Filters
Results 1 - 10 of 1828
Results 1 - 10 of 1828.
Search took: 0.025 seconds
Sort by: date | relevance |
Li, Yan; Loh, Ying Ru; Hung, Alvin W.; Kang, CongBao, E-mail: cbkang@etc.a-star.edu.sg2018
AbstractAbstract
[en] Highlights: • The TGKR residues in eZiPro protease are dynamic in solution. • Peptides derived from NS2B C-terminus exhibit different binding affinities to protease. • Free NS2B cofactor region is flexible in solution. • The eZiPro construct binds to peptides and a fragment. Zika virus (ZIKV) protease is a two-component complex in which NS3 contains the catalytic triad and NS2B cofactor region is important for protease folding and activity. A protease construct-eZiPro without the transmembrane domains of NS2B was designed. Structural study on eZiPro reveals that the Thr-Gly-Lys-Arg (TGKR) sequence at the C-terminus of NS2B binds to the active site after cleavage. The bZiPro construct only contains NS2B cofactor region and the N-terminus of NS3 without any artificial linker or protease cleavage site, giving rise to an empty pocket accessible to substrate and inhibitor binding. Herein, we demonstrate that the TGKR sequence of NS2B in eZiPro is dynamic. Peptides from NS2B with various lengths exhibit different binding affinities to bZiPro. TGKR binding to the active site in eZiPro does not affect protease binding to small-molecule compounds. Our results suggest that eZiPro will also be useful for evaluating small-molecule protease inhibitors.
Primary Subject
Source
S0006291X18313743; Available from http://dx.doi.org/10.1016/j.bbrc.2018.06.062; Copyright (c) 2018 Elsevier Inc. All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Journal
Biochemical and Biophysical Research Communications; ISSN 0006-291X;
; CODEN BBRCA9; v. 503(2); p. 691-696

Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
AbstractAbstract
[en] Malignant pleural mesothelioma (MPM) is an aggressive malignancy closely associated with asbestos exposure and extremely resistant to current treatments. It exhibits a steady increase in incidence, thus necessitating an urgent development of effective new treatments. Proteasome inhibitors (PIs) and TNFα-Related Apoptosis Inducing Ligand (TRAIL), have emerged as promising new anti-MPM agents. To develop effective new treatments, the proapoptotic effects of PIs, MG132 or Bortezomib, and TRAIL were investigated in MPM cell lines NCI-H2052, NCI-H2452 and NCI-H28, which represent three major histological types of human MPM. Treatment with 0.5-1 μM MG132 alone or 30 ng/mL Bortezomib alone induced a limited apoptosis in MPM cells associated with the elevated Mcl-1 protein level and hyperactive PI3K/Akt signaling. However, whereas 10–20 ng/ml TRAIL alone induced a limited apoptosis as well, TRAIL and PI combination triggered a robust apoptosis in all three MPM cell lines. The robust proapoptotic activity was found to be the consequence of a positive feedback mechanism-governed amplification of caspase activation and cleavage of both Mcl-1 and Akt proteins, and exhibited a relative selectivity in MPM cells than in non-tumorigenic Met-5A mesothelial cells. The combinatorial treatment using TRAIL and PI may represent an effective new treatment for MPMs
Primary Subject
Secondary Subject
Source
Available from http://dx.doi.org/10.1186/1471-2407-13-140; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3665596; PMCID: PMC3665596; PUBLISHER-ID: 1471-2407-13-140; PMID: 23517112; OAI: oai:pubmedcentral.nih.gov:3665596; Copyright (c) 2013 Yuan et al.; licensee BioMed Central Ltd.; This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0) (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Journal
BMC cancer (Online); ISSN 1471-2407;
; v. 13; p. 140

Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
External URLExternal URL
AbstractAbstract
[en] The properties of hammerhead ribozymes are described. Various hammerhead ribozyme constructs for target RNA cleavage were considered. Approaches to enhancement of the stability of artificial ribozymes in biological media and to regulation of the catalytic activity of hammerhead ribozymes using effector molecules are described. The effect of ribozymes on extended structured natural RNAs is discussed. Applications of artificial hammerhead ribozymes as inhibitors of gene expression at matrix RNA level were considered.
Primary Subject
Source
Available from http://dx.doi.org/10.1070/RC2011v080n02ABEH004142; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Journal
Russian Chemical Reviews (Print); ISSN 0036-021X;
; v. 80(2); p. 127-143

Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
Sánchez-Martínez, Cristina; Grueso, Esther; Carroll, Miles; Rommelaere, Jean; Almendral, José M., E-mail: jmalmendral@cbm.uam.es2012
AbstractAbstract
[en] The unordered N-termini of parvovirus capsid proteins (Nt) are translocated through a channel at the icosahedral five-fold axis to serve for virus traffick. Heterologous peptides were genetically inserted at the Nt of MVM to study their functional tolerance to manipulations. Insertion of a 5T4-single-chain antibody at VP2-Nt (2Nt) yielded chimeric capsid subunits failing to enter the nucleus. The VEGFR2-binding peptide (V1) inserted at both 2Nt and VP1-Nt efficiently assembled in virions, but V1 disrupted VP1 and VP2 entry functions. The VP2 defect correlated with restricted externalization of V1-2Nt out of the coat. The specific infectivity of MVM and wtVP-pseudotyped mosaic MVM-V1 virions, upon heating and/or partial 2Nt cleavage, demonstrated that some 2Nt domains become intracellularly translocated out of the virus shell and cleaved to initiate entry. The V1 insertion defines a VP2-driven endosomal enlargement of the channel as an essential structural rearrangement performed by the MVM virion to infect.
Primary Subject
Source
S0042-6822(12)00276-0; Available from http://dx.doi.org/10.1016/j.virol.2012.05.025; Copyright (c) 2012 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Journal
Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
AbstractAbstract
[en] Flavivirus RNA replication starts at 3′-end, where it folds into a highly conserved stem-loop structure. We attempted to identify the viral non-structural proteins (NSPs) that might specifically interact with the 3′-stemloop (3′SL) through a genetic approach. WNV/DENV2 chimeric recombinants that contain Dengue2 (DENV2) gene(s) in West Nile virus (WNV) backbone were tested for replication competence. Three of seven recombinant viruses, containing the DENV2 NS1, NS2A, or NS4B gene and terminated with a mutated 3′SL (MutC 3′SL), were viable. Of these three, only those bearing the DENV2 NS1 and NS2A substitutions remained infectious when the MutC 3′SL was replaced by the wildtype WNV 3′SL. However, none of the seven chimeric recombinants bearing the DENV2 3′SL were viable. We then investigated the causes for failed replication of WNV/DENV2 chimeric recombinants. Proteolytic cleavage of NS polyproteins was defective by heterologous protease NS2B/3, but was efficient by homologous DENV2 NS2B/3 protease. Whereas, the heterologous polyproteins that contained DENV2 homologous protease were found to produce abnormal vesicles. WNV/DENV2 recombinants expressing the DENV2 homologous protease did not produce infectious virus either. We examined NS protein-protein interaction (PPI) and found that heterologous PPI (hPPI) between WNV and DENV2 NSPs were impaired to various degrees. Insufficient PPIs occurred mainly between heterologous NS2B and NS3; NS2B and NS4A; NS3 and NS5, correlating to those non-viability of substitution mutants. Our results indicate that impaired PPI may decrease protease activity and affect vesicle formation, and is the essential cause for non-viability of the WNV/DENV2 recombinants.
Primary Subject
Source
S004268221830254X; Available from http://dx.doi.org/10.1016/j.virol.2018.08.013; Published by Elsevier Inc.; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Journal
Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
AbstractAbstract
[en] The peptidyl-tRNA hydrolase from M. tuberculosis has been crystallized in three closely related forms, two orthorhombic and one monoclinic, and X-ray diffraction data have been collected from them. Peptidyl-tRNA hydrolase catalyses the cleavage of the ester link between the peptide and the tRNA in peptidyl-tRNAs that, for various reasons, have dropped off the translating ribosomes. This enzyme from Mycobacterium tuberculosis has been crystallized in three related but distinct forms: P212121, unit-cell parameters a = 36.30, b = 61.85, c = 73.97 Å, P21, a = 35.83, b = 73.79, c = 59.79 Å, β = 92.3°, and P212121, a = 35.84, b = 57.06, c = 72.59 Å. X-ray data have been collected from all three forms
Source
S1744309106031125; Available from http://dx.doi.org/10.1107/S1744309106031125; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2242860; PMCID: PMC2242860; PMID: 16946478; PUBLISHER-ID: bw5155; OAI: oai:pubmedcentral.nih.gov:2242860; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Journal
Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
External URLExternal URL
Galande, Sanjeev; Dickinson, Liliane A.; Mian, I.Saira; Sikorska, Marianna; Kohwi-Shigematsu, Terumi
Lawrence Berkeley National Lab., CA (United States). Funding organisation: USDOE Director, Office of Science. Office of Biological and Environmental Research. Life Sciences Division (United States)2001
Lawrence Berkeley National Lab., CA (United States). Funding organisation: USDOE Director, Office of Science. Office of Biological and Environmental Research. Life Sciences Division (United States)2001
AbstractAbstract
No abstract available
Primary Subject
Source
LBNL--47950; AC03-76SF00098; Available from Lawrence Berkeley National Lab., CA (US); Journal Publication Date: Aug. 2001
Record Type
Journal Article
Journal
Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
AbstractAbstract
[en] A series of functionalized furans were synthesized by way of a palladium -catalyzed coupling reaction of 2,3,5-tri substituted furans with aryl chlorides through C-H bond cleavages at C-4 position. The feature of the reaction was facilitative preparation of furan derivatives with good functional group tolerance. All reactions gave the desired products in moderate to good yields in the presences of BuAd2P and t-BuOK in DMF at 120 .deg. C after 15 h
Primary Subject
Source
42 refs, 2 figs, 3 tabs
Record Type
Journal Article
Journal
Bulletin of the Korean Chemical Society; ISSN 0253-2964;
; v. 33(8); p. 2623-2626

Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
Nabavi, Sadeq; Nazar, Ross N., E-mail: rnnazar@uoguelph.ca2010
AbstractAbstract
[en] The maturation of many small nuclear RNAs is dependent on RNase III-like endonuclease mediated cleavage, which generates a loading site for the exosome complex that trims the precursor at its 3' end. Using a temperature sensitive Pac1 nuclease, here we show that the endonuclease cleavage is equally important in terminating the transcription of the U2 snRNA in Schizosaccharomyces pombe. Using a temperature sensitive Dhp1p 5' → 3' exonuclease, we demonstrate that it also is an essential component of the termination pathway. Taken together the results support a 'reversed torpedoes' model for the termination and maturation of the U2 snRNA; the Pac1 endonuclease cleavage provides entry sites for the 3' and 5' exonuclease activities, leading to RNA maturation in one direction and transcript termination in the other.
Primary Subject
Source
S0006-291X(10)00234-2; Available from http://dx.doi.org/10.1016/j.bbrc.2010.02.023; Copyright (c) 2010 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Record Type
Journal Article
Journal
Biochemical and Biophysical Research Communications; ISSN 0006-291X;
; CODEN BBRCA9; v. 393(3); p. 461-465

Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
Taylor, A.B.; Smith, B.S.; Kitada, S.; Kojima, K.; Miyaura, H.; Otwinowski, Z.; Ito, A.; Deisenhofer, J.
Ernest Orlando Lawrence Berkeley National Lab., Advanced Light Source, Berkeley, CA (United States). Funding organisation: US Department of Energy (United States)2001
Ernest Orlando Lawrence Berkeley National Lab., Advanced Light Source, Berkeley, CA (United States). Funding organisation: US Department of Energy (United States)2001
AbstractAbstract
No abstract available
Primary Subject
Source
LBNL/ALS--43273; AC03-76SF00098; Journal Publication Date: July 2001
Record Type
Journal Article
Journal
Structure (London); ISSN 0969-2126;
; v. 9(7); [10 p.]

Country of publication
Reference NumberReference Number
INIS VolumeINIS Volume
INIS IssueINIS Issue
1 | 2 | 3 | Next |