Year |
Citation |
Score |
2018 |
Kim J, Chen B, Bru JL, Huynh E, Momen M, Aswad DW. New findings on SNP variants of human protein L-isoaspartyl methyltransferase that affect catalytic activity, thermal stability, and aggregation. Plos One. 13: e0198266. PMID 29856810 DOI: 10.1371/journal.pone.0198266 |
0.403 |
|
2017 |
Juang C, Chen B, Bru JL, Nguyen K, Huynh E, Momen M, Kim J, Aswad DW. Polymorphic Variants of Human Protein L-Isoaspartyl Methyltransferase Affect Catalytic Activity, Aggregation, and Thermal Stability; Implications for the Etiology of Neurological Disorders and Cognitive Aging. The Journal of Biological Chemistry. PMID 28100787 DOI: 10.1074/jbc.M116.765222 |
0.364 |
|
2016 |
Pulido MA, DerHartunian MK, Qin Z, Chung EM, Kang DS, Woodham AW, Tsou JA, Klooster R, Akbari O, Wang L, Kast WM, Liu SV, Verschuuren JJ, Aswad DW, Laird-Offringa IA. Isoaspartylation appears to trigger small cell lung cancer-associated autoimmunity against neuronal protein ELAVL4. Journal of Neuroimmunology. 299: 70-78. PMID 27725125 DOI: 10.1016/J.Jneuroim.2016.09.002 |
0.337 |
|
2015 |
Qin Z, Zhu JX, Aswad DW. The D-isoAsp-25 variant of histone H2B is highly enriched in active chromatin: potential role in the regulation of gene expression? Amino Acids. PMID 26666674 DOI: 10.1007/S00726-015-2140-9 |
0.593 |
|
2015 |
Qin Z, Dimitrijevic A, Aswad DW. Accelerated protein damage in brains of PIMT+/- mice; a possible model for the variability of cognitive decline in human aging. Neurobiology of Aging. 36: 1029-36. PMID 25465735 DOI: 10.1016/j.neurobiolaging.2014.10.036 |
0.348 |
|
2014 |
Dimitrijevic A, Qin Z, Aswad DW. Isoaspartyl formation in creatine kinase B Is associated with loss of enzymatic activity; implications for the linkage of isoaspartate accumulation and neurological dysfunction in the PIMT knockout mouse. Plos One. 9: e100622. PMID 24955845 DOI: 10.1371/journal.pone.0100622 |
0.44 |
|
2014 |
Qin Z, Yang J, Klassen HJ, Aswad DW. Isoaspartyl protein damage and repair in mouse retina. Investigative Ophthalmology & Visual Science. 55: 1572-9. PMID 24550364 DOI: 10.1167/iovs.13-13668 |
0.464 |
|
2013 |
Qin Z, Kaufman RS, Khoury RN, Khoury MK, Aswad DW. Isoaspartate accumulation in mouse brain is associated with altered patterns of protein phosphorylation and acetylation, some of which are highly sex-dependent. Plos One. 8: e80758. PMID 24224061 DOI: 10.1371/journal.pone.0080758 |
0.393 |
|
2013 |
Doyle HA, Aswad DW, Mamula MJ. Autoimmunity to isomerized histone H2B in systemic lupus erythematosus. Autoimmunity. 46: 6-13. PMID 22967069 DOI: 10.3109/08916934.2012.710859 |
0.323 |
|
2012 |
Morrison GJ, Ganesan R, Qin Z, Aswad DW. Considerations in the identification of endogenous substrates for protein L-isoaspartyl methyltransferase: the case of synuclein. Plos One. 7: e43288. PMID 22905247 DOI: 10.1371/journal.pone.0043288 |
0.51 |
|
2008 |
Carter WG, Aswad DW. Formation, localization, and repair of L-isoaspartyl sites in histones H2A and H2B in nucleosomes from rat liver and chicken erythrocytes. Biochemistry. 47: 10757-64. PMID 18795804 DOI: 10.1021/bi8013467 |
0.42 |
|
2007 |
Zhu JX, Aswad DW. Selective cleavage of isoaspartyl peptide bonds by hydroxylamine after methyltransferase priming. Analytical Biochemistry. 364: 1-7. PMID 17376395 DOI: 10.1016/J.Ab.2007.02.013 |
0.665 |
|
2006 |
