B
Bulent Mutus
Researcher at University of Windsor
Publications - 105
Citations - 3381
Bulent Mutus is an academic researcher from University of Windsor. The author has contributed to research in topics: Protein disulfide-isomerase & Nitric oxide. The author has an hindex of 32, co-authored 103 publications receiving 3139 citations. Previous affiliations of Bulent Mutus include University of Science and Technology Beijing & National Republican Congressional Committee.
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Journal ArticleDOI
Mechanism of transfer of NO from extracellular S-nitrosothiols into the cytosol by cell-surface protein disulfide isomerase.
TL;DR: The findings suggest that csPDI catalyzed NO released from extracellular S-nitrosothiols accumulates in the membrane where it reacts with O2 to produce N2O3, which may then be nitrosated by N2 O3 at the membrane-cytosol interface.
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Visible light photochemical release of nitric oxide from S-nitrosoglutathione: potential photochemotherapeutic applications.
TL;DR: The finding that NO can be readily liberated from S‐nitrosoglutathione by visible radiation indicates that the photochemical properties of this compound in the visible spectrum must be considered in order to obtain meaningful data as to its physiological role and the S‐NitrosoglUTathione and related compounds may find use as photochemotherapeutic agents.
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Cytotoxic Activities of Mannich Bases of Chalcones and Related Compounds
Dimmock,Kandepu Nm,Hetherington M,Quail Jw,Pugazhenthi U,Sudom Am,M. Chamankhah,Rose P,Pass E,Allen Tm,Halleran S,Szydlowski J,Bulent Mutus,Tannous M,Elias K. Manavathu,Timothy G. Myers,De Clercq E,Balzarini J +17 more
TL;DR: Various Mannich bases of chalcones and related compounds displayed significant cytotoxicity toward murine P388 and L1210 leukemia cells as well as a number of human tumor cell lines, and 21 in particular serves as an useful prototypic molecule.
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Protein disulfide isomerase a multifunctional protein with multiple physiological roles
Hyder Ali Khan,Bulent Mutus +1 more
TL;DR: This review will provide an overview of the recent advances in relating the structural features of PDI to its multiple catalytic roles as well as its physiological and pathophysiological functions related to redox regulation and protein folding.
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Characterization of the S-denitrosation activity of protein disulfide isomerase.
TL;DR: The present demonstration that PDI can be S-nitrosated and thatPDI-SNO can be denitrosated by PDI suggests that this enzyme could be intimately involved in the transport of intracellular NO equivalents to the cell surface as well as the previous demonstration of PDI in the transfer of S- Nitrosothiol-bound NO to the cytosol.