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Wyszukujesz frazę ""Protein Structure, Secondary"" wg kryterium: Temat


Tytuł:
Interaction of constituents of MDT regimen for leprosy with Mycobacterium leprae HSP18: impact on its structure and function.
Autorzy:
Chakraborty A; School of Basic Sciences, Indian Institute of Technology Bhubaneswar, India.
Ghosh R; School of Basic Sciences, Indian Institute of Technology Bhubaneswar, India.
Biswas A; School of Basic Sciences, Indian Institute of Technology Bhubaneswar, India.
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Źródło:
The FEBS journal [FEBS J] 2022 Feb; Vol. 289 (3), pp. 832-853. Date of Electronic Publication: 2021 Oct 10.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Antigens, Bacterial/*genetics
Bacterial Proteins/*genetics
Heat-Shock Proteins/*genetics
Leprosy/*drug therapy
Mycobacterium leprae/*genetics
Antigens, Bacterial/immunology ; Bacterial Proteins/ultrastructure ; Clofazimine/pharmacology ; Dapsone/pharmacology ; Heat-Shock Proteins/ultrastructure ; Host-Pathogen Interactions/genetics ; Humans ; Hydrophobic and Hydrophilic Interactions/drug effects ; Leprostatic Agents/chemistry ; Leprostatic Agents/pharmacology ; Leprosy/genetics ; Leprosy/immunology ; Leprosy/microbiology ; Molecular Chaperones/chemistry ; Molecular Chaperones/genetics ; Mycobacterium leprae/pathogenicity ; Protein Binding/drug effects ; Protein Structure, Secondary/drug effects ; Rifampin/pharmacology
Czasopismo naukowe
Tytuł:
Tryptophan Side-Chain Oxidase Enzyme Suppresses Hepatocellular Carcinoma Growth through Degradation of Tryptophan.
Autorzy:
Ai Y; The State Key Laboratory of Virology, College of Life Sciences, Wuhan University, 299 BaYi Road, Wuhan 430065, China.
Wang B; The State Key Laboratory of Virology, College of Life Sciences, Wuhan University, 299 BaYi Road, Wuhan 430065, China.
Xiao S; The State Key Laboratory of Virology, College of Life Sciences, Wuhan University, 299 BaYi Road, Wuhan 430065, China.
Luo S; The State Key Laboratory of Virology, College of Life Sciences, Wuhan University, 299 BaYi Road, Wuhan 430065, China.
Wang Y; The State Key Laboratory of Virology, College of Life Sciences, Wuhan University, 299 BaYi Road, Wuhan 430065, China.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Nov 18; Vol. 22 (22). Date of Electronic Publication: 2021 Nov 18.
Typ publikacji:
Journal Article
MeSH Terms:
Antineoplastic Agents/*pharmacology
Bacterial Proteins/*pharmacology
Carcinoma, Hepatocellular/*drug therapy
Liver Neoplasms/*drug therapy
Mixed Function Oxygenases/*pharmacology
Tryptophan/*metabolism
Animals ; Antineoplastic Agents/chemistry ; Antineoplastic Agents/isolation & purification ; Apoptosis/drug effects ; Apoptosis/genetics ; Bacterial Proteins/biosynthesis ; Bacterial Proteins/genetics ; Bacterial Proteins/isolation & purification ; Carcinoma, Hepatocellular/genetics ; Carcinoma, Hepatocellular/metabolism ; Carcinoma, Hepatocellular/pathology ; Cell Line, Tumor ; Cell Movement/drug effects ; Cell Proliferation/drug effects ; Gene Expression Regulation, Neoplastic ; Glycogen Synthase Kinase 3 beta/genetics ; Glycogen Synthase Kinase 3 beta/metabolism ; Hep G2 Cells ; Humans ; Liver Neoplasms/genetics ; Liver Neoplasms/metabolism ; Liver Neoplasms/pathology ; Matrix Metalloproteinase 2/genetics ; Matrix Metalloproteinase 2/metabolism ; Mice ; Mice, Nude ; Mixed Function Oxygenases/biosynthesis ; Mixed Function Oxygenases/genetics ; Mixed Function Oxygenases/isolation & purification ; Models, Molecular ; Proliferating Cell Nuclear Antigen/genetics ; Proliferating Cell Nuclear Antigen/metabolism ; Protein Structure, Secondary ; Pseudomonas/chemistry ; Pseudomonas/enzymology ; Pseudomonas/genetics ; Signal Transduction ; Tumor Burden/drug effects ; Xenograft Model Antitumor Assays ; bcl-2-Associated X Protein/genetics ; bcl-2-Associated X Protein/metabolism
Czasopismo naukowe
Tytuł:
Characterisation of a putative M23-domain containing protein in Mycobacterium tuberculosis.
