Interaction of peroxiredoxin V with dihydrolipoamide branched chain transacylase E2 (DBT) in mouse kidney under hypoxia

[1]  H. Choy,et al.  Peroxiredoxin V selectively regulates IL-6 production by modulating the Jak2-Stat5 pathway. , 2013, Free radical biology & medicine.

[2]  V. Haase Mechanisms of hypoxia responses in renal tissue. , 2013, Journal of the American Society of Nephrology : JASN.

[3]  Hyung-Seok Kim,et al.  Comparative proteomic analysis for the insoluble fractions of colorectal cancer patients. , 2012, Journal of proteomics.

[4]  Jean-Paul Declercq,et al.  Peroxiredoxin 5: structure, mechanism, and function of the mammalian atypical 2-Cys peroxiredoxin. , 2011, Antioxidants & redox signaling.

[5]  J. Weinberg Mitochondrial biogenesis in kidney disease. , 2011, Journal of the American Society of Nephrology : JASN.

[6]  Z. Ryoo,et al.  Proteomic analysis of protein expression affected by peroxiredoxin V knock-down in hypoxic kidney. , 2010, Journal of proteome research.

[7]  David W. Smith,et al.  Intrarenal oxygenation: unique challenges and the biophysical basis of homeostasis. , 2008, American journal of physiology. Renal physiology.

[8]  J. Norman,et al.  Chronic hypoxia as a mechanism of progression of chronic kidney diseases: from hypothesis to novel therapeutics. , 2008, Kidney international.

[9]  Y. Sasaguri,et al.  Ets regulates peroxiredoxin1 and 5 expressions through their interaction with the high‐mobility group protein B1 , 2008, Cancer Science.

[10]  Yet-Ran Chen,et al.  A Multiplexed Quantitative Strategy for Membrane Proteomics , 2008, Molecular & Cellular Proteomics.

[11]  André Clippe,et al.  Human peroxiredoxin 5 is a peroxynitrite reductase , 2004, FEBS letters.

[12]  K. Eckardt,et al.  Role of Hypoxia in the Pathogenesis of Renal Disease , 2003, Blood Purification.

[13]  B. Knoops,et al.  Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution. , 2001, Journal of molecular biology.

[14]  Tsutomu Mori,et al.  cDNA cloning of the chicken branched‐chain α‐keto acid dehydrogenase complex , 2001 .

[15]  S. Rhee,et al.  Identification of a New Type of Mammalian Peroxiredoxin That Forms an Intramolecular Disulfide as a Reaction Intermediate* , 2000, The Journal of Biological Chemistry.

[16]  C. Hermans,et al.  Cloning and Characterization of AOEB166, a Novel Mammalian Antioxidant Enzyme of the Peroxiredoxin Family* , 1999, The Journal of Biological Chemistry.

[17]  S. Subramani,et al.  Characterization of Human and Murine PMP20 Peroxisomal Proteins That Exhibit Antioxidant Activity in Vitro * , 1999, The Journal of Biological Chemistry.

[18]  J. Peragón,et al.  Stimulation of rat-liver branched-chain alpha-keto acid dehydrogenase activity by chronic metabolic acidosis. , 1998, The international journal of biochemistry & cell biology.

[19]  A. V. Kropotov,et al.  A human B‐box‐binding protein downregulated in adenovirus 5‐transformed human cells , 1996, FEBS letters.

[20]  D. Chuang,et al.  Characterization and conservation of the inner E2 core domain structure of branched-chain alpha-keto acid dehydrogenase complex from bovine liver. Construction of a cDNA encoding the entire transacylase (E2b) precursor. , 1988, The Journal of biological chemistry.

[21]  L. Reed,et al.  Purification and characterization of branched chain alpha-keto acid dehydrogenase complex of bovine kidney. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[22]  Z. A. Wood,et al.  Structure, mechanism and regulation of peroxiredoxins. , 2003, Trends in biochemical sciences.

[23]  T. Suzuki,et al.  cDNA cloning of the chicken branched-chain alpha-keto acid dehydrogenase complex. Chicken-specific residues of the acyltransferase affect the overall activity and the interaction with the dehydrogenase. , 2001, European Journal of Biochemistry.

[24]  S. Rhee,et al.  Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin. , 1999, Methods in enzymology.