44. Oxysterols provide innate immunity to bacterial infection by mobilizing cell surface accessible cholesterol.

Abrams, M.E., Johnson, K.A., Perelman, S.S., Zhang, L., Endapally, S., Mar, K.B., Thompson, B.M., McDonald, J.G., Schoggins, J.W., Radhakrishnan, A., and Alto, N.M.

Nature Microbiology 5, 929-942.

See News & Views: Andrews, N. W. Cholesterol access aids pathogen spread. 

See News & Views:Dang, E.V., Madhani, H.D., and Vance, R.E. Cholesterol in quarantine. 

 

43. Cholesterol stabilizes TAZ in hepatocytes to promote experimental non-alcoholic steatoheptatitis.

Wang, X., Cai, B., Yang, X., Sonubi, O.O., Zheng, Z., Ramakrishnan, R., Shi, H., Valenti, L., Pajvani, U.B., Sandhu, J., Infante, R.E., Radhakrishnan, A., Covey, D.F., Guan, K-L., Buck, J., Levin, L.R., Tontonoz, P., Schwabe, R.F., and Tabas, I.

Cell Metabolism 31, 969-986.

42. Cholesterol accessibility at the ciliary membrane controls Hedgehog signaling.

Kinnebrew, M., Iverson, E.J., Patel, B.B., Pusapati, G.V., Kong, J.H., Johnson, K.A., Luchetti, G., Eckert, K.M., McDonald, J.G., Covey, D.F., Siebold, C., Radhakrishnan, A., and Rohatgi, R.

eLife 2019; 8:e50051.

 

41. Ostreolysin A and anthrolysin O use different mechanisms to control movement of cholesterol from the plasma membrane to the endoplasmic reticulum.

Johnson, K.A., Endapally S., Vazquez, D.C., Infante, R.E., and Radhakrishnan, A.

Biol. Chem. 294, 17289-17300.

 

40. Monitoring and modulating intracellular cholesterol trafficking using ALOD4, a cholesterol-binding protein.

Endapally, S., Infante, R.E., and Radhakrishnan, A.

Methods Mol. Biol. 1949, 153-163.

 

39. Molecular discrimination between two conformations of sphingomyelin in plasma membranes.

Endapally, S., Frias, D., Grzemska, M., Gay, A., Tomchick, D.R., and Radhakrishnan, A.

Cell 176, 1040-1053.

2018

38. Retrospective on cholesterol homeostasis: The central role of Scap.

Brown, M.S., Radhakrishnan, A., and Goldstein, J.L.

Annu. Rev. Biochem. 87, 783-807.

2017

37. Continuous transport of a small fraction of plasma membrane cholesterol to endoplasmic reticulum regulates total cellular cholesterol.

Infante, R.E., and Radhakrishnan, A.

eLife 2017; 6:e25466.

 

36. Cholesterol-induced conformational changes in the sterol-sensing domain of the Scap protein suggest feedback mechanism to control cholesterol synthesis.  

Gao, Y., Zhou, Y., Goldstein, J.L., Brown, M.S., and Radhakrishnan, A. 

Biol. Chem. 292, 8729-8737.

 

35. Variability of cholesterol accessibility in human red blood cells measured using a bacterial cholesterol-binding toxin.

Chakrabarti, R.S., Ingham, S.A., Kozlitina, J., Gay, A., Cohen, J.C., Radhakrishnan, A., and Hobbs, H.H. 

eLife 2017; 6:e23355.

2016

34. Direct demonstration that Loop1 of Scap binds to Loop7:  A crucial event in cholesterol homeostasis.

Zhang, Y., Lee, K.M., Kinch, L.N., Clark, L., Grishin, N.V., Rosenbaum, D.M., Brown, M.S., Goldstein, J.L., and Radhakrishnan, A. 

Biol. Chem. 291, 12888-12896.

2015

33. Crystal structure of a mycobacterial Insig homolog provides insight into how these sensors monitor sterol levels.  

Ren, R., Zhou, X., He, Y., Ke, M., Wu, J., Liu, X., Yan, C., Wu, Y., Gong, X., Lei, X., Yan, F.S., Radhakrishnan, A., and Yan, N. 

Science 349, 187-191.