Autorzy:
Papadopoulos AO; Faculty of Health Sciences, DSI/NRF Centre of Excellence for Biomedical TB Research, School of Pathology, University of the Witwatersrand, National Health Laboratory Service, Johannesburg, South Africa.
Ealand C; Faculty of Health Sciences, DSI/NRF Centre of Excellence for Biomedical TB Research, School of Pathology, University of the Witwatersrand, National Health Laboratory Service, Johannesburg, South Africa.
Gordhan BG; Faculty of Health Sciences, DSI/NRF Centre of Excellence for Biomedical TB Research, School of Pathology, University of the Witwatersrand, National Health Laboratory Service, Johannesburg, South Africa.
VanNieuwenhze M; Department of Chemistry, Indiana University Bloomington, Bloomington, Indiana, United States of America.
Kana BD; Faculty of Health Sciences, DSI/NRF Centre of Excellence for Biomedical TB Research, School of Pathology, University of the Witwatersrand, National Health Laboratory Service, Johannesburg, South Africa.
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Źródło:
PloS one [PLoS One] 2021 Nov 16; Vol. 16 (11), pp. e0259181. Date of Electronic Publication: 2021 Nov 16 (Print Publication: 2021).
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms:
Bacterial Proteins/*metabolism
Endopeptidases/*metabolism
Mycobacterium tuberculosis/*metabolism
Amino Acid Motifs ; Antitubercular Agents/pharmacology ; Bacterial Proteins/chemistry ; Bacterial Proteins/classification ; Bacterial Proteins/genetics ; Cell Wall/metabolism ; Endopeptidases/chemistry ; Endopeptidases/classification ; Endopeptidases/genetics ; Mutation ; Mycobacterium tuberculosis/drug effects ; Mycobacterium tuberculosis/growth & development ; Phylogeny ; Protein Structure, Secondary
Czasopismo naukowe
Tytuł:
Structural and Functional Insights into the Biofilm-Associated BceF Tyrosine Kinase Domain from Burkholderia cepacia .
Autorzy:
Mayer M; Department of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel.; Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7610001, Israel.
Matiuhin Y; Department of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel.; Entoprotech Ltd., 2 Ner Halayla, Caesarea 3088900, Israel.
Nawatha M; Department of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel.
Tabachnikov O; Department of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel.
Fish I; Department of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.; Department of Pharmaceutical Chemistry, University of California San Francisco, 1700 4th Street, San Francisco, CA 94143-2550, USA.
Schutz N; Kamari Pharma, Nes Ziona 7403626, Israel.
Dvir H; Institute of Animal Science, Volcani Institute, Agricultural Research Organization, Rishon LeZiyon 7528809, Israel.
Landau M; Department of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel.; European Molecular Biology Laboratory (EMBL), 22607 Hamburg, Germany.
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Źródło:
Biomolecules [Biomolecules] 2021 Aug 12; Vol. 11 (8). Date of Electronic Publication: 2021 Aug 12.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Bacterial Proteins/*chemistry
Bacterial Proteins/*physiology
Biofilms/*growth & development
Burkholderia cepacia/*physiology
Protein-Tyrosine Kinases/*chemistry
Protein-Tyrosine Kinases/*physiology
Crystallography, X-Ray/methods ; Humans ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Virulence/physiology
Czasopismo naukowe
Tytuł:
Structural and Functional Elucidation of IF-3 Protein of Chloroflexus aurantiacus Involved in Protein Biosynthesis: An In Silico Approach.
Autorzy:
Saikat ASM; Department of Biochemistry and Molecular Biology, Bangabandhu Sheikh Mujibur Rahman Science and Technology University, Gopalganj 8100, Bangladesh.
Uddin ME; Department of Biochemistry and Molecular Biology, Gono University, Dhaka 1344, Bangladesh.
