Year |
Citation |
Score |
2023 |
Potter M, Debnath S, Drover MW, Rondeau-Gagné S, Mutus B. An Azomethine-H-Based Fluorogenic Sensor for Formic Acid. Acs Applied Materials & Interfaces. PMID 37671912 DOI: 10.1021/acsami.3c09522 |
0.596 |
|
2022 |
Awada A, Potter M, Wijerathne D, Gauld JW, Mutus B, Rondeau-Gagné S. Conjugated Polymer Nanoparticles as a Universal High-Affinity Probe for the Selective Detection of Microplastics. Acs Applied Materials & Interfaces. 14: 46562-46568. PMID 36194585 DOI: 10.1021/acsami.2c12338 |
0.699 |
|
2019 |
Mutus B. The catalytic mechanism for NO production by the mitochondrial enzyme, sulfite oxidase. The Biochemical Journal. 476: 1955-1956. PMID 31308158 DOI: 10.1042/Bcj20190338 |
0.333 |
|
2019 |
Onukwue N, Ventimiglia L, Potter Sara Aljoudi M, Mutus B. Simple Fluorescent Reagents for Monitoring Disulfide Reductase and S-Nitroso Reductase Activities in vitro and in Live Cells in Culture. Methods (San Diego, Calif.). PMID 31278980 DOI: 10.1016/J.Ymeth.2019.06.028 |
0.317 |
|
2019 |
Ure D, Awada A, Frowley N, Munk N, Stanger A, Mutus B. Greenhouse tomato plant roots/carboxymethyl cellulose method for the efficient removal and recovery of inorganic phosphate from agricultural wastewater. Journal of Environmental Management. 233: 258-263. PMID 30580121 DOI: 10.1016/J.Jenvman.2018.12.053 |
0.564 |
|
2018 |
Caba C, Ali Khan H, Auld J, Ushioda R, Araki K, Nagata K, Mutus B. Conserved Residues Lysand Lysof Protein Disulfide Isomerase Maintain an Active Site Conformation for Optimal Activity: Implications for Post-Translational Regulation. Frontiers in Molecular Biosciences. 5: 18. PMID 29541639 DOI: 10.3389/Fmolb.2018.00018 |
0.372 |
|
2017 |
Sun BL, Palmer L, Alam SR, Adekoya I, Brown-Steinke K, Periasamy A, Mutus B. O-Aminobenzoyl-S-Nitrosoglutathione: a Fluorogenic, Cell Permeable, Pseudo-Substrate for S-Nitrosoglutathione Reductase. Free Radical Biology & Medicine. PMID 28419866 DOI: 10.1016/J.Freeradbiomed.2017.04.008 |
0.369 |
|
2015 |
Jarosz AP, Wei W, Gauld JW, Auld J, Özcan F, Aslan M, Mutus B. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is inactivated by S-sulfuration in vitro. Free Radical Biology & Medicine. 89: 512-521. PMID 26453916 DOI: 10.1016/J.Freeradbiomed.2015.09.007 |
0.365 |
|
2015 |
Liu H, Chen J, Li W, Rose ME, Shinde SN, Balasubramani M, Uechi GT, Mutus B, Graham SH, Hickey RW. Protein disulfide isomerase as a novel target for cyclopentenone prostaglandins: implications for hypoxic ischemic injury. The Febs Journal. 282: 2045-59. PMID 25754985 DOI: 10.1111/Febs.13259 |
0.319 |
|
2014 |
Ali Khan H, Mutus B. Protein disulfide isomerase a multifunctional protein with multiple physiological roles. Frontiers in Chemistry. 2: 70. PMID 25207270 DOI: 10.3389/Fchem.2014.00070 |
0.365 |
|
2013 |
Kallakunta VM, Slama-Schwok A, Mutus B. Protein disulfide isomerase may facilitate the efflux of nitrite derived S-nitrosothiols from red blood cells. Redox Biology. 1: 373-80. PMID 24024174 DOI: 10.1016/J.Redox.2013.07.002 |
0.749 |
|
2013 |
Madhuri Kallakunta V, Reid C, Ananvoranich S, Mutus B. Protein Disulfide Isomerase-Red Fluorescent Protein Construct as a Cell Surface Oxidative Stress Sensor Free Radical Biology and Medicine. 65: S55-S56. DOI: 10.1016/J.Freeradbiomed.2013.10.523 |
0.342 |
|
2012 |
Kaur H, Mutus B. Platelet function and thymosin β4. Biological Chemistry. 393: 595-8. PMID 22944663 DOI: 10.1515/Hsz-2012-0131 |
0.627 |
|
2012 |
Chaube R, Kallakunta VM, Espey MG, McLarty R, Faccenda A, Ananvoranich S, Mutus B. Endoplasmic reticulum stress-mediated inhibition of NSMase2 elevates plasma membrane cholesterol and attenuates NO production in endothelial cells. Biochimica Et Biophysica Acta. 1821: 313-23. PMID 22063270 DOI: 10.1016/J.Bbalip.2011.10.015 |