Yang ML, Doyle HA, Gee RJ, Lowenson JD, Clarke S, Lawson BR, Aswad DW, Mamula MJ. Intracellular protein modification associated with altered T cell functions in autoimmunity. Journal of Immunology (Baltimore, Md. : 1950). 177: 4541-9. PMID 16982891 DOI: 10.4049/Jimmunol.177.7.4541 |
0.581 |
|
2006 |
Zhu JX, Doyle HA, Mamula MJ, Aswad DW. Protein repair in the brain, proteomic analysis of endogenous substrates for protein L-isoaspartyl methyltransferase in mouse brain. The Journal of Biological Chemistry. 281: 33802-13. PMID 16959769 DOI: 10.1074/Jbc.M606958200 |
0.698 |
|
2006 |
Reissner KJ, Paranandi MV, Luc TM, Doyle HA, Mamula MJ, Lowenson JD, Aswad DW. Synapsin I is a major endogenous substrate for protein L-isoaspartyl methyltransferase in mammalian brain. The Journal of Biological Chemistry. 281: 8389-98. PMID 16443604 DOI: 10.1074/jbc.M510716200 |
0.405 |
|
2005 |
Young GW, Hoofring SA, Mamula MJ, Doyle HA, Bunick GJ, Hu Y, Aswad DW. Protein L-isoaspartyl methyltransferase catalyzes in vivo racemization of Aspartate-25 in mammalian histone H2B. The Journal of Biological Chemistry. 280: 26094-8. PMID 15908425 DOI: 10.1074/jbc.M503624200 |
0.461 |
|
2003 |
Reissner KJ, Aswad DW. Deamidation and isoaspartate formation in proteins: unwanted alterations or surreptitious signals? Cellular and Molecular Life Sciences : Cmls. 60: 1281-95. PMID 12943218 DOI: 10.1007/s00018-003-2287-5 |
0.452 |
|
2002 |
Li H, Park S, Kilburn B, Jelinek MA, Henschen-Edman A, Aswad DW, Stallcup MR, Laird-Offringa IA. Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase. The Journal of Biological Chemistry. 277: 44623-30. PMID 12237300 DOI: 10.1074/Jbc.M206187200 |
0.414 |
|
2001 |
Ma H, Baumann CT, Li H, Strahl BD, Rice R, Jelinek MA, Aswad DW, Allis CD, Hager GL, Stallcup MR. Hormone-dependent, CARM1-directed, arginine-specific methylation of histone H3 on a steroid-regulated promoter. Current Biology : Cb. 11: 1981-5. PMID 11747826 DOI: 10.1016/S0960-9822(01)00600-5 |
0.341 |
|
2001 |
Young AL, Carter WG, Doyle HA, Mamula MJ, Aswad DW. Structural integrity of histone H2B in vivo requires the activity of protein L-isoaspartate O-methyltransferase, a putative protein repair enzyme. The Journal of Biological Chemistry. 276: 37161-5. PMID 11479322 DOI: 10.1074/jbc.M106682200 |
0.365 |
|
2000 |
Stallcup MR, Chen D, Koh SS, Ma H, Lee YH, Li H, Schurter BT, Aswad DW. Co-operation between protein-acetylating and protein-methylating co-activators in transcriptional activation. Biochemical Society Transactions. 28: 415-8. PMID 10961931 DOI: 10.1042/Bst0280415 |
0.355 |
|
2000 |
Schurter BT, Aswad DW. Analysis of isoaspartate in peptides and proteins without the use of radioisotopes. Analytical Biochemistry. 282: 227-31. PMID 10873277 DOI: 10.1006/abio.2000.4601 |
0.441 |
|
2000 |
Aswad DW, Paranandi MV, Schurter BT. Isoaspartate in peptides and proteins: formation, significance, and analysis. Journal of Pharmaceutical and Biomedical Analysis. 21: 1129-36. PMID 10708396 DOI: 10.1016/S0731-7085(99)00230-7 |
0.48 |
|
1999 |
David CL, Pierce VA, Aswad DW, Gibbs AG. The effect of urea exposure on isoaspartyl content and protein L-isoaspartate methyltransferase activity in Drosophila melanogaster. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 124: 423-7. PMID 10665370 DOI: 10.1016/S0305-0491(99)00135-2 |
0.39 |
|
1999 |
Chen D, Ma H, Hong H, Koh SS, Huang SM, Schurter BT, Aswad DW, Stallcup MR. Regulation of transcription by a protein methyltransferase. Science (New York, N.Y.). 284: 2174-7. PMID 10381882 DOI: 10.1126/Science.284.5423.2174 |
