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hexapeptide/ساركومة

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مقالاتالتجارب السريريةبراءات الاختراع
12 النتائج

Effect of HGF-like basic hexapeptides on angiogenesis.

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The interaction of glycosaminoglycans (GAG) with peptides relies on noncovalent binding to basic amino acid sequences, for which a minimal requirement is a pentapeptide region in the protein and the sulfated and carboxyl region in the GAG. Since such sequences are present in the heparin-binding

[A novel immunoregulating hexapeptide with antineoplastic effect].

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A synthesized analog of myelopeptide HP-2-->M[symbol: see text]-2 (Leu-Val-Val-Tyr-Pro-Trp) caused a significant (60-80%) and prolonged inhibition of s.c. grafted tumors P388, Ca-755, B-16 and sarcoma 180 in isogenic mice but did not affect the growth of tumor B-16 in nude mice. Nor did it influence

Some properties of cathepsins chemically fixed to carriers.

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An insoluble preparation of rat liver cathepsin D was obtained by coupling the enzyme to Enzacryl Polyacetal (EPA-cathepsin) and to CNBr-activated Sepharose 4B. EPA-cathepsin was active toward the synthetic hexapeptides (Gly-Phe-Leu)2 and did not split hemoglobin. The optimum pH of splitting was

Communication between the active sites and dimer interface of a herpesvirus protease revealed by a transition-state inhibitor.

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Structurally diverse organophosphonate inhibitors targeting the active site of the enzyme were used to investigate the relationship of the active site and the dimer interface of wild-type protease in solution. Positional scanning synthetic combinatorial libraries revealed Kaposi's sarcoma-associated

Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts.

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The genome of avian sarcoma virus CT10 encodes a fusion protein in which viral Gag sequences are fused to cellular Crk sequences containing primarily Src homology 2 (SH2) and Src homology 3 (SH3) domains. Transformation of chicken embryo fibroblasts (CEF) with the Gag-Crk fusion protein results in

A repetitive element containing a critical tyrosine residue is required for transcriptional activation by the EWS/ATF1 oncogene.

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Chromosomal fusion of the N-terminal region of the Ewings Sarcoma Oncogene (EWS-activation-domain, EAD) to the DNA-binding domains of a variety of cellular transcription factors produce oncogenic proteins (EWS-fusion proteins (EFPs)) that cause distinct malignancies. In EFPs, the EAD acts as a

[Cathepsins D from normal and some human neoplasms].

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Cathepsins D were isolated from human liver and spleen, from three malignant tumours (kidney cancer, sarcoma, spleen tumour caused by chronic myeloleucosis) and from one non-malignant tumour (uterine myoma). The isolation procedure involved adsorption on pepstatin-Sepharose and gel-filtration on

Substrate modulation of enzyme activity in the herpesvirus protease family.

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The herpesvirus proteases are an example in which allosteric regulation of an enzyme activity is achieved through the formation of quaternary structure. Here, we report a 1.7 A resolution structure of Kaposi's sarcoma-associated herpesvirus protease in complex with a hexapeptide transition state

Isolation of proteins with kinase activity and related to pp60 src from human cells.

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A protein kinase activity (PK) was associated with immunoprecipitates between polypeptides of human lymphoblastoid cells of malignant origin (Raji cell line) or of their normal counterparts ( Priess cell line) and antibodies directed against avian pp60 src or against the carboxyterminal hexapeptide

Biological and biochemical properties of the c-src+ gene product overexpressed in chicken embryo fibroblasts.

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The c-src protein isolated from neuronal cells (pp60c-src+) displays a higher level of protein kinase activity than does pp60c-src from nonneural tissues. There are two structural alterations present in the amino-terminal half of pp60c-src+ expressed in neurons which could contribute to the enhanced

Multiple aromatic side chains within a disordered structure are critical for transcription and transforming activity of EWS family oncoproteins.

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Chromosomal translocations involving the N-terminal approximately 250 residues of the Ewings sarcoma (EWS) oncogene produce a group of EWS fusion proteins (EFPs) that cause several distinct human cancers. EFPs are potent transcriptional activators and interact with other proteins required for mRNA

The proto-oncoprotein SYT interacts with SYT-interacting protein/co-activator activator (SIP/CoAA), a human nuclear receptor co-activator with similarity to EWS and TLS/FUS family of proteins.

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The proto-oncoprotein SYT is involved in the unique translocation t(X;18) found in synovial sarcoma SYT-SSX fusions. SYT has a conserved N-terminal domain (SNH domain) that interacts with the human paralog of Drosophila Brahma (hBRM) and Brahma-related gene 1 (BRG1) chromatin remodeling proteins and
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