 

32. Switch-like responses of two cholesterol sensors do not require protein oligomerization in membranes.

Gay, A., Rye, D., and Radhakrishnan, A.

Biophys. J. 108, 1459-1469.

2014

31. Three pools of plasma membrane cholesterol and their relation to cholesterol homeostasis.

Das, A., Brown, M.S., Anderson, D.D., Goldstein, J.L., and Radhakrishnan, A.

eLife 2014; 3:e02882.

2013

30. Use of mutant ¹²⁵I-Perfringolysin O to probe transport and organization of cholesterol in membranes of animal cells.  

Das, A., Goldstein, J.L., Anderson, D.D., Brown, M.S., and Radhakrishnan, A.

Proc. Natl. Acad. Sci. USA. 110, 10580-10585.

Prior to 2013

29. Accessibility of cholesterol in endoplasmic reticulum membranes and activation of SREBP-2 switch abruptly at a common cholesterol threshold.

Sokolov, A., and Radhakrishnan, A.

Biol. Chem. 285, 29480-29490. (2010).

See Commentary:  Wattenberg, B. (2010).  Hyperactive cholesterol breaks free to signal enough is enough.  ASBMB Lipid Corner, 15 July 2010.

 

28. Phase separations in binary and ternary cholesterol-phospholipid mixtures.

Radhakrishnan, A.

Biophys. J. 98, L41-L43. (2010).

 

27. Cyclodextrin overcomes deficient lysosome-to-endoplasmic reticulum transport of cholesterol in Niemann-Pick type C cells.

Abi-Mosleh, L., Infante, R.E., Radhakrishnan, A., Goldstein, J.L., and Brown, M.S.

Proc. Natl. Acad. Sci. USA. 106, 19316-19321.  (2009).

 

26. The SREBP Pathway: Gene regulation through sterol sensing and gated protein trafficking.

Radhakrishnan, A., Sun, L., Espenshade, P.J., Goldstein, J.L., and Brown, M.S

In Handbook of Cell Signaling, 2^nd edition (edited by R. Bradshaw and E. Dennis). Academic Press Inc., New York, Chapter 298, 2505-2510. (2009). 

 

25. Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol.

Radhakrishnan, A., Goldstein, J.L., McDonald, J.G., and Brown, M.S.

Cell Metabolism 8, 512-521. (2008)

See Preview: Hampton, R.Y. (2008). A cholesterol toggle switch.  

 

24. NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes.

Infante, R.E., Wang, M.L., Radhakrishnan, A., Kwon, H.J., Brown, M.S., and Goldstein, J.L. 

Proc. Natl. Acad. Sci. USA. 105, 15287-15292. (2008).

See Commentary:  Subramanian, K., and Balch, W.E. (2008). NPC1/NPC2 function as a tag team duo to mobilize cholesterol.

 

23. Molecular motion at the critical point in lipid membranes. 

McConnell, H., and Radhakrishnan, A.

Biophys. J. 95, L22-L24. (2008).

 

22. Purified NPC1 protein: II. Localization of sterol binding to a 240-amino acid soluble luminal loop.

Infante, R.E., Radhakrishnan, A., Abi-Mosleh, L., Kinch, L.N., Wang, M.L., Grishin, N.V., Goldstein, J.L., and Brown, M.S.

Biol. Chem. 283, 1064-1075. (2008).

 

21. Purified NPC1 protein: I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein.

Infante, R.E., Abi-Mosleh, L., Radhakrishnan, A., Dale, J.D., Brown, M.S., and Goldstein, J.L.

Biol. Chem. 283, 1052-1063. (2008).

 

20. Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: I. Oxysterols block transport by binding to Insigs.

Radhakrishnan, A., Ikeda, Y., Kwon, H.J., Brown, M.S., and Goldstein, J.L.

Proc. Natl. Acad. Sci. USA. 104, 6511-6518. (2007).

See Commentary:  Schekman, R. (2007). How sterols regulate protein sorting and traffic.

 

19. Composition fluctuations, chemical exchange and nuclear relaxation in membranes containing cholesterol.

Radhakrishnan, A., and McConnell, H.

Chem. Phys. 126, 185101. (2007).

 

18. Theory of the deuterium NMR of sterol-phospholipid membranes.

McConnell H., and Radhakrishnan, A.

