PNP cDNA ORF clone, Homo sapiens(human)

Lupus-Associated Functional Polymorphism in PNP Causes Cell Cycle Abnormalities and Interferon Pathway Activation in Human Immune Cells.
Ghodke-Puranik Y, Dorschner JM, Vsetecka DM, Amin S, Makol A, Ernste F, Osborn T, Moder K, Chowdhary V, Eliopoulos E, Zervou MI, Goulielmos GN, Jensen MA, Niewold TB
Arthritis & rheumatology (Hoboken, N.J.)69(12)2328-2337(2017 12)

Thermodynamics of the Purine Nucleoside Phosphorylase Reaction Revealed by Computer Simulations.
Isaksen GV, ?qvist J, Brandsdal BO
Biochemistry56(1)306-312(2017 Jan)

Computer Simulations Reveal Substrate Specificity of Glycosidic Bond Cleavage in Native and Mutant Human Purine Nucleoside Phosphorylase.
Isaksen GV, Hopmann KH, ?qvist J, Brandsdal BO
Biochemistry55(14)2153-62(2016 Apr)

Isotope-specific and amino acid-specific heavy atom substitutions alter barrier crossing in human purine nucleoside phosphorylase.
Suarez J, Schramm VL
Proceedings of the National Academy of Sciences of the United States of America112(36)11247-51(2015 Sep)

The PNP rs1049564 T allele is a loss-of-function variant that induces S-phase block and IFN pathway activation in lymphocytes. The S-phase block could be rescued in our in vitro experiments, suggesting the potential for personalized treatment.
Title: Lupus-Associated Functional Polymorphism in PNP Causes Cell Cycle Abnormalities and Interferon Pathway Activation in Human Immune Cells.

Data show that the mutations in purine nucleoside phosphorylase (PNP) alters the enthalpy-entropy balance with little effect on the catalytic rates.
Title: Thermodynamics of the Purine Nucleoside Phosphorylase Reaction Revealed by Computer Simulations.

Data (including data from empirical valence bond/molecular dynamic simulations) suggest that PNP substrate specificity for inosine and guanosine is a direct result of electrostatic preorganization energy along the reaction coordinate.
Title: Computer Simulations Reveal Substrate Specificity of Glycosidic Bond Cleavage in Native and Mutant Human Purine Nucleoside Phosphorylase.

Data show that [15N, 2H]His8-purine nucleoside phosphorylase (PNP) had reduced catalytic site chemistry larger than proportional to the enzymatic mass difference.
Title: Isotope-specific and amino acid-specific heavy atom substitutions alter barrier crossing in human purine nucleoside phosphorylase.

the binding mechanism of a transition state analogue (DADMe-immucillin-H) to the purine nucleoside phosphorylase (PNP) enzyme, is reported.
Title: The ligand binding mechanism to purine nucleoside phosphorylase elucidated via molecular dynamics and machine learning.