0.725 |
|
2012 |
Kaur H, Carriveau R, Mutus B. A Simple Parallel Plate Flow Chamber to Study Effects of Shear Stress on Endothelial Cells American Journal of Biomedical Sciences. 70-78. DOI: 10.5099/Aj120100070 |
0.615 |
|
2011 |
Kallakunta V, Schwok A, Mutus B. P52. Protein disulfide isomerase facilitates the efflux of NO-equivalents from RBC Nitric Oxide. 24: S35. DOI: 10.1016/J.Niox.2011.03.283 |
0.729 |
|
2010 |
Kaur H, Heeney R, Carriveau R, Sosne G, Mutus B. Whole blood, flow-chamber studies in real-time indicate a biphasic role for thymosin β-4 in platelet adhesion. Biochimica Et Biophysica Acta. 1800: 1256-61. PMID 20797426 DOI: 10.1016/J.Bbagen.2010.08.003 |
0.61 |
|
2010 |
Faccenda A, Bonham CA, Vacratsis PO, Zhang X, Mutus B. Gold nanoparticle enrichment method for identifying S-nitrosylation and S-glutathionylation sites in proteins. Journal of the American Chemical Society. 132: 11392-4. PMID 20677743 DOI: 10.1021/Ja103591V |
0.313 |
|
2010 |
Kallakunta VM, Staruch A, Mutus B. Sinapinic acid can replace ascorbate in the biotin switch assay. Biochimica Et Biophysica Acta. 1800: 23-30. PMID 19837133 DOI: 10.1016/J.Bbagen.2009.10.004 |
0.743 |
|
2010 |
Kallakunta VM, Hudson J, Schwok A, Mutus B. Protein Disulfide Isomerase-mediated Oxygen and Nitrite Dependent Efflux of NO-equivalents from Red Blood Cells Free Radical Biology and Medicine. 49: S115. DOI: 10.1016/J.Freeradbiomed.2010.10.310 |
0.741 |
|
2009 |
Mikula I, Durocher S, Martasek P, Mutus B, Slama-Schwok A. Isoform-specific differences in the nitrite reductase activity of nitric oxide synthases under hypoxia. The Biochemical Journal. 418: 673-82. PMID 19046140 DOI: 10.1042/Bj20080987 |
0.346 |
|
2007 |
Raturi A, Mutus B. Characterization of redox state and reductase activity of protein disulfide isomerase under different redox environments using a sensitive fluorescent assay. Free Radical Biology & Medicine. 43: 62-70. PMID 17561094 DOI: 10.1016/J.Freeradbiomed.2007.03.025 |
0.332 |
|
2007 |
Miersch S, Sliskovic I, Raturi A, Mutus B. Antioxidant and antiplatelet effects of rosuvastatin in a hamster model of prediabetes. Free Radical Biology & Medicine. 42: 270-9. PMID 17189832 DOI: 10.1016/J.Freeradbiomed.2006.10.045 |
0.309 |
|
2005 |
Miersch S, Mutus B. Protein S-nitrosation: biochemistry and characterization of protein thiol-NO interactions as cellular signals. Clinical Biochemistry. 38: 777-91. PMID 16005861 DOI: 10.1016/J.Clinbiochem.2005.05.014 |
0.367 |
|
2005 |
Raturi A, Vacratsis PO, Seslija D, Lee L, Mutus B. A direct, continuous, sensitive assay for protein disulphide-isomerase based on fluorescence self-quenching. The Biochemical Journal. 391: 351-7. PMID 15960611 DOI: 10.1042/Bj20050770 |
0.347 |
|
2005 |
Sliskovic I, Raturi A, Mutus B. Characterization of the S-denitrosation activity of protein disulfide isomerase. The Journal of Biological Chemistry. 280: 8733-41. PMID 15611098 DOI: 10.1074/Jbc.M408080200 |
0.392 |
|
2005 |
Al-Kassim L, Wang Z, Szabo AG, Taylor KE, Mutus B. Synthesis and characterization of a synthetic heme-based oxygen carrier Journal of Chemical Technology and Biotechnology. 80: 1026-1030. DOI: 10.1002/Jctb.1279 |
0.301 |
|
2004 |
Root P, Sliskovic I, Mutus B. Platelet cell-surface protein disulphide-isomerase mediated S-nitrosoglutathione consumption. The Biochemical Journal. 382: 575-80. PMID 15171728 DOI: 10.1042/Bj20040759 |
0.343 |
|
2004 |
