(Q74228443)

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Purine nucleoside phosphorylase from Cellulomonas sp.: physicochemical properties and binding of substrates determined by ligand-dependent enhancement of enzyme intrinsic fluorescence, and by protective effects of ligands on thermal inactivation of

scientific article published on 01 June 2002

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9 November 2019

Purine nucleoside phosphorylase from Cellulomonas sp.: physicochemical properties and binding of substrates determined by ligand-dependent enhancement of enzyme intrinsic fluorescence, and by protective effects of ligands on thermal inactivation of the enzyme (English)

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9 November 2019

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Agnieszka Bzowska

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9 November 2019

Beata Wielgus-Kutrowska

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Beata Wielgus-Kutrowska

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9 November 2019

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Jan Tebbe

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9 November 2019

Gertraud Koellner

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9 November 2019

David Shugar

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9 November 2019

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1 June 2002

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9 November 2019

Biochimica et Biophysica Acta

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9 November 2019

1597

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9 November 2019

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9 November 2019

320-334

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9 November 2019

Purine nucleoside phosphorylases: properties, functions, and clinical aspects

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Synthesis of 1,1-difluoro-5-(1H-9-purinyl)-2-pentenylphosphonic acids and the related methano analogues. Remarkable effect of the nucleobases and the cyclopropane rings on inhibitory activity toward purine nucleoside phosphorylase

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Synthesis and biological evaluation of 1,1-difluoro-2-(tetrahydro-3-furanyl)ethylphosphonic acids possessing a N9-purinylmethyl functional group at the ring. a new class of inhibitors for purine nucleoside phosphorylases

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Crystal structure of the purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implication for the mechanism of trimeric PNPs

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Crystallization and preliminary X-ray studies of purine nucleoside phosphorylase from Cellulomonas sp

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72 Purine nucleoside phosphorylase from human erythrocytes

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Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol

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Calf spleen purine nucleoside phosphorylase: purification, sequence and crystal structure of its complex with an N(7)‐acycloguanosine inhibitor

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Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism

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31P nuclear magnetic resonance spectra of the thiophosphate analogs of adenine nucleotides; effects of pH and Mg2+ binding

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Purine nucleoside phosphorylase: its use in a spectroscopic assay for inorganic phosphate and for removing inorganic phosphate with the aid of phosphodeoxyribomutase

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Bovine brain purine-nucleoside phosphorylase purification, characterization, and catalytic mechanism

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Purification and properties of inosine-guanosine phosphorylase from Escherichia coli K-12.

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Purine nucleoside phosphorylase. Inosine hydrolysis, tight binding of the hypoxanthine intermediate, and third-the-sites reactivity

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10.1016/S0167-4838(02)00313-8

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12044910%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12044910%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

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