Ahmad T; Department of Biotechnology and Genetic Engineering, Islamic University, Jhenidah-Kushtia, Bangladesh.
Mahmud S; Department of Biotechnology and Genetic Engineering, Islamic University, Jhenidah-Kushtia, Bangladesh.
Imran MAS; Department of Biotechnology and Genetic Engineering, Islamic University, Jhenidah-Kushtia, Bangladesh.
Ahmed S; Department of Biochemistry and Molecular Biology, Jahangirnagar University, Dhaka 1342, Bangladesh.
Alyami SA; Department of Mathematics and Statistics, Faculty of Science, Imam Mohammad Ibn Saud Islamic University (IMSIU), Riyadh 13318, Saudi Arabia.
Moni MA; School of Psychiatry, Faculty of Medicine, University of New South Wales, Sydney, NSW 2052, Australia.; Healthy Ageing Theme, The Garvan Institute of Medical Research, Darlinghurst, NSW 2010, Australia.
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Źródło:
BioMed research international [Biomed Res Int] 2021 Jul 01; Vol. 2021, pp. 9050026. Date of Electronic Publication: 2021 Jul 01 (Print Publication: 2021).
Typ publikacji:
Journal Article
MeSH Terms:
Computer Simulation*
Protein Biosynthesis*
Bacterial Proteins/*chemistry
Bacterial Proteins/*metabolism
Chloroflexus/*metabolism
Amino Acid Sequence ; Catalytic Domain ; Models, Molecular ; Molecular Sequence Annotation ; Protein Interaction Maps ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Structure-Activity Relationship ; Subcellular Fractions/metabolism
SCR Organism:
Chloroflexus aurantiacus
Czasopismo naukowe
Tytuł:
Crystal structures of Val58Ile tryptophan repressor in a domain-swapped array in the presence and absence of L-tryptophan.
Autorzy:
Sprenger J; Department of Chemistry, University of Copenhagen, DK-2100 Copenhagen, Denmark.
Lawson CL; Institute for Quantitative Biomedicine, Rutgers University, Piscataway, NJ 08854, USA.
von Wachenfeldt C; Department of Biology, Lund University, SE-221 00 Lund, Sweden.
Lo Leggio L; Department of Chemistry, University of Copenhagen, DK-2100 Copenhagen, Denmark.
Carey J; Chemistry Department, Princeton University, Princeton, NJ 08544, USA.
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Źródło:
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2021 Jul 01; Vol. 77 (Pt 7), pp. 215-225. Date of Electronic Publication: 2021 Jul 30.
Typ publikacji:
Journal Article
MeSH Terms:
Bacterial Proteins/*chemistry
Isoleucine/*chemistry
Repressor Proteins/*chemistry
Tryptophan/*chemistry
Valine/*chemistry
X-Ray Diffraction/*methods
Amino Acid Sequence ; Bacterial Proteins/genetics ; Crystallography, X-Ray/methods ; Escherichia coli/genetics ; Isoleucine/genetics ; Protein Domains/genetics ; Protein Structure, Secondary ; Repressor Proteins/genetics ; Tryptophan/genetics ; Valine/genetics
Czasopismo naukowe
Tytuł:
Evolution of a virus-like architecture and packaging mechanism in a repurposed bacterial protein.
Autorzy:
Tetter S; Laboratory of Organic Chemistry, ETH Zurich, 8093 Zurich, Switzerland.
Terasaka N; Laboratory of Organic Chemistry, ETH Zurich, 8093 Zurich, Switzerland.
Steinauer A; Laboratory of Organic Chemistry, ETH Zurich, 8093 Zurich, Switzerland.
Bingham RJ; Departments of Mathematics and Biology, University of York, York YO10 5DD, UK.
Clark S; Departments of Mathematics and Biology, University of York, York YO10 5DD, UK.
Scott AJP; Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
Patel N; Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
Leibundgut M; Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.
Wroblewski E; Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
Ban N; Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.
Stockley PG; Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
Twarock R; Departments of Mathematics and Biology, University of York, York YO10 5DD, UK.
Hilvert D; Laboratory of Organic Chemistry, ETH Zurich, 8093 Zurich, Switzerland. .