Raturi A, Mutus B. Use of 2,3-diaminonapthalene for studying denitrosation activity of protein disulfide isomerase. Analytical Biochemistry. 326: 281-3. PMID 15003571 DOI: 10.1016/J.Ab.2003.12.015 |
0.322 |
|
2004 |
Raturi A, Mutus B. Erratum to “Use of 2,3-diaminonaphthalene for studying denitrosation activity of protein disulfide isomerase” [Anal. Biochem. 326 (2004) 281–283] Analytical Biochemistry. 328: 246. DOI: 10.1016/J.Ab.2004.03.003 |
0.329 |
|
2003 |
Akhter S, Green JR, Root P, Thatcher GJ, Mutus B. Peroxynitrite and NO+ donors form colored nitrite adducts with sinapinic acid: potential applications. Nitric Oxide : Biology and Chemistry / Official Journal of the Nitric Oxide Society. 8: 214-21. PMID 12895430 DOI: 10.1016/S1089-8603(03)00031-4 |
0.716 |
|
2002 |
Akhter S, Vignini A, Wen Z, English A, Wang PG, Mutus B. Evidence for S-nitrosothiol-dependent changes in fibrinogen that do not involve transnitrosation or thiolation. Proceedings of the National Academy of Sciences of the United States of America. 99: 9172-7. PMID 12089331 DOI: 10.1073/Pnas.142136499 |
0.727 |
|
2001 |
Ramachandran N, Root P, Jiang XM, Hogg PJ, Mutus B. Mechanism of transfer of NO from extracellular S-nitrosothiols into the cytosol by cell-surface protein disulfide isomerase. Proceedings of the National Academy of Sciences of the United States of America. 98: 9539-44. PMID 11493694 DOI: 10.1073/Pnas.171180998 |
0.362 |
|
2001 |
Mutus B. The S-nitroso derivative of omapatrilat (Vanlev) can act as a substrate for cell surface protein disulfide isomerase and thus deliver NO to the cytosol of human umbilical endothelial cells,in vitro American Journal of Hypertension. 14: A99. DOI: 10.1016/S0895-7061(01)01401-7 |
0.349 |
|
1999 |
Mutus B, Redmond RW, Akhter S. Evidence for peroxynitrite formation during S-nitrosoglutathione photolysis in air saturated solutions. Febs Letters. 449: 79-82. PMID 10225433 DOI: 10.1016/S0014-5793(99)00311-7 |
0.701 |
|
1999 |
Ramachandran N, Jacob S, Zielinski B, Curatola G, Mazzanti L, Mutus B. N-dansyl-S-nitrosohomocysteine a fluorescent probe for intracellular thiols and S-nitrosothiols. Biochimica Et Biophysica Acta. 1430: 149-54. PMID 10082943 DOI: 10.1016/S0167-4838(98)00286-6 |
0.305 |
|
1997 |
Tannous M, Labbe N, Redmond RW, Mutus B. A photo-activated, protein-based, NO/H2O2 generating system with tumoricidal activity composed of the nitric oxide derivative of apo-metallothionein (thionein-NO) and glucose oxidase. Journal of Photochemistry and Photobiology. B, Biology. 41: 249-54. PMID 9447722 DOI: 10.1016/S1011-1344(97)00115-2 |
0.327 |
|
1997 |
Francescutti D, Baldwin J, Lee L, Mutus B. Peroxynitrite modification of glutathione reductase: modeling studies and kinetic evidence suggest the modification of tyrosines at the glutathione disulfide binding site. Protein Engineering. 9: 189-94. PMID 9005440 DOI: 10.1093/Protein/9.2.189 |
0.342 |
|
1996 |
Wood PD, Mutus B, Redmond RW. The Mechanism of Photochemical Release of Nitric Oxide from S-Nitrosoglutathione Photochemistry and Photobiology. 64: 518-524. DOI: 10.1111/J.1751-1097.1996.Tb03099.X |
0.319 |
|
1995 |
Baldwin JS, Lee L, Leung TK, Muruganandam A, Mutus B. Identification of the site of non-enzymatic glycation of glutathione peroxidase: rationalization of the glycation-related catalytic alterations on the basis of three-dimensional protein structure. Biochimica Et Biophysica Acta. 1247: 60-4. PMID 7873592 DOI: 10.1016/0167-4838(94)00202-R |
0.33 |
|
1995 |
Sexton DJ, Mutus B. Platelet glutathione transport: characteristics and evidence for regulation by intraplatelet thiol status Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 73: 155-162. PMID 7576489 DOI: 10.1139/O95-019 |
