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provides coniferyl ferulate(CAS#:7464-93-9) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Emerging evidence suggests that an amplifiable protease cascade consisting of multiple aspartate specific cysteine proteases (ASCPs) is responsible for the apoptotic changes observed in mammalian cells undergoing programmed cell death. Here we describe the cloning of two novel ASCPs from human Jurkat T-lymphocytes. Like other ASCPs, the new proteases, named Mch4 and Mch5, are derived from single chain proenzymes. However, their putative active sites contain a QACQG pentapeptide instead of the QACRG present in ail known ASCPs. Also, their N termini contain FADD-like death effector domains, suggesting possible interaction with FADD. Expression of Mch4 in Escherichia coli produced an active protease that, like other ASCPs, was potently inhibited (Kj = 14 nM) by the tetrapeptide aldehyde DEVD-CHO. Interestingly, both Mch4 and the serine protease granzyme B cleave recombinant proCPP32 and proMch3 at a conserved IXXD-S sequence to produce the large and small subunits of the active proteases. Granzyme B also cleaves proMch4 at a homologous IXXD-A processing sequence to produce mature Mch4. These observations suggest that CPP32 and Mch3 are targets of mature Mch4 protease in apoptotic cells. The presence of the FADD-like domains in Mch4 and Mch5 suggests a role for these proteases in the Fas-apoptotic pathway. In addition, these proteases could participate in the granzyme B apoptotic pathways.
In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains.
T Fernandes-Alnemri, R C Armstrong, J Krebs, S M Srinivasula, L Wang, F Bullrich, L C Fritz, J A Trapani, K J Tomaselli, G Litwack, and E S Alnemri
1996 Jul 23
Objectives To examine how lifestyle, hormonal, and other factors influence the sensitivity and specificity of mammography.
Methods Women recruited into the Million Women Study completed a questionnaire about various personal factors before routine mammographic screening. A sample of 122 355 women aged 50-64 years were followed for outcome of screening and incident breast cancer in the next 12 months. Sensitivity and specificity were calculated by using standard definitions, with adjustment for potential confounding factors.
Results Breast cancer was diagnosed in 726 (0.6%) women, 629 in screen positive and 97 in screen negative women; 3885 (3.2%) were screen positive but had no subsequent diagnosis of breast cancer. Overall sensitivity was 86.6% and specificity was 96.8%. Three factors had an adverse effect on both measures: use of hormone replacement therapy (sensitivity: 83.0% (95% confidence interval 77.4% to 87.6%), 84.7% (73.9% to 91.6%), and 92.1% (87.6% to 95.0%); specificity: 96.8% (96.6% to 97.0%), 97.8% (97.5% to 98.0%), and 98.1% (98.0% to 98.2%), respectively, for current, past, and never use); previous breast surgery v no previous breast surgery (sensitivity: 83.5% (75.7% to 89.1%) v 89.4% (86.5% to 91.8%); specificity: 96.2% (95.8% to 96.5%) v 97.4% (97.3% to 97.5%), respectively); and body mass index < 25 v ≥ 25 (sensitivity: 85.7% (81.2% to 89.3%) v 91.0% (87.5% to 93.6%); specificity: 97.2% (97.0% to 97.3%) v 97.4% (97.3% to 97.6%), respectively). Neither sensitivity nor specificity varied significantly according to age, family history of breast cancer, parity, past oral contraceptive use, tubal ligation, physical activity, smoking, or alcohol consumption. Conclusions The efficiency, and possibly the effectiveness, of mammographic screening is lower in users of hormone replacement therapy, in women with previous breast surgery, and in thin women compared with other wome
Influence of personal characteristics of individual women on sensitivity and specificity of mammography in the Million Women Study: cohort study
Emily Banks, deputy director,1 Gillian Reeves, statistical epidemiologist,1 Valerie Beral, director,1 Diana Bull, senior statistician,1 Barbara Crossley, chief data manager,1 Moya Simmonds, clinical coordinator,1 Elizabeth Hilton, clinical coordinator,1 Stephen Bailey, clinical director,2 Nigel Barrett, clinical director,3 Peter Briers, clinical director,4 Ruth English, clinical director,5 Alan Jackson, consultant radiologist,6 Elizabeth Kutt, clinical director,7 Janet Lavelle, clinical director,8 Linda Rockall, clinical director,9 Matthew G Wallis, clinical director,10 Mary Wilson, clinical director,11 and Julietta Patnick, national coordinator12
2004 Aug 28;
endo?α?1,2?Mannosidases and ?mannanases, members of glycoside hydrolase family 99 (GH99), cleave α?Glc/Man?1,3?α?Man?OR structures within mammalian N?linked glycans and fungal α?mannan, respectively. They are proposed to act through a two?step mechanism involving a 1,2?anhydrosugar “epoxide” intermediate incorporating two conserved catalytic carboxylates. In the first step, one carboxylate acts as a general base to deprotonate the 2?hydroxy group adjacent to the fissile glycosidic bond, and the other provides general acid assistance to the departure of the aglycon. We report herein the synthesis of two inhibitors designed to interact with either the general base (α?mannosyl?1,3?(2?aminodeoxymannojirimycin), Man2NH2DMJ) or the general acid (α?mannosyl?1,3?mannoimidazole, ManManIm). Modest affinities were observed for an endo?α?1,2?mannanase from Bacteroides thetaiotaomicron. Structural studies revealed that Man2NH2DMJ binds like other iminosugar inhibitors, which suggests that the poor inhibition shown by this compound is not a result of a failure to achieve the expected interaction with the general base, but rather the reduction in basicity of the endocyclic nitrogen caused by introduction of a vicinal, protonated amine at C2. ManManIm binds with the imidazole headgroup distorted downwards, a result of an unfavourable interaction with a conserved active site tyrosine. This study has identified important limitations associated with mechanism?inspired inhibitor design for GH99 enzymes.
enzymes, glycosidase, imidazole rings, inhibitors, X-ray crystallography
Exploration of Strategies for Mechanism?Based Inhibitor Design for Family GH99 endo?α?1,2?Mannanases
Pearl Z. Fernandes, 1 Marija Petricevic, 1 Lukasz Sobala, 2 Prof. Gideon J. Davies,corresponding author 2 and Prof. Spencer J. Williamscorresponding author 1
2018 May 23;