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Źródło:
Science (New York, N.Y.) [Science] 2021 Jun 11; Vol. 372 (6547), pp. 1220-1224.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms:
Directed Molecular Evolution*
Bacterial Proteins/*genetics
Bacterial Proteins/*metabolism
Capsid/*metabolism
RNA, Messenger/*metabolism
Amino Acid Substitution ; Aquifex/enzymology ; Bacterial Proteins/chemistry ; Capsid/chemistry ; Cryoelectron Microscopy ; Multienzyme Complexes/chemistry ; Multienzyme Complexes/genetics ; Multienzyme Complexes/metabolism ; Nucleocapsid/chemistry ; Nucleocapsid/genetics ; Nucleocapsid/metabolism ; Protein Domains ; Protein Structure, Secondary ; Protein Subunits ; RNA, Messenger/chemistry ; RNA, Messenger/genetics ; Ribonucleases/metabolism
SCR Organism:
Aquifex aeolicus
Czasopismo naukowe
Tytuł:
Stability Enhancement of a Dimeric HER2-Specific Affibody Molecule through Sortase A-Catalyzed Head-to-Tail Cyclization.
Autorzy:
Westerlund K; Department of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, AlbaNova University Center, SE-10691 Stockholm, Sweden.
Myrhammar A; Department of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, AlbaNova University Center, SE-10691 Stockholm, Sweden.
Tano H; Department of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, AlbaNova University Center, SE-10691 Stockholm, Sweden.
Gestin M; Department of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, AlbaNova University Center, SE-10691 Stockholm, Sweden.
Karlström AE; Department of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, AlbaNova University Center, SE-10691 Stockholm, Sweden.
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Źródło:
Molecules (Basel, Switzerland) [Molecules] 2021 May 12; Vol. 26 (10). Date of Electronic Publication: 2021 May 12.
Typ publikacji:
Journal Article
MeSH Terms:
Biocatalysis*
Protein Multimerization*
Aminoacyltransferases/*metabolism
Bacterial Proteins/*metabolism
Breast Neoplasms/*metabolism
Cysteine Endopeptidases/*metabolism
Receptor, ErbB-2/*metabolism
Recombinant Fusion Proteins/*chemistry
Recombinant Fusion Proteins/*metabolism
Breast Neoplasms/pathology ; Circular Dichroism ; Cyclization ; Female ; Humans ; Kinetics ; MCF-7 Cells ; Microscopy, Fluorescence ; Peptide Hydrolases/metabolism ; Protein Binding ; Protein Structure, Secondary ; Surface Plasmon Resonance
Czasopismo naukowe
Tytuł:
The structure of MgtE in the absence of magnesium provides new insights into channel gating.
Autorzy:
Jin F; State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Shanghai Key Laboratory of Bioactive Small Molecules, Department of Physiology and Biophysics, School of Life Sciences, Fudan University, Shanghai, China.
Sun M; State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Shanghai Key Laboratory of Bioactive Small Molecules, Department of Physiology and Biophysics, School of Life Sciences, Fudan University, Shanghai, China.
Fujii T; Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan.; Riken Quantitative Biology Center, Osaka, Japan.
Yamada Y; Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan.
Wang J; School of Basic Medicine and Clinical Pharmacy, China Pharmaceutical University, Nanjing, China.
Maturana AD; Department of Bioengineering Sciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
Wada M; Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Chiba, Japan.
Su S; State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Multiscale Research Institute for Complex Systems, Department of Biochemistry, School of Life Sciences, Fudan University, Shanghai, China.
Ma J; State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Multiscale Research Institute for Complex Systems, Department of Biochemistry, School of Life Sciences, Fudan University, Shanghai, China.
Takeda H; Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.
Kusakizako T; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Tomita A; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Nakada-Nakura Y; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Liu K; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Uemura T; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Nomura Y; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Nomura N; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Ito K; Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Chiba, Japan.
Nureki O; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Namba K; Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan.; Riken Quantitative Biology Center, Osaka, Japan.
Iwata S; Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.; RIKEN SPring-8 Center, Kouto, Hyogo, Japan.
Yu Y; School of Basic Medicine and Clinical Pharmacy, China Pharmaceutical University, Nanjing, China.
Hattori M; State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Shanghai Key Laboratory of Bioactive Small Molecules, Department of Physiology and Biophysics, School of Life Sciences, Fudan University, Shanghai, China.