Proc. Natl. Acad. Sci. USA. 103, 1184-1189. (2006).

 

17. Condensed complexes in vesicles containing cholesterol and phospholipids.

Radhakrishnan, A., and McConnell H.

Proc. Natl. Acad. Sci. USA. 102, 12662-12666. (2005).

 

16. Intramembrane aspartic acid in Scap protein governs cholesterol-mediated conformational change.

Feramisco, J.D., Radhakrishnan, A., Ikeda, Y., Reitz, J., Brown, M.S. and Goldstein, J.L.

Proc. Natl. Acad. Sci. USA. 102, 3242-3247. (2005).

 

15. Direct binding of cholesterol to the purified membrane region of SCAP: Mechanism for a sterol-sensing domain.

Radhakrishnan, A., Sun, L., Kwon, H.J., Brown, M.S., and Goldstein, J.L.

Molecular Cell 15, 259-268. (2004).

 

14. Condensed complexes of cholesterol and phospholipid.

McConnell, H.M., and Radhakrishnan, A.

BBA Reviews 1610, 159-173. (2003).

 

13. Critical points in charged membranes containing cholesterol.

Radhakrishnan, A., and McConnell, H.M.

Proc. Natl. Acad. Sci. USA. 99, 13391-13396. (2002).

 

12. Two fatty acids can replace one phospholipid in condensed complexes with cholesterol.

Okonogi, T.M., Radhakrishnan, A., and McConnell, H.M.

Biochem. Biophys. Acta 1564, 1-4. (2002).   

 

11. Thermal dissociation of condensed complexes of cholesterol and phospholipid.

Radhakrishnan, A., and McConnell, H.M.

Phys. Chem. B 106, 4755-4762. (2002).

 

10. Stoichiometry of cholesterol-sphingomyelin condensed complexes in monolayers.

Radhakrishnan, A., Li, X., Brown, R.E., and McConnell, H.M.

Biochem. Biophys. Acta 1511, 1-6. (2001).

 

9. Condensed complexes, rafts and the chemical activity of cholesterol.

Radhakrishnan, A., Anderson, T.G., and McConnell, H.M.

Proc. Natl. Acad. Sci. USA. 97, 12422-12427. (2000).

 

8. Saturated phospholipids with high melting temperatures form complexes with cholesterol in monolayers.

Keller, S.L., Radhakrishnan, A., and McConnell, H.M.

Phys. Chem. B 104, 7522-7527. (2000).

 

7. Chemical activity of cholesterol in membranes.

Radhakrishnan, A., and McConnell, H.M.

Biochemistry 39, 8119-8124. (2000).

 

6. Electric field effect on cholesterol-phospholipid complexes.

Radhakrishnan, A., and McConnell, H.M.

Proc. Natl. Acad. Sci. USA. 97, 1073-1078. (2000).

 

5. Condensed complexes of cholesterol and phospholipids.

Radhakrishnan, A., and McConnell, H.M.

Biophys. J. 77, 1507-1517. (1999).

 

4. Cholesterol-phospholipid complexes in membranes.

Radhakrishnan, A., and McConnell, H.M.

Am. Chem. Soc. 121, 486-487. (1999).

 

3. Ultra-high throughput rotary capillary array electrophoresis scanner for fluorescent DNA sequencing and analysis.

Scherer, J.R., Kheterpal, I. Radhakrishnan, A., Ja, W.W., and Mathies, R.A.

Electrophoresis 20, 1508-1517. (1999).

 

2. DNA sequencing using a four-color confocal fluorescence capillary array scanner.

Kheterpal, I., Scherer, J.R., Clark, S.M., Radhakrishnan, A., Ju, J., Ginther, C.L., Sensabaugh, G.F., and Mathies, R.A.

Electrophoresis 17, 1852-1859. (1996). 

 

1. DNA sequencing using four-color capillary array electrophoresis and energy transfer primers.

Kheterpal, I., Ju, J., Radhakrishnan, A., Brandt, G.S., Ginther, C.L., Clark, S.M., Scherer, J.R., Sensabaugh, G.F., and Mathies, R.A.

Ultrasensitive Biochemical Diagnostics – Proceedings of the International Society for Optical Engineering-SPIE 2680, 204-213. (1996).