OPMSP: A Computational Method Integrating Protein Interaction and Sequence Information for the Identification of Novel Putative Oncogenes.

Oncogenes are genes that have the potential to cause cancer. Oncogene research can provide insight into the occurrence and development of cancer, thereby helping to prevent cancer and to design effective treatments. This study proposes a network method called the oncogene prediction method based on shortest path algorithm (OPMSP) for the identification of novel oncogenes in a large protein network built using protein-protein interaction data.

Functional analysis of the distal region of the third intracellular loop of PROKR2.

Mutations in the G-protein-coupled receptor PROKR2 have been identified in patients with idiopathic hypogonadotropic hypogonadism (IHH) and Kallmann syndrome (KS) manifesting with delayed puberty and infertility. Recently, the homozygous mutation V274D was identified in a man displaying KS with an apparent reversal of hypogonadism. The affected amino acid, valine 274, is located at the junction region of the third intracellular loop (IL3) and the sixth transmembrane domain (TM6).

Expression and characterization of a variant of TACI (CRD2-shortTACIFc) in Pichia pastoris.

TACI is a member of the tumor necrosis factor receptor superfamily and serves as a key regulator of B cell function. The extracellular domain of a typical TNFR contains multiple copies of CRD, which bind in the monomermonomer interfaces of a trimeric ligand. TACI binds to two ligands, APRIL and BAFF, with high affinity and contains two CRD in its extracellular regions, while BCMA and BR3, contain a single or partial CRD for binding the two ligands.

Protein sumoylation sites prediction based on two-stage feature selection.

Protein sumoylation is one of the most important post-translational modifications. Accurate prediction of sumoylation sites is very useful for the analysis of proteome. Though the putative motif Psi K XE can be used, optimization of prediction models still remains a challenge.

[A method for delineation of domains in proteins based on refolding free energy--application to continuous and discontinuous domains].

Domain is a protein architecture in a subunit. It might be defined as a basic unit for structure, function, folding, evolution and design. Different combinations of domains lead to the formation of various tertiary structures with various functions for proteins.

Delineation of Continuous Domains in Proteins by Differences of Free Energy.

Domain is a protein architecture under proteins' tertiary structure,which can be identified in most of proteins. Different combinations of domains lead to the formation of diverse tertiary structures with diverse function for proteins. The delineation of domains for a protein is important not only conceptually but also practically.