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Źródło:
PLoS biology [PLoS Biol] 2021 Apr 27; Vol. 19 (4), pp. e3001231. Date of Electronic Publication: 2021 Apr 27 (Print Publication: 2021).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Antiporters/*chemistry
Bacterial Proteins/*chemistry
Ion Channel Gating/*physiology
Antiporters/metabolism ; Bacterial Proteins/metabolism ; Binding Sites/drug effects ; Biological Transport ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Cytoplasm/metabolism ; Ion Channel Gating/drug effects ; Kinetics ; Magnesium/metabolism ; Magnesium/pharmacology ; Models, Molecular ; Protein Domains/drug effects ; Protein Domains/physiology ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Thermus thermophilus/metabolism
Czasopismo naukowe
Tytuł:
The Importance of Therapeutically Targeting the Binary Toxin from Clostridioides difficile .
Autorzy:
Abeyawardhane DL; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.; Baltimore-Institute for Bioscience and Biotechnology Research, University of Maryland-Institute for Bioscience and Biotechnology Research, Rockville, MD 20850, USA.; The Center for Biomolecular Therapeutics, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Godoy-Ruiz R; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.; Baltimore-Institute for Bioscience and Biotechnology Research, University of Maryland-Institute for Bioscience and Biotechnology Research, Rockville, MD 20850, USA.; The Center for Biomolecular Therapeutics, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Adipietro KA; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.; The Center for Biomolecular Therapeutics, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Varney KM; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.; Baltimore-Institute for Bioscience and Biotechnology Research, University of Maryland-Institute for Bioscience and Biotechnology Research, Rockville, MD 20850, USA.; The Center for Biomolecular Therapeutics, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Rustandi RR; Merck & Co., Inc., Kenilworth, NJ 07033, USA.
Pozharski E; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.; Baltimore-Institute for Bioscience and Biotechnology Research, University of Maryland-Institute for Bioscience and Biotechnology Research, Rockville, MD 20850, USA.; The Center for Biomolecular Therapeutics, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Weber DJ; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.; Baltimore-Institute for Bioscience and Biotechnology Research, University of Maryland-Institute for Bioscience and Biotechnology Research, Rockville, MD 20850, USA.; The Center for Biomolecular Therapeutics, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Mar 13; Vol. 22 (6). Date of Electronic Publication: 2021 Mar 13.
Typ publikacji:
Journal Article; Review
MeSH Terms:
Bacterial Proteins/*antagonists & inhibitors
Bacterial Toxins/*antagonists & inhibitors
Clostridioides difficile/*pathogenicity
Cross Infection/*drug therapy
Enterocolitis, Pseudomembranous/*drug therapy
Enterotoxins/*antagonists & inhibitors
ADP-Ribosylation/drug effects ; Actin Cytoskeleton/drug effects ; Actin Cytoskeleton/metabolism ; Actin Cytoskeleton/ultrastructure ; Actins/deficiency ; Actins/genetics ; Anti-Bacterial Agents/therapeutic use ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Bacterial Toxins/chemistry ; Bacterial Toxins/genetics ; Bacterial Toxins/metabolism ; Binding Sites ; Clostridioides difficile/drug effects ; Clostridioides difficile/genetics ; Clostridioides difficile/metabolism ; Cross Infection/metabolism ; Cross Infection/microbiology ; Cross Infection/pathology ; Endocytosis/drug effects ; Enterocolitis, Pseudomembranous/metabolism ; Enterocolitis, Pseudomembranous/microbiology ; Enterocolitis, Pseudomembranous/pathology ; Enterotoxins/chemistry ; Enterotoxins/genetics ; Enterotoxins/metabolism ; Epithelial Cells/drug effects ; Epithelial Cells/metabolism ; Epithelial Cells/microbiology ; Epithelial Cells/ultrastructure ; Humans ; Models, Molecular ; Protein Binding ; Protein Domains ; Protein Interaction Domains and Motifs ; Protein Structure, Secondary
Czasopismo naukowe
Tytuł:
New genotypes of Helicobacter Pylori VacA d-region identified from global strains.
Autorzy:
Soyfoo DM; Department of Gastroenterology, The First Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Doomah YH; Department of Obstetrics and Gynecology, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Xu D; Department of Electrical Engineering and Computer Science, Bond Life Sciences Center, University of Missouri, Columbia, MO, USA.