0.304 |
|
1994 |
Sexton DJ, Muruganandam A, McKenney DJ, Mutus B. Visible light photochemical release of nitric oxide from S-nitrosoglutathione: potential photochemotherapeutic applications. Photochemistry and Photobiology. 59: 463-7. PMID 8022889 DOI: 10.1111/J.1751-1097.1994.Tb05065.X |
0.309 |
|
1994 |
Muruganandam A, Mutus B. Isolation of nitric oxide synthase from human platelets. Biochimica Et Biophysica Acta. 1200: 1-6. PMID 7514442 DOI: 10.1016/0304-4165(94)90019-1 |
0.305 |
|
1992 |
Muruganandam A, Drouillard C, Thibert RJ, Cheung RM, Draisey TF, Mutus B. Glutathione metabolic enzyme activities in diabetic platelets as a function of glycemic control. Thrombosis Research. 67: 385-97. PMID 1357772 DOI: 10.1016/0049-3848(92)90268-F |
0.309 |
|
1991 |
Grewal J, Mutus B. Modification of sialic acid-MBTH assay for quantitative determination of nonenzymatically glucosylated proteins Microchemical Journal. 44: 276-281. DOI: 10.1016/0026-265X(91)90049-U |
0.357 |
|
1990 |
Palmer EJ, MacManus JP, Mutus B. Inhibition of glutathione reductase by oncomodulin. Archives of Biochemistry and Biophysics. 277: 149-54. PMID 2306116 DOI: 10.1016/0003-9861(90)90563-E |
0.352 |
|
1988 |
Mutus B, Palmer EJ, MacManus JP. Disulfide-linked dimer of oncomodulin: comparison to calmodulin. Biochemistry. 27: 5615-22. PMID 3179268 DOI: 10.1021/Bi00415A033 |
0.324 |
|
1987 |
Mutus B, Palmer EJ, MacManus JP. Disulphide-Linked Dimer of Oncomodulin: Structural and Functional Properties Calcium-Binding Proteins in Health and Disease. 567-569. DOI: 10.1016/B978-0-12-521040-9.50100-5 |
0.327 |
|
1985 |
Suryanarayana K, Thomas DD, Mutus B. Calmodulin from the water mold Achlya ambisexualis: isolation and characterization. Cell Biology International Reports. 9: 389-400. PMID 3995600 DOI: 10.1016/0309-1651(85)90034-7 |
0.33 |
|
1983 |
Mutus B, Duncan DV, Tomlinson G. Modification of acetylcholinesterase with the fluorescent thiol reagent S-mercuric-N-dansylcysteine. Biochemical and Biophysical Research Communications. 112: 941-7. PMID 6847689 DOI: 10.1016/0006-291X(83)91708-4 |
0.441 |
|
1982 |
Tomlinson G, Mutus B, McLennan I. Activation and inactivation of acetylcholinesterase by metal ions. Canadian Journal of Biochemistry. 59: 728-35. PMID 7317819 DOI: 10.1139/O81-101 |
0.471 |
|
1982 |
Mutus B, Tomlinson G, Duncan DV. Modification of acetylcholinesterase with N-dansylaziridine. Biochemical and Biophysical Research Communications. 102: 1136-43. PMID 7317044 DOI: 10.1016/S0006-291X(81)80130-1 |
0.4 |
|
1982 |
Tomlinson G, Mutus B, McLennan I, Mooibroek MJ. Activation and inactivation of purified acetylcholinesterase from Electrophorus electricus by lanthanum (III). Biochimica Et Biophysica Acta. 703: 142-8. PMID 7082678 DOI: 10.1016/0167-4838(82)90042-5 |
0.474 |
|
1980 |
Widmer F, Gross E, Mutus B, Snieckus VA, Viswanatha T. Purification and some properties of tryptophan-5-monooxygenase from rabbit hindbrain Journal of Solid-Phase Biochemistry. 5: 97-114. DOI: 10.1007/Bf02995867 |
0.536 |
|
1979 |
Tomlinson G, Mutus B, Rutherford WJ. Equilibrium and kinetic studies of the interaction of site-specific ligands with acetylcholinesterase from Electrophorus electricus. Canadian Journal of Biochemistry. 56: 1133-40. PMID 750073 DOI: 10.1139/O78-178 |
0.474 |
|
1975 |
Widmer F, Mutus B, RamaMurthy J, Snieckus VA, Viswanatha T. Partial purification of rabbit hind brain tryptophan hydroxylase by affinity chromatography Life Sciences. 17: 1297-1302. PMID 1196011 DOI: 10.1016/0024-3205(75)90141-1 |
0.528 |
|
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