R
Richard H. Furneaux
Researcher at Victoria University of Wellington
Publications - 238
Citations - 8288
Richard H. Furneaux is an academic researcher from Victoria University of Wellington. The author has contributed to research in topics: Purine nucleoside phosphorylase & Transition state analog. The author has an hindex of 52, co-authored 233 publications receiving 7951 citations. Previous affiliations of Richard H. Furneaux include Albert Einstein College of Medicine & University of Montana.
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Chemical methods for the analysis of sulphated galactans from red algae
TL;DR: Improved analytical methods have been applied successfully to kappa-, iota-, and lambda-carrageenans, as well as some agars, enabling the rapid determination of the substitution pattern of these polysaccharides.
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Production of levoglucosan and glucose from pyrolysis of cellulosic materials
TL;DR: In this paper, it was found that pyrolysis proceeds at a much faster rate at the higher temperatures without detrimental effect on the yields, yielding a tar that contained 39% levoglucosan and, upon mild acid hydrolysis, gave 49% Dglucose.
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One-Third-the-Sites Transition-State Inhibitors for Purine Nucleoside Phosphorylase†
TL;DR: Interaction of transition-state inhibitors with purine nucleoside phosphorylase is different from reactant-state (substrate and product analogue) inhibitors of the enzyme which bind equally to all subunits of the homotrimer.
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Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis
Alexander A. Fedorov,Wuxian Shi,Gregory A. Kicska,Elena V. Fedorov,Peter C. Tyler,Richard H. Furneaux,J C Hanson,Graeme J. Gainsford,John Z. Larese,Vern L. Schramm,Steven C. Almo +10 more
TL;DR: Immucillin-H is a 23 pM inhibitor of bovine purine nucleoside phosphorylase (PNP) specifically designed as a transition state mimic and its structures are compared to previously reported complexes of PNP with substrate and product analogues in the catalytic sites and with the experimentally determined transition state structure.
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Immucillin H, a powerful transition-state analog inhibitor of purine nucleoside phosphorylase, selectively inhibits human T lymphocytes.
Greg A. Kicska,Li Long,Heidi Hörig,Craig Fairchild,Peter C. Tyler,Richard H. Furneaux,Vern L. Schramm,Howard L. Kaufman +7 more
TL;DR: The design of Imm-H from an enzymatic transition-state analysis exemplifies a powerful approach for developing high-affinity enzyme inhibitors with pharmacologic activity and may have clinical potential for treatment of human T cell leukemia and lymphoma and for other diseases characterized by abnormal activation of T lymphocytes.