Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Suranjana Haldar"'
Autor:
Suranjana Haldar, Atish Haldar
Publikováno v:
A Basic Overview of Environment and Sustainable Development ISBN: 9788195795420
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::067401fdd4b282ff596f7ec4c2104155
https://doi.org/10.52756/boesd.2022.e01.003
https://doi.org/10.52756/boesd.2022.e01.003
Autor:
Edward I. Solomon, Takehiko Tosha, Elizabeth C. Theil, Jennifer K. Schwartz, Yeonju Kwak, Suranjana Haldar, Rabindra K. Behera
Publikováno v:
Biochemistry
Ferritin has a binuclear non-heme iron active site that functions to oxidize iron as a substrate for formation of an iron mineral core. Other enzymes of this class have tightly bound diiron cofactor sites that activate O2 to react with substrate. Fer
Autor:
Mateen A. Khan, Elizabeth C. Theil, Jia Ma, Sohani Das Sharma, Suranjana Haldar, Dixie J. Goss, William C. Merrick
Publikováno v:
Proceedings of the National Academy of Sciences. 109:8417-8422
Iron increases synthesis rates of proteins encoded in iron-responsive element (IRE)-mRNAs; metabolic iron (“free,” “labile”) is Fe 2+ . The noncoding IRE-RNA structure, approximately 30 nt, folds into a stem loop to control synthesis of prote
Publikováno v:
Journal of Biological Chemistry. 286:25620-25627
Eukaryotic H ferritins move iron through protein cages to form biologically required, iron mineral concentrates. The biominerals are synthesized during protein-based Fe2+/O2 oxidoreduction and formation of [Fe3+O]n multimers within the protein cage,
Autor:
Suranjana Haldar, William C. Merrick, Mateen A. Khan, Jia Ma, Elizabeth C. Theil, Dixie J. Goss
Publikováno v:
The FASEB Journal. 26
Autor:
William C. Merrick, Suranjana Haldar, Mateen A. Khan, Jia Ma, Elizabeth C. Theil, Dixie J. Goss
Publikováno v:
The FASEB Journal. 25
Autor:
Lluis Masip, Jonathan L. Pan, George Georgiou, James E. Penner-Hahn, Jean-François Collet, James C.A. Bardwell, Matthew P. DeLisa, Suranjana Haldar
Publikováno v:
Science (New York, N.Y.). 303(5661)
We have engineered a pathway for the formation of disulfide bonds. By imposing evolutionary pressure, we isolated mutations that changed thioredoxin, which is a monomeric disulfide reductase, into a [2Fe-2S] bridged dimer capable of catalyzing O 2 -d