Arun Radhakrishnan - Publications

Affiliations: 
Molecular Genetics University of Texas Southwestern Medical Center, Dallas, TX, United States 
Area:
Regulation of cellular cholesterol, Protein sensors for membrane cholesterol and sphingomyelin
Website:
http://www.utsouthwestern.edu/fis/faculty/57962/arun-radhakrishnan.html

62 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
2024 Xu S, Donnelly L, Kober DL, Mak M, Radhakrishnan A. Development of a monoclonal antibody to study MARCH6, an E3 ligase that regulates proteins that control lipid homeostasis. Journal of Lipid Research. 100650. PMID 39306038 DOI: 10.1016/j.jlr.2024.100650  0.306
2024 Xu S, Smothers JC, Rye D, Endapally S, Chen H, Li S, Liang G, Kinnebrew M, Rohatgi R, Posner BA, Radhakrishnan A. A cholesterol-binding bacterial toxin provides a strategy for identifying a specific Scap inhibitor that blocks lipid synthesis in animal cells. Proceedings of the National Academy of Sciences of the United States of America. 121: e2318024121. PMID 38330014 DOI: 10.1073/pnas.2318024121  0.829
2023 Heisler DB, Johnson KA, Ma DH, Ohlson MB, Zhang L, Tran M, Corley CD, Abrams ME, McDonald JG, Schoggins JW, Alto NM, Radhakrishnan A. A concerted mechanism involving ACAT and SREBPs by which oxysterols deplete accessible cholesterol to restrict microbial infection. Elife. 12. PMID 36695568 DOI: 10.7554/eLife.83534  0.758
2022 Kinnebrew M, Johnson KA, Radhakrishnan A, Rohatgi R. Measuring and Manipulating Membrane Cholesterol for the Study of Hedgehog Signaling. Methods in Molecular Biology (Clifton, N.J.). 2374: 73-87. PMID 34562244 DOI: 10.1007/978-1-0716-1701-4_7  0.788
2021 Kinnebrew M, Luchetti G, Sircar R, Frigui S, Viti LV, Naito T, Beckert F, Saheki Y, Siebold C, Radhakrishnan A, Rohatgi R. Patched 1 reduces the accessibility of cholesterol in the outer leaflet of membranes. Elife. 10. PMID 34698632 DOI: 10.7554/eLife.70504  0.589
2021 Kober DL, Radhakrishnan A, Goldstein JL, Brown MS, Clark LD, Bai XC, Rosenbaum DM. Scap structures highlight key role for rotation of intertwined luminal loops in cholesterol sensing. Cell. PMID 34139175 DOI: 10.1016/j.cell.2021.05.019  0.576
2021 Johnson KA, Radhakrishnan A. The use of anthrolysin O and ostreolysin A to study cholesterol in cell membranes. Methods in Enzymology. 649: 543-566. PMID 33712199 DOI: 10.1016/bs.mie.2021.01.011  0.78
2020 Abrams ME, Johnson KA, Radhakrishnan A, Alto NM. Accessible cholesterol is localized in bacterial plasma membrane protrusions. Journal of Lipid Research. 61: 1538. PMID 33531234 DOI: 10.1194/jlr.ILR120000891  0.733
2020 Radhakrishnan A, Rohatgi R, Siebold C. Cholesterol access in cellular membranes controls Hedgehog signaling. Nature Chemical Biology. 16: 1303-1313. PMID 33199907 DOI: 10.1038/s41589-020-00678-2  0.513
2020 Kober DL, Xu S, Li S, Bajaj B, Liang G, Rosenbaum DM, Radhakrishnan A. Identification of a degradation signal at the carboxy terminus of SREBP2: A new role for this domain in cholesterol homeostasis. Proceedings of the National Academy of Sciences of the United States of America. PMID 33106423 DOI: 10.1073/pnas.2018578117  0.44