0.345 |
|
1999 |
David CL, Keener J, Aswad DW. Isoaspartate in ribosomal protein S11 of Escherichia coli. Journal of Bacteriology. 181: 2872-7. PMID 10217780 DOI: 10.1128/Jb.181.9.2872-2877.1999 |
0.424 |
|
1998 |
David CL, Orpiszewski J, Zhu XC, Reissner KJ, Aswad DW. Isoaspartate in chrondroitin sulfate proteoglycans of mammalian brain. The Journal of Biological Chemistry. 273: 32063-70. PMID 9822681 DOI: 10.1074/jbc.273.48.32063 |
0.411 |
|
1997 |
David CL, Szumlanski CL, DeVry CG, Park-Hah JO, Clarke S, Weinshilboum RM, Aswad DW. Human erythrocyte protein L-isoaspartyl methyltransferase: heritability of basal activity and genetic polymorphism for thermal stability. Archives of Biochemistry and Biophysics. 346: 277-86. PMID 9343375 DOI: 10.1006/Abbi.1997.0303 |
0.519 |
|
1997 |
David CL, Keener J, Aswad DW. Escherichia coli ribosomal protein 11 is a major substrate for protein l-isoaspartyl methyltransferase (PIMT) Faseb Journal. 11: A1274. |
0.332 |
|
1996 |
Rich RC, Aswad DW. Characterization of the phosphorylation site of PP59, a substrate for cyclic AMP-dependent protein kinase that is enriched in the synaptic membrane fraction of rat cerebellum. Journal of Neurochemistry. 67: 2581-9. PMID 8931493 DOI: 10.1046/J.1471-4159.1996.67062581.X |
0.426 |
|
1996 |
Orpiszewski J, Aswad DW. High mass methyl-accepting protein (HMAP), a highly effective endogenous substrate for protein L-isoaspartyl methyltransferase in mammalian brain. The Journal of Biological Chemistry. 271: 22965-8. PMID 8798482 DOI: 10.1074/jbc.271.38.22965 |
0.481 |
|
1996 |
Najbauer J, Orpiszewski J, Aswad DW. Molecular aging of tubulin: accumulation of isoaspartyl sites in vitro and in vivo. Biochemistry. 35: 5183-90. PMID 8611502 DOI: 10.1021/bi953063g |
0.453 |
|
1995 |
David CL, Aswad DW. Cloning, expression, and purification of rat brain protein L-isoaspartyl methyltransferase. Protein Expression and Purification. 6: 312-8. PMID 7663167 DOI: 10.1006/prep.1995.1041 |
0.399 |
|
1994 |
Paranandi MV, Guzzetta AW, Hancock WS, Aswad DW. Deamidation and isoaspartate formation during in vitro aging of recombinant tissue plasminogen activator. The Journal of Biological Chemistry. 269: 243-53. PMID 8276801 |
0.35 |
|
1994 |
Shahrokh Z, Eberlein G, Buckley D, Paranandi MV, Aswad DW, Stratton P, Mischak R, Wang YJ. Major degradation products of basic fibroblast growth factor: detection of succinimide and iso-aspartate in place of aspartate. Pharmaceutical Research. 11: 936-44. PMID 7937552 DOI: 10.1023/A:1018962732067 |
0.336 |
|
1993 |
Rich RC, Aswad DW. Identification of a 59-kDa Substrate for cAMP-Dependent Protein Kinase That Is Enriched in Rat Cerebellar Membranes. Molecular and Cellular Neurosciences. 4: 562-70. PMID 19912964 DOI: 10.1006/mcne.1993.1069 |
0.36 |
|
1993 |
Johnson BA, Aswad DW. Kinetic properties of bovine brain protein L-isoaspartyl methyltransferase determined using a synthetic isoaspartyl peptide substrate. Neurochemical Research. 18: 87-94. PMID 8464537 DOI: 10.1007/BF00966926 |
0.594 |
|
1993 |
Johnson BA, Najbauer J, Aswad DW. Accumulation of substrates for protein L-isoaspartyl methyltransferase in adenosine dialdehyde-treated PC12 cells. The Journal of Biological Chemistry. 268: 6174-81. PMID 8454593 |
0.553 |
|
1993 |
Potter SM, Henzel WJ, Aswad DW. In vitro aging of calmodulin generates isoaspartate at multiple Asn-Gly and Asp-Gly sites in calcium-binding domains II, III, and IV. Protein Science : a Publication of the Protein Society. 2: 1648-63. PMID 8251940 DOI: 10.1002/pro.5560021011 |