Zhang C; Institute for Computational Biomedicine, Weill Cornell Medicine, New York, NY, 10021, USA.; Division of Hematology and Medical Oncology, Department of Medicine, Weill Cornell Medicine, New York, NY, 10021, USA.
Sang HM; Department of Gastroenterology, The First Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Liu YY; Department of Gastroenterology, The First Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Zhang GX; Department of Gastroenterology, The First Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Jiang JX; Department of Gastroenterology, The First Affiliated Hospital of Nanjing Medical University, Nanjing, China. .
Xu SF; Department of Gastroenterology, The First Affiliated Hospital of Nanjing Medical University, Nanjing, China. .
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Źródło:
BMC molecular and cell biology [BMC Mol Cell Biol] 2021 Jan 07; Vol. 22 (1), pp. 4. Date of Electronic Publication: 2021 Jan 07.
Typ publikacji:
Journal Article
MeSH Terms:
Bacterial Proteins/*genetics
Helicobacter pylori/*genetics
Amino Acid Motifs ; Amino Acid Sequence ; Bacterial Proteins/chemistry ; Genotype ; Humans ; Prevalence ; Protein Structure, Secondary ; Solvents ; Stomach Neoplasms/epidemiology ; Stomach Neoplasms/microbiology
Czasopismo naukowe
Tytuł:
A Monoclonal Antibody against the C-Terminal Domain of Bacillus cereus Hemolysin II Inhibits HlyII Cytolytic Activity.
Autorzy:
Rudenko N; Pushchino Branch, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
Nagel A; FSBIS FRC Pushchino Scientific Centre of Biological Research, G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 5 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
Zamyatina A; Pushchino Branch, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.; Pushchino State Institute of Natural Sciences, 3 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
Karatovskaya A; Pushchino Branch, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
Salyamov V; FSBIS FRC Pushchino Scientific Centre of Biological Research, G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 5 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
Andreeva-Kovalevskaya Z; FSBIS FRC Pushchino Scientific Centre of Biological Research, G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 5 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
Siunov A; FSBIS FRC Pushchino Scientific Centre of Biological Research, G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 5 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
Kolesnikov A; FSBIS FRC Pushchino Scientific Centre of Biological Research, G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 5 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
Shepelyakovskaya A; Pushchino Branch, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
Boziev K; Pushchino Branch, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
Melnik B; Protein Institute of the Russian Academy of Sciences, 4 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
Brovko F; Pushchino Branch, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
Solonin A; FSBIS FRC Pushchino Scientific Centre of Biological Research, G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 5 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia.
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Źródło:
Toxins [Toxins (Basel)] 2020 Dec 19; Vol. 12 (12). Date of Electronic Publication: 2020 Dec 19.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Antibodies, Monoclonal/*pharmacology
Bacillus cereus/*drug effects
Bacterial Proteins/*antagonists & inhibitors
Erythrocytes/*drug effects
Hemolysin Proteins/*antagonists & inhibitors
Hemolysis/*drug effects
Animals ; Antibodies, Monoclonal/chemistry ; Bacillus cereus/chemistry ; Bacillus cereus/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Erythrocytes/metabolism ; Female ; Hemolysin Proteins/chemistry ; Hemolysin Proteins/metabolism ; Hemolysis/physiology ; Mice ; Mice, Inbred BALB C ; Protein Domains/drug effects ; Protein Domains/physiology ; Protein Structure, Secondary ; Rabbits
Czasopismo naukowe
Tytuł:
Specificity of Interactions between Components of Two Zinc ABC Transporters in Paracoccus denitrificans .
Autorzy:
Meléndez AB; Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, NM 88003, USA.
Valencia D; Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, NM 88003, USA.
Yukl ET; Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, NM 88003, USA.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2020 Nov 30; Vol. 21 (23). Date of Electronic Publication: 2020 Nov 30.
Typ publikacji:
Journal Article
MeSH Terms:
ATP-Binding Cassette Transporters/*metabolism
Bacterial Proteins/*metabolism
Paracoccus denitrificans/*metabolism
Zinc/*metabolism
ATP-Binding Cassette Transporters/chemistry ; Bacterial Proteins/chemistry ; Biological Transport ; Protein Binding ; Protein Structure, Secondary
Czasopismo naukowe
Tytuł:
Comparative Analysis of Aggregation of Thermus thermophilus Ribosomal Protein bS1 and Its Stable Fragment.