2020 Abrams ME, Johnson KA, Radhakrishnan A, Alto NM. Accessible cholesterol is localized in bacterial plasma membrane protrusions. Journal of Lipid Research. PMID 32661016 DOI: 10.1194/Jlr.Ilr120000891  0.756
2020 Johnson KA, Radhakrishnan A. Accessibility of cholesterol at cell surfaces. Journal of Lipid Research. PMID 32327483 DOI: 10.1194/Jlr.Ilr120000836  0.683
2020 Abrams ME, Johnson KA, Perelman SS, Zhang LS, Endapally S, Mar KB, Thompson BM, McDonald JG, Schoggins JW, Radhakrishnan A, Alto NM. Oxysterols provide innate immunity to bacterial infection by mobilizing cell surface accessible cholesterol. Nature Microbiology. PMID 32284563 DOI: 10.1038/S41564-020-0701-5  0.832
2020 Wang X, Cai B, Yang X, Sonubi OO, Zheng Z, Ramakrishnan R, Shi H, Valenti L, Pajvani UB, Sandhu J, Infante RE, Radhakrishnan A, Covey DF, Guan KL, Buck J, et al. Cholesterol Stabilizes TAZ in Hepatocytes to Promote Experimental Non-alcoholic Steatohepatitis. Cell Metabolism. PMID 32259482 DOI: 10.1016/J.Cmet.2020.03.010  0.546
2020 Wang X, Radhakrishnan A, Covey D, Horton J, Schwabe R, Tontonoz P, Guan K, Tabas I. Abstract B04: Hepatic cholesterol upregulates TAZ in nonalcoholic steatohepatitis Molecular Cancer Research. 18. DOI: 10.1158/1557-3125.Hippo19-B04  0.507
2019 Kinnebrew M, Iverson EJ, Patel BB, Pusapati GV, Kong JH, Johnson KA, Luchetti G, Eckert KM, McDonald JG, Covey DF, Siebold C, Radhakrishnan A, Rohatgi R. Cholesterol accessibility at the ciliary membrane controls Hedgehog signaling. Elife. 8. PMID 31657721 DOI: 10.7554/Elife.50051  0.796
2019 Johnson KA, Endapally S, Vazquez DC, Infante RE, Radhakrishnan A. Ostreolysin A and anthrolysin O use different mechanisms to control movement of cholesterol from the plasma membrane to the endoplasmic reticulum. The Journal of Biological Chemistry. PMID 31597703 DOI: 10.1074/Jbc.Ra119.010393  0.843
2019 Endapally S, Infante RE, Radhakrishnan A. Monitoring and Modulating Intracellular Cholesterol Trafficking Using ALOD4, a Cholesterol-Binding Protein. Methods in Molecular Biology (Clifton, N.J.). 1949: 153-163. PMID 30790255 DOI: 10.1007/978-1-4939-9136-5_12  0.854
2019 Endapally S, Frias D, Grzemska M, Gay A, Tomchick DR, Radhakrishnan A. Molecular Discrimination between Two Conformations of Sphingomyelin in Plasma Membranes. Cell. PMID 30712872 DOI: 10.1016/J.Cell.2018.12.042  0.803
2019 Kinnebrew M, Iverson EJ, Patel BB, Pusapati GV, Kong JH, Johnson KA, Luchetti G, Eckert KM, McDonald JG, Covey DF, Siebold C, Radhakrishnan A, Rohatgi R. Author response: Cholesterol accessibility at the ciliary membrane controls hedgehog signaling Elife. DOI: 10.7554/Elife.50051.025  0.722
2018 Endapally S, Frias D, Tomchick D, Radhakrishnan A. Sphingomyelin-Cholesterol Complexes in Plasma Membranes Biophysical Journal. 114. DOI: 10.1016/J.Bpj.2017.11.3750  0.832
2017 Brown MS, Radhakrishnan A, Goldstein JL. Retrospective on Cholesterol Homeostasis: The Central Role of Scap. Annual Review of Biochemistry. PMID 28841344 DOI: 10.1146/Annurev-Biochem-062917-011852  0.735
2017 Infante RE, Radhakrishnan A. Continuous transport of a small fraction of plasma membrane cholesterol to endoplasmic reticulum regulates total cellular cholesterol. Elife. 6. PMID 28414269 DOI: 10.7554/Elife.25466  0.67