0.597 |
|
1993 |
Najbauer J, Johnson BA, Young AL, Aswad DW. Peptides with sequences similar to glycine, arginine-rich motifs in proteins interacting with RNA are efficiently recognized by methyltransferase(s) modifying arginine in numerous proteins. The Journal of Biological Chemistry. 268: 10501-9. PMID 7683681 |
0.532 |
|
1992 |
Najbauer J, Johnson BA, Aswad DW. Analysis of stable protein methylation in cultured cells. Archives of Biochemistry and Biophysics. 293: 85-92. PMID 1731643 DOI: 10.1016/0003-9861(92)90369-8 |
0.568 |
|
1992 |
Potter SM, Johnson BA, Henschen A, Aswad DW, Guzzetta AW. The type II isoform of bovine brain protein L-isoaspartyl methyltransferase has an endoplasmic reticulum retention signal (...RDEL) at its C-terminus. Biochemistry. 31: 6339-47. PMID 1627573 DOI: 10.1021/Bi00142A025 |
0.681 |
|
1991 |
Johnson BA, Shirokawa JM, Geddes JW, Choi BH, Kim RC, Aswad DW. Protein L-isoaspartyl methyltransferase in postmortem brains of aged humans. Neurobiology of Aging. 12: 19-24. PMID 2002878 DOI: 10.1016/0197-4580(91)90034-H |
0.548 |
|
1991 |
Johnson BA, Aswad DW. Optimal conditions for the use of protein L-isoaspartyl methyltransferase in assessing the isoaspartate content of peptides and proteins. Analytical Biochemistry. 192: 384-91. PMID 1827964 DOI: 10.1016/0003-2697(91)90553-6 |
0.588 |
|
1991 |
Najbauer J, Johnson BA, Aswad DW. Amplification and detection of substrates for protein carboxyl methyltransferases in PC12 cells. Analytical Biochemistry. 197: 412-20. PMID 1785697 DOI: 10.1016/0003-2697(91)90413-N |
0.593 |
|
1991 |
Johnson BA, Ngo SQ, Aswad DW. Widespread phylogenetic distribution of a protein methyltransferase that modifies L-isoaspartyl residues. Biochemistry International. 24: 841-7. PMID 1776952 |
0.529 |
|
1990 |
Najbauer J, Aswad DW. Diversity of methyl acceptor proteins in rat pheochromocytoma (PC12) cells revealed after treatment with adenosine dialdehyde. The Journal of Biological Chemistry. 265: 12717-21. PMID 2373708 |
0.322 |
|
1990 |
Johnson BA, Aswad DW. Fragmentation of isoaspartyl peptides and proteins by carboxypeptidase Y: release of isoaspartyl dipeptides as a result of internal and external cleavage. Biochemistry. 29: 4373-80. PMID 2140948 DOI: 10.1021/Bi00470A017 |
0.557 |
|
1989 |
Johnson BA, Shirokawa JM, Aswad DW. Deamidation of calmodulin at neutral and alkaline pH: quantitative relationships between ammonia loss and the susceptibility of calmodulin to modification by protein carboxyl methyltransferase. Archives of Biochemistry and Biophysics. 268: 276-86. PMID 2912379 DOI: 10.1016/0003-9861(89)90589-4 |
0.517 |
|
1989 |
Henzel WJ, Stults JT, Hsu CA, Aswad DW. The primary structure of a protein carboxyl methyltransferase from bovine brain that selectively methylates L-isoaspartyl sites. The Journal of Biological Chemistry. 264: 15905-11. PMID 2777770 |
0.389 |
|
1989 |
Johnson BA, Shirokawa JM, Hancock WS, Spellman MW, Basa LJ, Aswad DW. Formation of isoaspartate at two distinct sites during in vitro aging of human growth hormone. The Journal of Biological Chemistry. 264: 14262-71. PMID 2760065 |
0.528 |
|
1989 |
O'Connor CM, Germain BJ, Guthrie KM, Aswad DW, Millette CF. Protein carboxyl methyltransferase activity specific for age-modified aspartyl residues in mouse testes and ovaries: evidence for translation during spermiogenesis. Gamete Research. 22: 307-19. PMID 2707731 DOI: 10.1002/mrd.1120220308 |
