Michael Sinensky - Publications

Affiliations: 
East Tennessee State University, Johnson City, TN, United States 
Area:
Biochemistry, Cell Biology

14 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2011 Sinensky M. Insights into the Function of Prenylation from Nuclear Lamin Farnesylation Enzymes. 29: 5-20. DOI: 10.1016/B978-0-12-381339-8.00002-0  0.395
2000 Sinensky M. Functional aspects of polyisoprenoid protein substituents: Roles in protein-protein interaction and trafficking Biochimica Et Biophysica Acta - Molecular and Cell Biology of Lipids. 1529: 203-209. PMID 11111089 DOI: 10.1016/S1388-1981(00)00149-9  0.344
2000 Sinensky M. Recent advances in the study of prenylated proteins Biochimica Et Biophysica Acta - Molecular and Cell Biology of Lipids. 1484: 93-106. PMID 10760460 DOI: 10.1016/S1388-1981(00)00009-3  0.357
1999 Kilic F, Johnson DA, Sinensky M. Subcellular localization and partial purification of prelamin A endoprotease: An enzyme which catalyzes the conversion of farnesylated prelamin A to mature lamin A Febs Letters. 450: 61-65. PMID 10350058 DOI: 10.1016/S0014-5793(99)00482-2  0.388
1998 Thewke DP, Panini SR, Sinensky M. Oleate potentiates oxysterol inhibition of transcription from sterol regulatory element-1-regulated promoters and maturation of sterol regulatory element-binding proteins Journal of Biological Chemistry. 273: 21402-21407. PMID 9694903 DOI: 10.1074/Jbc.273.33.21402  0.316
1998 Siddiqui AA, Garland JR, Dalton MB, Sinensky M. Evidence for a high affinity, saturable, prenylation-dependent p21(Ha- ras) binding site in plasma membranes Journal of Biological Chemistry. 273: 3712-3717. PMID 9452502 DOI: 10.1074/Jbc.273.6.3712  0.327
1997 Kilic F, Salas-Marco J, Garland J, Sinensky M. Regulation of prelamin A endoprotease activity by prelamin A. Febs Letters. 414: 65-8. PMID 9305733 DOI: 10.1016/S0014-5793(97)00989-7  0.326
1997 Kilic F, Dalton MB, Burrell SK, Mayer JP, Patterson SD, Sinensky M. In vitro assay and characterization of the farnesylation-dependent prelamin A endoprotease Journal of Biological Chemistry. 272: 5298-5304. PMID 9030603 DOI: 10.1074/Jbc.272.8.5298  0.316
1992 Wei C, Lutz R, Sinensky M, Macara IG. p23rab2, a ras-like GTPase with a -GGGCC C-terminus, is isoprenylated but not detectably carboxymethylated in NIH3T3 cells Oncogene. 7: 467-473. PMID 1549360  0.302
1991 Khosravi-Far R, Lutz RJ, Cox AD, Conroy L, Bourne JR, Sinensky M, Balch WE, Buss JE, Der CJ. Isoprenoid modification of rab proteins terminating in CC or CXC motifs. Proceedings of the National Academy of Sciences of the United States of America. 88: 6264-8. PMID 1648736 DOI: 10.1073/Pnas.88.14.6264  0.391
1979 Sinensky M, Pinkerton F, Sutherland E, Simon FR. Rate limitation of (Na+ + K+)-stimulated adenosinetriphosphatase by membrane acyl chain ordering Proceedings of the National Academy of Sciences of the United States of America. 76: 4893-4897. PMID 228269 DOI: 10.1073/Pnas.76.10.4893  0.335
1978 Sinensky M. Defective regulation of cholesterol biosynthesis and plasma membrane fluidity in a Chinese hamster ovary cell mutant Proceedings of the National Academy of Sciences of the United States of America. 75: 1247-1249. PMID 274716 DOI: 10.1073/Pnas.75.3.1247  0.331
1978 Davis RA, Kern F, Showalter R, Sutherland E, Sinensky M, Simon FR. Alterations of hepatic Na +,K +-ATPase and bile flow by estrogen: effects on liver surface membrane lipid structure and function Proceedings of the National Academy of Sciences of the United States of America. 75: 4130-4134. PMID 212735 DOI: 10.1073/Pnas.75.9.4130  0.341
1974 Sinensky M. Homeoviscous adaptation: a homeostatic process that regulates the viscosity of membrane lipids in Escherichia coli Proceedings of the National Academy of Sciences of the United States of America. 71: 522-525. PMID 4360948 DOI: 10.1073/Pnas.71.2.522  0.311
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