2017 Gao Y, Zhou Y, Goldstein JL, Brown MS, Radhakrishnan A. Cholesterol-induced conformation changes in the sterol-sensing domain of the scap protein suggest feedback mechanism to control cholesterol synthesis. The Journal of Biological Chemistry. PMID 28377508 DOI: 10.1074/Jbc.M117.783894  0.728
2017 Chakrabarti RS, Ingham SA, Kozlitina J, Gay A, Cohen JC, Radhakrishnan A, Hobbs HH. Variability of cholesterol accessibility in human red blood cells measured using a bacterial cholesterol-binding toxin Elife. PMID 28169829 DOI: 10.7554/eLife.23355  0.607
2017 Chakrabarti RS, Ingham SA, Kozlitina J, Gay A, Cohen JC, Radhakrishnan A, Hobbs HH. Variability of cholesterol accessibility in human red blood cells measured using a bacterial cholesterol-binding toxin. Elife. 6. PMID 28169829 DOI: 10.7554/Elife.23355  0.832
2017 Infante RE, Radhakrishnan A. Author response: Continuous transport of a small fraction of plasma membrane cholesterol to endoplasmic reticulum regulates total cellular cholesterol Elife. DOI: 10.7554/Elife.25466.013  0.668
2017 Chakrabarti RS, Ingham SA, Kozlitina J, Cohen JC, Radhakrishnan A, Hobbs HH. Author response: Variability of cholesterol accessibility in human red blood cells measured using a bacterial cholesterol-binding toxin Elife. DOI: 10.7554/Elife.23355.022  0.542
2016 Zhang Y, Lee KM, Kinch LN, Clark L, Grishin NV, Rosenbaum DM, Brown MS, Goldstein JL, Radhakrishnan A. Direct Demonstration that Loop1 of Scap Binds to Loop7, a crucial event in cholesterol homeostasis. The Journal of Biological Chemistry. PMID 27068746 DOI: 10.1074/Jbc.M116.729798  0.594
2015 Ren R, Zhou X, He Y, Ke M, Wu J, Liu X, Yan C, Wu Y, Gong X, Lei X, Yan SF, Radhakrishnan A, Yan N. PROTEIN STRUCTURE. Crystal structure of a mycobacterial Insig homolog provides insight into how these sensors monitor sterol levels. Science (New York, N.Y.). 349: 187-91. PMID 26160948 DOI: 10.1126/Science.Aab1091  0.363
2015 Gay A, Rye D, Radhakrishnan A. Switch-like responses of two cholesterol sensors do not require protein oligomerization in membranes. Biophysical Journal. 108: 1459-69. PMID 25809258 DOI: 10.1016/J.Bpj.2015.02.008  0.849
2015 Subramaniam S, Radhakrishnan A, Chakravarthi S, Palanisamy UD, Haleagrahara N. Antihyperglycemic effects of Nephelium lappaceum rind extract in high fat-induced diabetic rats International Journal of Pharmacology. 11: 542-551. DOI: 10.3923/ijp.2015.542.551  0.353
2014 Das A, Brown MS, Anderson DD, Goldstein JL, Radhakrishnan A. Three pools of plasma membrane cholesterol and their relation to cholesterol homeostasis. Elife. 3. PMID 24920391 DOI: 10.7554/Elife.02882  0.745
2013 Das A, Goldstein JL, Anderson DD, Brown MS, Radhakrishnan A. Use of mutant 125I-perfringolysin O to probe transport and organization of cholesterol in membranes of animal cells. Proceedings of the National Academy of Sciences of the United States of America. 110: 10580-5. PMID 23754385 DOI: 10.1073/Pnas.1309273110  0.76
2013 Radhakrishnan A. Cholesterol Sensing in Membranes Biophysical Journal. 104: 4-4. DOI: 10.1016/J.Bpj.2012.11.2412  0.705
