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Human Polyclonal NP Primary Antibody for IHC, IHC (p) - ABIN4348699
Kojima, Chiyomaru, Kawakami, Yoshino, Enokida, Nohata, Fuse, Ichikawa, Naya, Nakagawa, Seki: Tumour suppressors miR-1 and miR-133a target the oncogenic function of purine nucleoside phosphorylase (PNP) in prostate cancer. in British journal of cancer 2012
The study suggests that mass-constrained femtosecond motions at the catalytic site of PNP can improve transition state barrier crossing by more frequent sampling of essential catalytic site contacts.
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.
Data show that the mutations in purine nucleoside phosphorylase (PNP) alters the enthalpy-entropy balance with little effect on the catalytic rates.
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.
the binding mechanism of a transition state analogue (DADMe-immucillin-H) to the purine nucleoside phosphorylase (PNP) enzyme, is reported.
Data show that [15N, 2H]His8-purine nucleoside phosphorylase (PNP) had reduced catalytic site chemistry larger than proportional to the enzymatic mass difference.
Study of genetic heterogeneity in systemic lupus erythematosus, the top associations in European ancestry were protein kinase, cyclic GMP-dependent, type I (PRKG1) rs7897633 (P(Meta) = 2.75 x 10(-8)) and purine nucleoside phosphorylase (PNP) rs1049564 (P(Meta) = 1.24 x 10(-7)).
Human small intestine is a key site for ribavirin phosphorolysis and that PNP is primarily involved in the metabolism.
insufficient data to evaluated impact of genetic polymorphisms on disease susceptibility
Complete lack of PNP triggers accumulation of deoxyguanosine, thereby disrupting B-cell development, the consequence of which is more profound with time, as was found in the older sister.
Biochemical and genetic data on a cohort of seven patients from six families identified as PNPase deficient, is reported.
This study for the first time describes elevated levels of alpha synuclein in pancreatic adenocarcinoma as well as highlights the potential of evaluating NP protein expression.
investigation of catalytic mechanisms involved in catalysis by PNP: transition states in arsenolysis and phosphorolysis
Results show that some regions, responsible for entrance and exit of substrate, present a conformational variability, which is dissected by dynamics simulation analysis.
PNP operating at maximum catalytic potential permits more rapid peptide amide deuterium exchange and greater conformational flexibility of water-peptide bond exchange rate than in either of the complexes with transition state analogues.
The optimum pH for PNP from human erythrocytes with xanthosine and xanthine is in the range 5-6, whereas those with guanosine, guanine, inosine & hypoxanthine are in the range 7-8. Possible PNP binding modes of Xan and Xao by mammalian PNPs are proposed.
Crystal structure of human purine nucleoside phosphorylase.
These data provide a framework in which to conduct genetic association studies of these two genes in relevant populations, thereby allowing hNP and hGSTO1-1 to be evaluated as potential susceptibility genes in human arsenicism.
investigation of the quaternary structure of recombinant human purine nucleoside phosphorylase
crystal structures in complex with inosine and 2',3'-dideoxyinosine, refined to 2.8A resolution using synchrotron radiation. The structures provide explanation for ligand binding, refine the purine-binding site and can be used for future inhibitor design.
the biological role of packing of the PNP monomers into a trimeric structure
The high-affinity binding of transition-state analogues to NP is not the result of single interactions, but results from a constellation of cooperative hydrogen bond interactions, all of which are required to form the tightly bound complex.
crystal structure complexed with analogs of the inhibitor 2-diaminopurine aglycone (purine nucleoside phosphorylase)
crystal structure was refined to a resolution of 2.2 A
PNP purine nucleoside phosphorylase was crystallized in space group P2(1)2(1)2(1) in the presence of (S)-PMPDAP and phosphate, and the resulting structure of the binary PNP/(S)-PMPDAP complex was refined at 2.05A resolution.
involvement of the neutral purine molecule, and not its monoanion, as the substrate in the reverse, synthetic reaction
alf spleen enzyme is a homotrimer and previous suggestions for dissociation of this enzyme into more active monomers, upon dilution of the enzyme or addition of phosphate, are incorrect.
This result questions the involvement of the anionic forms in the reaction catalyzed by trimeric PNPs, and contradicts the hypothesis of a strong hydrogen bond formation between the enzyme Asn 243 residue and the purine N7 position.
PCR amplification of the calf phosphorylase from the calf spleen library, cloning, overexpression of the recombinant PNP, its enzymatic activity and interactions with typical ligands of mammalian wild type PNP are described.
The transition-state structure of triple mutant PNP is altered as a consequence of the amino acids in the second sphere from the catalytic site.
Loss of PNP expression is associated with hearing loss.
PNP deficiency causes cerebellar abnormalities, including Purkinje cell damage and progressive motor deficits.
PNP is important for the survival of DP thymocytes. Accumulation of dGuo in cases of PNP deficiency leads to mitochondria-initiated apoptosis of DP thymocytes, which can be prevented by restoring PNP activity in the cells.
This gene encodes an enzyme which reversibly catalyzes the phosphorolysis of purine nucleosides. The enzyme is trimeric, containing three identical subunits. Mutations which result in nucleoside phosphorylase deficiency result in defective T-cell (cell-mediated) immunity but can also affect B-cell immunity and antibody responses. Neurologic disorders may also be apparent in patients with immune defects. A known polymorphism at aa position 51 that does not affect enzyme activity has been described. A pseudogene has been identified on chromosome 2.
, inosine-guanosine phosphorylase
, purine-nucleoside:orthophosphate ribosyltransferase
, nucleoside phosphorylase
, purine nucleoside phosphorylase
, purine-nucleoside phosphorylase 1