0.435 |
|
1989 |
Aswad DW. Protein carboxyl methylation in eukaryotes. Current Opinion in Cell Biology. 1: 1182-7. PMID 2699804 DOI: 10.1016/S0955-0674(89)80069-9 |
0.32 |
|
1988 |
Aswad DW, Johnson BA, Langmack EL, Shirokawa JM. Modification of isoaspartyl peptides and proteins by protein carboxyl methyltransferase from bovine brain. Advances in Experimental Medicine and Biology. 231: 247-59. PMID 3414433 DOI: 10.1007/978-1-4684-9042-8_19 |
0.637 |
|
1987 |
Johnson BA, Langmack EL, Aswad DW. Partial repair of deamidation-damaged calmodulin by protein carboxyl methyltransferase. The Journal of Biological Chemistry. 262: 12283-7. PMID 3624258 |
0.536 |
|
1987 |
Johnson BA, Murray ED, Clarke S, Glass DB, Aswad DW. Protein carboxyl methyltransferase facilitates conversion of atypical L-isoaspartyl peptides to normal L-aspartyl peptides. The Journal of Biological Chemistry. 262: 5622-9. PMID 3571226 |
0.523 |
|
1987 |
Aswad DW, Johnson BA, Glass DB. Modification of synthetic peptides related to lactate dehydrogenase (231-242) by protein carboxyl methyltransferase and tyrosine protein kinase: effects of introducing an isopeptide bond between aspartic acid-235 and serine-236. Biochemistry. 26: 675-81. PMID 3105574 DOI: 10.1021/Bi00377A003 |
0.615 |
|
1987 |
Aswad DW, Johnson BA. The unusual substrate specificity of eukaryotic protein carboxyl methyltransferases Trends in Biochemical Sciences. 12: 155-158. DOI: 10.1016/0968-0004(87)90073-9 |
0.605 |
|
1985 |
Johnson BA, Aswad DW. Identification and topography of substrates for protein carboxyl methyltransferase in synaptic membrane and myelin-enriched fractions of bovine and rat brain. Journal of Neurochemistry. 45: 1119-27. PMID 4031881 DOI: 10.1111/J.1471-4159.1985.Tb05531.X |
0.538 |
|
1985 |
Johnson BA, Freitag NE, Aswad DW. Protein carboxyl methyltransferase selectively modifies an atypical form of calmodulin. Evidence for methylation at deamidated asparagine residues. The Journal of Biological Chemistry. 260: 10913-6. PMID 4030774 |
0.563 |
|
1985 |
Johnson BA, Aswad DW. Enzymatic protein carboxyl methylation at physiological pH: cyclic imide formation explains rapid methyl turnover. Biochemistry. 24: 2581-6. PMID 4016073 DOI: 10.1021/Bi00331A028 |
0.598 |
|
1984 |
Aswad DW. Determination of D- and L-aspartate in amino acid mixtures by high-performance liquid chromatography after derivatization with a chiral adduct of o-phthaldialdehyde. Analytical Biochemistry. 137: 405-9. PMID 6731824 DOI: 10.1016/0003-2697(84)90106-4 |
0.317 |
|
1984 |
O'Connor CM, Aswad DW, Clarke S. Mammalian brain and erythrocyte carboxyl methyltransferases are similar enzymes that recognize both D-aspartyl and L-isoaspartyl residues in structurally altered protein substrates. Proceedings of the National Academy of Sciences of the United States of America. 81: 7757-61. PMID 6595658 DOI: 10.1073/Pnas.81.24.7757 |
0.646 |
|
1984 |
Hemmings HC, Nairn AC, Aswad DW, Greengard P. DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 4: 99-110. PMID 6319628 DOI: 10.1523/Jneurosci.04-01-00099.1984 |
0.651 |
|
1984 |
Detre JA, Nairn AC, Aswad DW, Greengard P. Localization in mammalian brain of G-substrate, a specific substrate for guanosine 3',5'-cyclic monophosphate-dependent protein kinase. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 4: 2843-9. PMID 6094745 DOI: 10.1523/Jneurosci.04-11-02843.1984 |
0.498 |
|
1984 |
