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Charles P. Scholes
Researcher at University at Albany, SUNY
Publications - 76
Citations - 2833
Charles P. Scholes is an academic researcher from University at Albany, SUNY. The author has contributed to research in topics: Electron paramagnetic resonance & Electron nuclear double resonance. The author has an hindex of 31, co-authored 76 publications receiving 2692 citations. Previous affiliations of Charles P. Scholes include State University of New York System & University of Illinois at Urbana–Champaign.
Papers
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Journal ArticleDOI
Porphyrin–phospholipid liposomes permeabilized by near-infrared light
Kevin A. Carter,Shuai Shao,Matthew I. Hoopes,Dandan Luo,Bilal Ahsan,Vladimir M. Grigoryants,Wentao Song,Haoyuan Huang,Guojian Zhang,Ravindra K. Pandey,Jumin Geng,Blaine A. Pfeifer,Charles P. Scholes,Joaquin Ortega,Mikko Karttunen,Jonathan F. Lovell +15 more
TL;DR: Liposomes doped with porphyrin–phospholipid that are permeabilized directly by near-infrared light are described and spatial and temporal control of release of entrapped fluorophores following intratumoral injection are demonstrated.
Journal ArticleDOI
Endonuclease III is an iron-sulfur protein.
Richard P. Cunningham,Hitomi Asahara,Janet F. Bank,Charles P. Scholes,John C. Salerno,Kristene K. Surerus,E Münck,John McCracken,Jack Peisach,Mark Emptage +9 more
TL;DR: Elemental analyses, Mössbauer, and EPR data show that endonuclease III of Escherichia coli is unique in being both a DNA repair enzyme and an iron-sulfur protein.
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Coordination Compounds of Polyoxovanadates with a Hexametalate Core. Chemical and Structural Characterization of [VV6O13{(OCH2)3CR}2]2−, [VV6O11(OH)2{(OCH2)3CR}2], [VIV4VV2O9(OH)4{(OCH2)3CR}2]2−, and [VIV6O7(OH)6{(OCH2)3CR}2]2−
TL;DR: In this article, the tris(hydroxymethylmethane)-derived ligands, (HOCH 2 ) 3 Cr, R=NO 2, CH 2 OH, and CH 3, with [(C 4 H 9 ) 4 N] 3 [H 3 V 10 O 28 ] in CH 3 CN yield the polyoxovanadate coordination complexes.
Journal ArticleDOI
Electron nuclear double resonance (ENDOR) from heme and histidine nitrogens in single crystals of aquometmyoglobin
Charles P. Scholes,Aviva Lapidot,Rita Mascarenhas,Toshiro Inubushi,R.A. Isaacson,George Feher +5 more
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Spectroscopic, kinetic, and electrochemical characterization of heterologously expressed wild-type and mutant forms of copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3.
Kenneth Olesen,Andrei Veselov,Yiwei Zhao,Yousheng Wang,Birgit Danner,Charles P. Scholes,James P. Shapleigh +6 more
TL;DR: A high-yield heterologous expression system for the copper-containing nitrite reductase from a denitrifying variant of Rhodobacter sphaeroides is reported, with blue color and midpoint potential of M182T and the mutation H287E which resulted in a 100-fold loss of enzyme activity and a Type 2 EPR spectrum which were no longer sensitive to the presence of nitrite.