Articles Related to ADP
Correlation of Hemostatic Parameters with Poly (ADP-ribose) Polymerase-1 (PARP-1) Polymorphisms, Mutations, Laboratory, and Clinical Characteristics in 114 Patients with Philadelphia-Negative Myeloproliferative Neoplasms
Patients with Philadelphia-negative myeloproliferative neoplasms (PN-MPN) are at a higher risk for venous thrombosis. Thromboelastometry may prove efficient to evaluate the patient’s thrombotic risk. In this study, based on data from 114 patients with PN-MPN from a single center in Greece, hemostatic profile was assessed with routine coagulation tests, Rotational Thromboelastometry (ROTEM® ), and Platelet Function Analyzer (PFA)-100 and correlated with clinical, laboratory, treatment characteristics, gene mutations and polymorphisms of poly (ADP-ribose) polymerase-1 (PARP-1)
PLIN2 belongs to one member of PAT (Perilipin, Adipophilin and Tip47) family, which plays an important role in regulating lipid storage and could be regarded as a candidate gene for intramuscular fat deposition in pigs. This study tried to clone the coding domain sequence (CDS) of PLIN2 gene, compare the nucleotide acids and deduced amino acids sequence, physiological characteristics, structure and the expression level between Wujin (fatty breed) and Landrace (lean breed) pigs. The results showed that the mutation of nucleotide acids led to the mutation of deduced amino acids between two pig breeds.
Peritoneal Dialysis (PD) is one of the 3 well-established modalities of renal replacement therapy used in patients with renal failure. Despite its significant role as a successful method of renal replacement therapy, PD is highly associated with peritonitis and catheter-related infections.
Mutation in a single nucleotide of a gene has the potential to change the structure and/or function of its protein. Albeit simply saying, it is not observed to be a general phenomenon. The effect of mutation is primarily determined by the stereochemical nature of the amino acid which has replaced the previous amino acid, resulting in the residue location being affected. Here we show that despite a change in the frequency of occurrence of a particular amino acid in a particular protein in different types of organisms, the overall function of the protein can still remain unaffected, even when the resultant protein conformation is relatively altered.