Weiner H, Sneen RA. Evidence for dual and distinct mechanisms in the solvolysis of 2-octyl brosylate in aqueous dioxane [15] Journal of the American Chemical Society. 84: 3599. DOI: 10.1021/Ja00877A048 |
0.633 |
|
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