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Recent "biomolecular" articles

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Conserved surface features form the double-stranded RNA binding site of non-structural protein 1 (NS1) from influenza A and B viruses.
Cuifeng Yin et al.
The Journal of biological chemistry 282 (28), 20584-92 (13 Jul 2007)
info:pmid/17475623 | info:doi/10.1074/jbc.M611619200
Posted by gabanyi to Viral Nonstructural Proteins viral Double-Stranded RNA secondary Quaternary protein structure protein folding Protein Binding Nucleic Acid Conformation Biomolecular Nuclear Magnetic Resonance Mortality human influenza Influenza B virus pathogenicity metabolism chemistry Influenza A Virus humans dimerization X-ray crystallography on Wed Aug 06 2008 at 18:42 UTC | info | related
 
Solution NMR structure of the junction between tropomyosin molecules: implications for actin binding and regulation.
Norma J Greenfield et al.
Journal of molecular biology 364 (1), 80-96 (17 Nov 2006)
info:pmid/16999976 | info:doi/10.1016/j.jmb.2006.08.033
Posted by gabanyi to tropomyosin rats Tertiary secondary protein structure Protein Binding genetics chemistry Peptides Biomolecular Nuclear Magnetic Resonance Multiprotein Complexes Molecular Sequence Data Molecular Models X-ray crystallography animals Amino Acid Sequence metabolism Actins on Wed Aug 06 2008 at 18:42 UTC | info | related
 
Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.
Marcius S Almeida et al.
Journal of virology 81 (7), 3151-61 (Apr 2007)
info:pmid/17202208 | info:doi/10.1128/JVI.01939-06
Posted by gabanyi to Viral Nonstructural Proteins Enzymology Sars Virus Recombinant Proteins RNA Replicase Tertiary secondary protein structure protein folding metabolism genetics chemistry Peptide Fragments Biomolecular Nuclear Magnetic Resonance Molecular Sequence Data Molecular Models Amino Acid Sequence on Wed Aug 06 2008 at 18:42 UTC | info | related
 
Applications of laser-polarized 129Xe to biomolecular assays
Thomas J Lowery et al.
Magnetic resonance imaging 21 (10), 1235-9 (Dec 2003)
info:pmid/14725931
Posted by gjwilliams2 to Xenon Isotopes Non-P.H.S. U.S. Gov't Non-U.S. Gov't Research Support Protein Conformation methods diagnostic use Biomolecular Nuclear Magnetic Resonance Ligands lasers humans on Thu Jul 03 2008 at 00:15 UTC | info | related
 
Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain
Silke Wiesner et al.
Cell 130 (4), 651-62 (24 Aug 2007)
info:pmid/17719543 | info:doi/10.1016/j.cell.2007.06.050
Posted by DrMatt to inhibitorschemistrygenetics*metabolism Ubiquitin-Protein Ligases*antagonists & Smad7 Proteinchemistry Recombinant Proteinsmetabolism Tertiary protein structure Protein Binding Phosphatidylinositolsmetabolism Biomolecular Nuclear Magnetic Resonance mutation Molecular chemical Biological Models humans Glutathione Transferasemetabolism Cysteinemetabolism Catalytic Domain binding sites uploaded on Thu Nov 15 2007 at 14:00 UTC | info | related
 
Atherogenic lipoprotein particles in atherosclerosis.
Atherogenic Lipoprotein Particles in Atherosclerosis
Circulation 109 (23_suppl_1), III-2 (2004)
info:doi/10.1161/01.cir.0000131511.50734.44
The importance of low-density lipoprotein (LDL) cholesterol in the development of atherosclerosis has long been recognized, and LDL cholesterol remains the primary target of therapy for the prevention of coronary heart disease. Nevertheless, increasing research attention over the past decade has been devoted to the heterogeneity of LDL particles and the atherogenicity of lipids and lipoproteins other than LDL. Particularly atherogenic forms of LDL include small, dense LDL particles and oxidized LDL. All lipoproteins that contain apolipoprotein B, such as LDL, very-low-density lipoprotein, and intermediate-density lipoprotein, tend to promote atherosclerosis; however, these particles differ in their apolipoprotein and triglyceride content. High levels of plasma triglycerides increase the risk of acute coronary events. Lipoprotein(a) is now considered an independent risk factor in both men and women. Ultimately, better understanding of the roles of these lipid particles and subfractions in the initiation and progression of atherosclerosis may affect treatment decisions.
Posted by mingzhai to Nucl Metabolic Syndrome X Male lipoproteins LDL cholesterol LDL humans gel female Epidemiologic Research Design disease susceptibility Density Gradient Coronary Arteriosclerosis Chromatography Centrifugation Biomolecular Arteriosclerosis on Mon Jul 16 2007 at 19:27 UTC | info | related
 
