H.J.Kelly Oh, Ph.D.

Research Assistant Professor
Chicago Medical School
Room 3.229
Building: BSB
Phone: 847.578.3000 Extension 3363
Fax: 847.578.3253
kelly.oh@rosalindfranklin.edu
Publications

Sancar F, Touroutine D, Gao S, Oh HJ, Gendrel M, Bessereau JL, Kim H, Zhen M, Richmond JE. The dystrophin-associated protein complex maintains muscle excitability by regulating Ca(2+)-dependent K(+) (BK) channel localization.

Journal of Biological Chemistry 286(38):33501-10, 2011

Abraham LS, Oh HJ, Sancar F., Richmond JE and Kim H. An alpha-catulin homologue controls neuromuscular function through localization of the dystrophin complex and BK channels in Caenorhabditis elegans PLoS Genetics  6(8). pii: e1001077, 2010 (Equal contribution first author)

Kim H, Pierce-Shimomura JT, Oh HJ, Johnson BE, Goodman MB, McIntire SL  The dystrophin complex controls bk channel localization and muscle activity in Caenorhabditis elegans. PLoS Genet. 5(12):e1000780, 2009

Peng H, Psulkowski ED, Gibson LC, Ivanov AV, Oh HJ, Lau Y-FC, and Rauscher III FJ.  A KRAB domain recruits the KAP1 silencing machinery to SRY and functions in gonad differentiation and sex determination. Journal of Biological Chemistry 284(51):35670-80, 2009

Oh HJ, Kido T and Lau Y.-F.C   PIAS1 represses SOX9 activity by a mechanism independent of its SUMO-ligase function for SOX9. Molecular Reproduction and Development 74(11):1446-55, 2007

Li Y., Oh HJ and Lau Y.-F.C.  The Poly (ADP-ribose) Polymerase 1 interacts with Sry and modulates its biological function. Molecular and Cellular Endocrinology 257-258: 35-46, 2006

Oh HJ and Lau Y.-.F. C.  KRAB: A partner for SRY action on chromatin Molecular and Cellular Endocrinology 247, 47-52, 2006

Oh HJ, Li Y. and Lau Y.-F. C.  The mouse Sry interacts with a protein containing the Krueppel-Associated Box (KRAB) domain.  Biology of Reproduction 72(2), 407-415, 2005

Wang XY, Chen X, Oh HJ, Repasky E, Kazim L and Subjeck J Characterization of native interaction of hsp110 with hsp25 and hsc70. FEBS Lett. 465, 98-102, 2000

Henics T, Nagy E, Oh HJ, Csermely P, von Gabain A and Subjeck JR  Mammalian Hsp70 and Hsp110 proteins bind to RNA motifs involved in mRNA stability. Journal of Biological Chemistry.274,17318-17324, 1999

Oh HJ, Easton D, Murrawski M, Kaneko Y and John R. Subjeck. The chaperoning activity of hsp110: Identification of functional domains by use of targeted deletions. Journal of Biological Chemistry.274,15712-15718, 1999

Oh HJ, Xing Chen, and John R. Subjeck. Hsp110 protects heat-denatured proteins and confers cellular thermoresistance. Journal of Biological Chemistry. 272, 31636-31640, 1997

Xing Chen, Douglas Easton, Oh HJ, Dong-Sin Lee-Yoon, Xiaoguang Liu, and John Subjeck.  The 170 Kda glucose regulated stress protein is a large HSP70-, HSP110-like protein of the endoplasmic reticulum. FEBS Letters 380, 68-72, 1996

 

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