نتایج جستجو برای: cysteine peptidase

تعداد نتایج: 43679  

Journal: :The Journal of biological chemistry 1984
M Tokunaga J M Loranger H C Wu

Prolipoprotein signal peptidase, a unique endopeptidase which recognizes glycyl glyceride cysteine as a cleavage site, was characterized in an in vitro assay system using purified prolipoprotein as the substrate. This enzyme did not require phospholipids for its catalytic activity and was found to be localized in the inner cytoplasmic membrane of the Escherichia coli cell envelope. Globomycin i...

Journal: :Biocell 2022

Head and neck squamous cell carcinoma is the sixth most common tumor worldwide, half of head patients are with oral (OSCC). 300,000 new cases OSCC were reported annually. Even multi-modality treatment, prognosis remains unsatisfactory. Thus, it urgent to discover novel therapeutic targets for OSCC. Some microarray studies have revealed that Keratin 4 (KRT4) downregulated in OSCC, whereas its ro...

Journal: :Atlas of Genetics and Cytogenetics in Oncology and Haematology 2011

Journal: :Applied and environmental microbiology 1993
S Sahlstrøm J Chrzanowska T Sørhaug

A peptidase from the cell wall fraction of Lactococcus lactis subsp. cremoris IMN-C12 has been purified to homogeneity by hydrophobic interaction chromatography, two steps of anion-exchange chromatography, and gel filtration. The molecular mass of the purified enzyme was estimated to be 72 kDa by gel filtration and 23 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme ...

Journal: :The Journal of general virology 1997
T Suzuki T Kanaya H Okazaki K Ogawa A Usami H Watanabe K Kadono-Okuda M Yamakawa H Sato H Mori S Takahashi K Oda

Infection by a baculovirus (Bombyx mori nuclear polyhedrosis virus, BmNPV) in silkworm (Bombyx mori) larvae is highly efficient as an expression system for the production of useful proteins. However, the amount of the protein of interest expressed tends to decrease in the later stages of infection presumably due, in part, to a proteinase produced in the larval haemolymph. The N-terminal amino a...

Journal: :Journal of bacteriology 1994
K D Everett D M Desiderio T P Hatch

The primary sequence of the small cysteine-rich protein (EnvA) of Chlamydia psittaci 6BC has been shown to possess a potential lipid modification/signal peptidase II-processing site, and the mature protein was labeled by a [3H]palmitic acid precursor. We further characterized the mature EnvA, showing that it lacks the N-terminal methionine of the primary peptide, is hydrophobic despite a peptid...

Journal: :Biochemical Society transactions 1990
F Ashall N Healy S Greig A Kiderlen A Curry J Blackwell

We have previously characterized a peptidase in Tiypanosomu crirzi that cleaves peptide substrates on the carboxyl side of arginine and lysinc residues at alkaline pH [ I ] . This alkaline peptidase occurs in all stages of the life cycle of T. criizi, and evidence was presented that a similar or identical enzyme was expressed by 15 other species of trypanosomatid, but not by any non-trypanosoma...

2011
Sabrina Di Bartolomeo Francesco Cecconi

Three mRNA isoforms have been identified in Homo sapiens. Caspase-9S, also classified as caspase-9b or caspase9beta, is a small variant of caspase-9 lacking exons 3-6, which contain the catalytic domain. Caspase-9S functions as an endogenous dominant-negative isoform of full-length caspase-9 by binding to the Apaf-1 protein thus hampering its binding and processing of the full-length procaspase...

Journal: :European journal of biochemistry 2000
J Dobers S Grams W Reutter H Fan

The multifunctional type II transmembrane glycoprotein, dipeptidyl peptidase IV (DPPIV, EC 3.4.14.5), is expressed by almost all mammalian cells and is identical to the adenosine deaminase binding protein CD26 on lymphocytes. The extracellular part of rat DPPIV can be divided into three domains the middle part of which harbors 10 of the 12 highly conserved cysteine residues. The cysteine-rich d...

2014
Selcen Öztürk Kolja Schleich Inna N Lavrik

Review on CASP8, with data on DNA/RNA, on the protein encoded and where the gene is implicated.

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