2010 Sokolov A, Radhakrishnan A. Accessibility of cholesterol in endoplasmic reticulum membranes and activation of SREBP-2 switch abruptly at a common cholesterol threshold. The Journal of Biological Chemistry. 285: 29480-90. PMID 20573965 DOI: 10.1074/Jbc.M110.148254  0.727
2010 Radhakrishnan A. Phase separations in binary and ternary cholesterol-phospholipid mixtures. Biophysical Journal. 98: L41-3. PMID 20441733 DOI: 10.1016/J.Bpj.2010.01.005  0.386
2010 Radhakrishnan A, Sun LP, Espenshade PJ, Goldstein JL, Brown MS. The SREBP pathway. gene regulation through sterol sensing and gated protein trafficking Handbook of Cell Signaling, 2/E. 3: 2505-2510. DOI: 10.1016/B978-0-12-374145-5.00298-9  0.337
2009 Abi-Mosleh L, Infante RE, Radhakrishnan A, Goldstein JL, Brown MS. Cyclodextrin overcomes deficient lysosome-to-endoplasmic reticulum transport of cholesterol in Niemann-Pick type C cells. Proceedings of the National Academy of Sciences of the United States of America. 106: 19316-21. PMID 19884502 DOI: 10.1073/Pnas.0910916106  0.746
2009 Infante R, Wang M, Radhakrishnan A, Kwon H, Brown M, Goldstein J. 69. NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a potential step in cholesterol egress from lysosomes Molecular Genetics and Metabolism. 96: S27. DOI: 10.1016/J.Ymgme.2008.11.070  0.736
2008 Radhakrishnan A, Goldstein JL, McDonald JG, Brown MS. Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol: a delicate balance. Cell Metabolism. 8: 512-21. PMID 19041766 DOI: 10.1016/J.Cmet.2008.10.008  0.736
2008 Infante RE, Wang ML, Radhakrishnan A, Kwon HJ, Brown MS, Goldstein JL. NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes. Proceedings of the National Academy of Sciences of the United States of America. 105: 15287-92. PMID 18772377 DOI: 10.1073/Pnas.0807328105  0.727
2008 McConnell H, Radhakrishnan A. Molecular motion at the critical point in lipid membranes. Biophysical Journal. 95: L22-4. PMID 18487306 DOI: 10.1529/Biophysj.108.134858  0.557
2008 Infante RE, Abi-Mosleh L, Radhakrishnan A, Dale JD, Brown MS, Goldstein JL. Purified NPC1 protein. I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein. The Journal of Biological Chemistry. 283: 1052-63. PMID 17989073 DOI: 10.1074/Jbc.M707943200  0.668
2008 Infante RE, Radhakrishnan A, Abi-Mosleh L, Kinch LN, Wang ML, Grishin NV, Goldstein JL, Brown MS. Purified NPC1 protein: II. Localization of sterol binding to a 240-amino acid soluble luminal loop. The Journal of Biological Chemistry. 283: 1064-75. PMID 17989072 DOI: 10.1074/Jbc.M707944200  0.631
2007 Radhakrishnan A, McConnell H. Composition fluctuations, chemical exchange, and nuclear relaxation in membranes containing cholesterol. The Journal of Chemical Physics. 126: 185101. PMID 17508832 DOI: 10.1063/1.2730805  0.641
2007 Radhakrishnan A, Ikeda Y, Kwon HJ, Brown MS, Goldstein JL. Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: oxysterols block transport by binding to Insig. Proceedings of the National Academy of Sciences of the United States of America. 104: 6511-8. PMID 17428920 DOI: 10.1073/Pnas.0700899104  0.6
2006 McConnell H, Radhakrishnan A. Theory of the deuterium NMR of sterol-phospholipid membranes. Proceedings of the National Academy of Sciences of the United States of America. 103: 1184-9. PMID 16432189 DOI: 10.1073/Pnas.0510514103  0.651