The Bacillus subtilis cell division proteins FtsL and DivIC are intrinsically unstable and do not interact with one another in the absence of other septasomal components
The Bacillus subtilis cell division proteins FtsL and DivIC are intrinsically unstable and do not interact with one another in the absence of other septasomal components
Scott A Robson et al.
Molecular microbiology 44 (3), 663-74 (May 2002)
info:pmid/11994149
DA - 20020507 IS - 0950-382X (Print) LA - eng PT - Journal Article RN - 0 (Bacterial Proteins) RN - 0 (Cell Cycle Proteins) RN - 0 (DivIC protein, Bacillus subtilis) RN - 0 (Escherichia coli Proteins) RN - 0 (Macromolecular Substances) RN - 0 (Membrane Proteins) RN - 0 (Recombinant Fusion Proteins) RN - 0 (ftsL protein, E coli) SB - IM
Posted by ndhoang to Ultracentrifugation Two-Hybrid System Techniques thermodynamics structure-activity relationship Amino Acid Sequence Homology Sequence Alignment Saccharomyces cerevisiae Recombinant Fusion Proteins proteins Tertiary protein structure Protein Interaction Mapping protein folding Protein Denaturation Protein Biomolecular Nuclear Magnetic Resonance Nephelometry and Turbidimetry Molecular Sequence Data methods metabolism membrane proteins Macromolecular Substances Isoelectric Point Escherichia coli Proteins Escherichia coli cytology COMPARATIVE STUDY circular dichroism chemistry cell division Cell Cycle Proteins cell cycle biochemistry Bacterial Proteins Bacillus subtilis Bacillus analysis Amino Acid Sequence on Wed Jan 10 2007 at 08:13 UTC | info | related
 
NMR-spectroscopic mapping of an engineered cavity in the I14A mutant of HPr from Staphylococcus carnosus using xenon
Christian Gröger et al.
Journal of the American Chemical Society 125 (29), 8726-7 (23 Jul 2003)
info:pmid/12862458 | info:doi/10.1021/ja030113t
DA - 20030716 IS - 0002-7863 (Print) LA - eng PT - Journal Article RN - 0 (Bacterial Proteins) RN - 0 (Nitrogen Isotopes) RN - 0 (Protons) RN - 56-41-7 (Alanine) RN - 73-32-5 (Isoleucine) RN - 7440-63-3 (Xenon) RN - EC 2.7.1.- (Phosphoenolpyruvate Sugar Phosphotransferase System) RN - EC 2.7.1.- (phosphocarrier protein HPr) SB - IM
Posted by ndhoang to xenon Staphylococcus Non-U.S.Gov't Research Support Protons proteins Protein engineering Protein Phosphoenolpyruvate Sugar Phosphotransferase System Biomolecular Nuclear Magnetic Resonance nitrogen isotopes nitrogen methods Isoleucine hydrophobicity genetics chemistry biophysics biochemistry Bacterial Proteins Amino Acid Substitution Alanine on Tue Jan 09 2007 at 17:56 UTC | info | related
 
Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphylococcus carnosus
Andreas Möglich et al.
European journal of biochemistry / FEBS 271 (23-24), 4815-24 (Dec 2004)
info:pmid/15606769 | info:doi/10.1111/j.1432-1033.2004.04447.x
DA - 20041220 IS - 0014-2956 (Print) LA - eng PT - Journal Article RN - 0 (Bacterial Proteins) RN - 7440-63-3 (Xenon) RN - EC 2.7.1.- (Phosphoenolpyruvate Sugar Phosphotransferase System) RN - EC 2.7.1.- (phosphocarrier protein HPr) SB - IM
Posted by ndhoang to xenon Staphylococcus Non-U.S.Gov't Research Support proteins Protein Conformation Protein Binding Protein Phosphoenolpyruvate Sugar Phosphotransferase System Biomolecular Nuclear Magnetic Resonance mutation Molecular Models metabolism hydrogen bonding hydrogen Histidine genetics chemistry biophysics biochemistry binding sites Bacterial Proteins on Tue Jan 09 2007 at 17:56 UTC | info | related
 
Structure of subtilosin A, a cyclic antimicrobial peptide from Bacillus subtilis with unusual sulfur to alpha-carbon cross-links: formation and reduction of alpha-thio-alpha-amino acid derivatives
Karen E Kawulka et al.
Biochemistry 43 (12), 3385-95 (30 Mar 2004)
info:pmid/15035610 | info:doi/10.1021/bi0359527
DA - 20040323 IS - 0006-2960 LA - eng PT - Journal Article RN - 0 (Anti-Bacterial Agents) RN - 0 (Antibiotics, Peptide) RN - 0 (Bacterial Proteins) RN - 0 (Boranes) RN - 0 (Cross-Linking Reagents) RN - 0 (Peptides) RN - 0 (Peptides, Cyclic) RN - 0 (Sulfhydryl Compounds) RN - 12619-90-8 (nickel boride) RN - 52-90-4 (Cysteine) RN - 63-91-2 (Phenylalanine) RN - 72-19-5 (Threonine) RN - 7440-02-0 (Nickel) RN - 7440-44-0 (Carbon) RN - 7704-34-9 (Sulfur) RN - 98914-01-3 (sboA protein, Bacillus subtilis) SB - IM
Posted by ndhoang to Threonine Sulfur Sulfhydryl Compounds Stereoisomerism Non-U.S.Gov't Research Support proteins Post-Translational Protein Processing Phenylalanine Cyclic Peptides Oxidation-Reduction Biomolecular Nuclear Magnetic Resonance Nickel Molecular Sequence Data methods Hydrolysis cysteine X-ray crystallography Cross-Linking Reagents chemistry carbon Boranes Bacterial Proteins Bacillus subtilis Bacillus peptide antibiotics Anti-Bacterial Agents analysis amino acids Amino Acid Sequence on Mon Jan 08 2007 at 18:52 UTC | info | related

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