Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Lynnette C. Johnson"'
Autor:
Tom E. Forshaw, Julie A. Reisz, Kimberly J. Nelson, Rajesh Gumpena, J. Reed Lawson, Thomas J. Jönsson, Hanzhi Wu, Jill E. Clodfelter, Lynnette C. Johnson, Cristina M. Furdui, W. Todd Lowther
Publikováno v:
Antioxidants, Vol 10, Iss 6, p 946 (2021)
Human peroxiredoxins (Prx) are a family of antioxidant enzymes involved in a myriad of cellular functions and diseases. During the reaction with peroxides (e.g., H2O2), the typical 2-Cys Prxs change oligomeric structure between higher order (do)decam
Externí odkaz:
https://doaj.org/article/d55fdb246166416a82421dcc5de5c96d
Autor:
Cristina M. Furdui, Jill E. Clodfelter, J. Reed Lawson, Julie A. Reisz, Hanzhi Wu, W. Todd Lowther, Rajesh Gumpena, Lynnette C. Johnson, Thomas J. Jönsson, Kimberly J. Nelson, Tom E. Forshaw
Publikováno v:
Antioxidants
Antioxidants, Vol 10, Iss 946, p 946 (2021)
Volume 10
Issue 6
Antioxidants, Vol 10, Iss 946, p 946 (2021)
Volume 10
Issue 6
Human peroxiredoxins (Prx) are a family of antioxidant enzymes involved in a myriad of cellular functions and diseases. During the reaction with peroxides (e.g., H2O2), the typical 2-Cys Prxs change oligomeric structure between higher order (do)decam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df55ebfbd319a2cc77be07fa4504987b
https://pubmed.ncbi.nlm.nih.gov/34208049
https://pubmed.ncbi.nlm.nih.gov/34208049
Autor:
Travis J Riedel, Lynnette C Johnson, John Knight, Roy R Hantgan, Ross P Holmes, W Todd Lowther
Publikováno v:
PLoS ONE, Vol 6, Iss 10, p e26021 (2011)
4-hydroxy-2-oxoglutarate (HOG) aldolase is a unique enzyme in the hydroxyproline degradation pathway catalyzing the cleavage of HOG to pyruvate and glyoxylate. Mutations in this enzyme are believed to be associated with the excessive production of ox
Externí odkaz:
https://doaj.org/article/c240ed0aa19144a8b5b3d254279b01cc
Autor:
Jill E. Clodfelter, Brian E. Fulp, Charles W. Pemble, Lynnette C. Johnson, Cristina M. Furdui, Melissa K. Ritchie, W. Todd Lowther, Steven J. Kridel
Publikováno v:
Journal of Biological Chemistry. 291:3520-3530
The type I fatty acid synthase (FASN) is responsible for the de novo synthesis of palmitate. Chain length selection and release is performed by the C-terminal thioesterase domain (TE1). FASN expression is up-regulated in cancer, and its activity leve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::898537d2920e3baf0e1a38a4ae84f56c
https://doi.org/10.1074/jbc.m115.702597
https://doi.org/10.1074/jbc.m115.702597
Autor:
Thomas J. Jönsson, Candice B. Summitt, Derek Parsonage, Ross P. Holmes, W. Todd Lowther, Lynnette C. Johnson
Publikováno v:
Biochemical Journal. 466:273-281
The primary hyperoxalurias (PH), types 1–3, are disorders of glyoxylate metabolism that result in increased oxalate production and calcium oxalate stone formation. The breakdown of trans-4-hydroxy-L-proline (Hyp) from endogenous and dietary sources
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d0cb606a86a52e5b955ab87cc5cf723
https://doi.org/10.1042/bj20141159
https://doi.org/10.1042/bj20141159
Publikováno v:
Journal of Biological Chemistry. 284:33305-33310
Oxidative stress can damage the active site cysteine of the antioxidant enzyme peroxiredoxin (Prx) to the sulfinic acid form, Prx-SO(2)(-). This modification leads to inactivation. Sulfiredoxin (Srx) utilizes a unique ATP-Mg(2+)-dependent mechanism t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f0727c7c1107939342012d39f8de007
https://doi.org/10.1074/jbc.m109.036400
https://doi.org/10.1074/jbc.m109.036400
Publikováno v:
Journal of Biological Chemistry. 283:23846-23851
Sulfiredoxin (Srx) catalyzes a novel enzymatic reaction, the reduction of protein cysteine sulfinic acid, \documentclass[10pt]{article} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepacka
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb2c9c1814703a3ac7bbf654ed76e0d8
https://doi.org/10.1074/jbc.m803244200
https://doi.org/10.1074/jbc.m803244200
Publikováno v:
Nature. 451:98-101
The X-ray crystal structure of peroxiredoxin bound to sulphiredoxin is solved. In this structure of the co-complex, the carboxy terminus of peroxiredoxin is completely unfolded, and it is 'packed' onto the backside of sulphiredoxin, away from the sul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::614f33cecb8aaa7553c2f5f22cc21e9c
https://doi.org/10.1038/nature06415
https://doi.org/10.1038/nature06415
Publikováno v:
Nature Structural & Molecular Biology. 14:704-709
Human fatty acid synthase (FAS) is uniquely expressed at high levels in many tumor types. Pharmacological inhibition of FAS therefore represents an important therapeutic opportunity. The drug Orlistat, which has been approved by the US Food and Drug
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea13940a6a28d4117f25b0fcd49ebfd8
https://doi.org/10.1038/nsmb1265
https://doi.org/10.1038/nsmb1265
Autor:
W. Todd Lowther, Herbert Weissbach, Mark O. Lively, Zhidong Lin, Lynnette C. Johnson, Nathan Brot
Publikováno v:
Proceedings of the National Academy of Sciences. 104:9597-9602
The reduction of methionine sulfoxide (MetO) is mediated by methionine sulfoxide reductases (Msr). The MsrA and MsrB families can reduce free MetO and MetO within a peptide or protein context. This process is stereospecific with the S - and R -forms
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::113f81da00fa2f351b0be43e8e0886ec
https://doi.org/10.1073/pnas.0703774104
https://doi.org/10.1073/pnas.0703774104