2005 Radhakrishnan A, McConnell H. Condensed complexes in vesicles containing cholesterol and phospholipids. Proceedings of the National Academy of Sciences of the United States of America. 102: 12662-6. PMID 16120676 DOI: 10.1073/Pnas.0506043102  0.685
2005 Feramisco JD, Radhakrishnan A, Ikeda Y, Reitz J, Brown MS, Goldstein JL. Intramembrane aspartic acid in SCAP protein governs cholesterol-induced conformational change. Proceedings of the National Academy of Sciences of the United States of America. 102: 3242-7. PMID 15728349 DOI: 10.1073/Pnas.0500206102  0.674
2004 Radhakrishnan A, Sun LP, Kwon HJ, Brown MS, Goldstein JL. Direct binding of cholesterol to the purified membrane region of SCAP: mechanism for a sterol-sensing domain. Molecular Cell. 15: 259-68. PMID 15260976 DOI: 10.1016/J.Molcel.2004.06.019  0.708
2003 McConnell HM, Radhakrishnan A. Condensed complexes of cholesterol and phospholipids. Biochimica Et Biophysica Acta. 1610: 159-73. PMID 12648771 DOI: 10.1016/S0005-2736(03)00015-4  0.663
2002 Radhakrishnan A, McConnell HM. Critical points in charged membranes containing cholesterol. Proceedings of the National Academy of Sciences of the United States of America. 99: 13391-6. PMID 12368466 DOI: 10.1073/Pnas.212522699  0.655
2002 Okonogi TM, Radhakrishnan A, McConnell HM. Two fatty acids can replace one phospholipid in condensed complexes with cholesterol. Biochimica Et Biophysica Acta. 1564: 1-4. PMID 12100988 DOI: 10.1016/S0005-2736(02)00451-0  0.549
2002 Radhakrishnan A, McConnell HM. Thermal dissociation of condensed complexes of cholesterol and phospholipid Journal of Physical Chemistry B. 106: 4755-4762. DOI: 10.1021/Jp013932D  0.634
2001 Radhakrishnan A, Li XM, Brown RE, McConnell HM. Stoichiometry of cholesterol-sphingomyelin condensed complexes in monolayers. Biochimica Et Biophysica Acta. 1511: 1-6. PMID 11248199 DOI: 10.1016/S0005-2736(01)00274-7  0.658
2000 Radhakrishnan A, Anderson TG, McConnell HM. Condensed complexes, rafts, and the chemical activity of cholesterol in membranes. Proceedings of the National Academy of Sciences of the United States of America. 97: 12422-7. PMID 11050164 DOI: 10.1073/Pnas.220418097  0.67
2000 Radhakrishnan A, McConnell HM. Chemical activity of cholesterol in membranes. Biochemistry. 39: 8119-24. PMID 10889017 DOI: 10.1021/Bi0005097  0.697
2000 Radhakrishnan A, McConnell HM. Electric field effect on cholesterol-phospholipid complexes. Proceedings of the National Academy of Sciences of the United States of America. 97: 1073-8. PMID 10655486 DOI: 10.1073/Pnas.97.3.1073  0.629
2000 Keller SL, Radhakrishnan A, McConnell HM. Saturated phospholipids with high melting temperatures form complexes with cholesterol in monolayers Journal of Physical Chemistry B. 104: 7522-7527. DOI: 10.1021/Jp000958G  0.691
1999 Radhakrishnan A, McConnell HM. Condensed complexes of cholesterol and phospholipids. Biophysical Journal. 77: 1507-17. PMID 10465761 DOI: 10.1016/S0006-3495(99)76998-5  0.605
1999 Radhakrishnan A, McConnell HM. Cholesterol - Phospholipid complexes in membranes Journal of the American Chemical Society. 121: 486-487. DOI: 10.1021/Ja9835537  0.747
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