Aswad DW. Stoichiometric methylation of porcine adrenocorticotropin by protein carboxyl methyltransferase requires deamidation of asparagine 25. Evidence for methylation at the alpha-carboxyl group of atypical L-isoaspartyl residues. The Journal of Biological Chemistry. 259: 10714-21. PMID 6088513 |
0.357 |
|
1984 |
Detre J, Nairn A, Aswad D, Greengard P. Localization in mammalian brain of G-substrate, a specific substrate for guanosine 3',5'-cyclic monophosphate-dependent protein kinase The Journal of Neuroscience. 4: 2843-2849. DOI: 10.1523/JNEUROSCI.04-11-02843.1984 |
0.577 |
|
1984 |
Hemmings H, Nairn A, Aswad D, Greengard P. DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus The Journal of Neuroscience. 4: 99-110. DOI: 10.1523/JNEUROSCI.04-01-00099.1984 |
0.618 |
|
1984 |
Aswad DW. cGMP-dependent protein phosphorylation in the nervous system Trends in Pharmacological Sciences. 5: 64-66. DOI: 10.1016/0165-6147(84)90369-9 |
0.39 |
|
1983 |
Aswad DW, Deight EA. Purification and characterization of two distinct isozymes of protein carboxymethylase from bovine brain. Journal of Neurochemistry. 40: 1718-26. PMID 6854329 DOI: 10.1111/J.1471-4159.1983.Tb08147.X |
0.468 |
|
1983 |
Aswad DW, Deight EA. Endogenous substrates for protein carboxyl methyltransferase in cytosolic fractions of bovine brain. Journal of Neurochemistry. 41: 1702-9. PMID 6644307 DOI: 10.1111/J.1471-4159.1983.Tb00883.X |
0.49 |
|
1983 |
Walaas SI, Aswad DW, Greengard P. A dopamine- and cyclic AMP-regulated phosphoprotein enriched in dopamine-innervated brain regions. Nature. 301: 69-71. PMID 6296685 DOI: 10.1038/301069a0 |
0.634 |
|
1981 |
Aitken A, Bilham T, Cohen P, Aswad D, Greengard P. A specific substrate from rabbit cerebellum for guanosine-3':5'-monophosphate-dependent protein kinase. III. Amino acid sequences at the two phosphorylation sites Journal of Biological Chemistry. 256: 3501-3506. PMID 6259172 |
0.304 |
|
1981 |
Aswad DW, Greengard P. A specific substrate from rabbit cerebellum for guanosine 3':5'-monophosphate-dependent protein kinase. I. Purification and characterization. The Journal of Biological Chemistry. 256: 3487-93. PMID 6259170 |
0.358 |
|
1981 |
Aitken A, Bilham T, Cohen P, Aswad D, Greengard P. THE SITES OF PHOSPHORYLATION ON C-SUBSTRATE FROM RABBIT CEREBELLUM AND THE MOLECULAR SPECIFICITIES OF CYCLIC CMP- AND CYCLIC AMP-DEPENDENT PROTEIN KINASES Biochemical Society Transactions. 9: 232P-232P. DOI: 10.1042/Bst009232Pc |
0.42 |
|
1980 |
Schlichter DJ, Detre JA, Aswad DW, Chehrazi B, Greengard P. Localization of cyclic GMP-dependent protein kinase and substrate in mammalian cerebellum. Proceedings of the National Academy of Sciences of the United States of America. 77: 5537-41. PMID 6254089 DOI: 10.1073/pnas.77.9.5537 |
0.472 |
|
1975 |
Aswad D, Koshland DE. Isolation, characterization and complementation of Salmonella typhimurium chemotaxis mutants Journal of Molecular Biology. 97: 225-235. PMID 1100857 DOI: 10.1016/S0022-2836(75)80036-2 |
0.336 |
|
1975 |
Aswad DW, Koshland DE. Evidence for an S-adenosylmethionine requirement in the chemotactic behavior of Salmonella typhimurium. Journal of Molecular Biology. 97: 207-23. PMID 1100856 DOI: 10.1016/S0022-2836(75)80035-0 |
0.408 |
|
1974 |
Aswad D, Koshland DE. Role of methionine in bacterial chemotaxis Journal of Bacteriology. 118: 640-645. PMID 4597455 DOI: 10.1128/Jb.118.2.640-645.1974 |
0.358 |
|
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