Autorzy:
Grishin SY; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
Dzhus UF; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
Selivanova OM; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
Balobanov VA; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
Surin AK; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia. .; State Research Center for Applied Microbiology and Biotechnology, Obolensk, Moscow Region, 142279, Russia.; Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
Galzitskaya OV; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia. .; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
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Źródło:
Biochemistry. Biokhimiia [Biochemistry (Mosc)] 2020 Mar; Vol. 85 (3), pp. 344-354.
Typ publikacji:
Comparative Study; Journal Article
MeSH Terms:
Bacterial Proteins/*metabolism
Ribosomal Proteins/*metabolism
Thermus thermophilus/*metabolism
Circular Dichroism ; Ions ; Light ; Mass Spectrometry ; Protein Binding ; Protein Domains ; Protein Structure, Secondary ; Proteolysis ; RNA, Bacterial/metabolism ; RNA, Messenger/metabolism ; Scattering, Radiation ; Spectrometry, Fluorescence ; Temperature
Czasopismo naukowe
Tytuł:
How Quickly Do Proteins Fold and Unfold, and What Structural Parameters Correlate with These Values?
Autorzy:
Glyakina AV; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russia.; Institute of Mathematical Problems of Biology, Russian Academy of Sciences, Keldysh Institute of Applied Mathematics, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russia.
Galzitskaya OV; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russia.; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russia.
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Źródło:
Biomolecules [Biomolecules] 2020 Jan 29; Vol. 10 (2). Date of Electronic Publication: 2020 Jan 29.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Protein Folding*
Protein Unfolding*
Bacterial Proteins/*chemistry
Algorithms ; Computational Biology ; Databases, Protein ; Kinetics ; Protein Denaturation ; Protein Stability ; Protein Structure, Secondary ; Thermodynamics
Czasopismo naukowe
Tytuł:
Structural basis for the recognition of MucA by MucB and AlgU in Pseudomonas aeruginosa.
Autorzy:
Li S; State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China.; College of Life Sciences, Nankai University, Tianjin, China.
Lou X; State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China.; College of Life Sciences, Nankai University, Tianjin, China.
Xu Y; College of Life Sciences, Nankai University, Tianjin, China.
Teng X; State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China.; College of Life Sciences, Nankai University, Tianjin, China.
Liu R; State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China.; College of Life Sciences, Nankai University, Tianjin, China.
Zhang Q; State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China.; College of Life Sciences, Nankai University, Tianjin, China.
Wu W; State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China.; College of Life Sciences, Nankai University, Tianjin, China.
Wang Y; College of Environmental Science & Engineering, Nankai University, Tianjin, China.
Bartlam M; State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China.; College of Life Sciences, Nankai University, Tianjin, China.
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Źródło:
The FEBS journal [FEBS J] 2019 Dec; Vol. 286 (24), pp. 4982-4994. Date of Electronic Publication: 2019 Jul 19.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Bacterial Proteins/*chemistry
Bacterial Proteins/*metabolism
Pseudomonas aeruginosa/*metabolism
Sigma Factor/*chemistry
Sigma Factor/*metabolism
Bacterial Proteins/genetics ; Crystallography, X-Ray ; Gene Expression Regulation, Bacterial/genetics ; Mutation/genetics ; Protein Structure, Secondary ; Pseudomonas aeruginosa/genetics ; Sigma Factor/genetics
Czasopismo naukowe
Tytuł:
Regulation of Streptococcus pneumoniae FtsZ assembly by divalent cations: paradoxical effects of Ca on the nucleation and bundling of FtsZ polymers.
Autorzy:
Dhaked HPS; Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, India.
Ray S; Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, India.; Department of Biotechnology, Mahatma Gandhi Central University, Motihari, Bihar, India.
Battaje RR; Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, India.
Banerjee A; Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, India.
Panda D; Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, India.
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Źródło:
The FEBS journal [FEBS J] 2019 Sep; Vol. 286 (18), pp. 3629-3646. Date of Electronic Publication: 2019 Jun 06.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Bacterial Proteins/*genetics
Cations, Divalent/*metabolism
Cytoskeletal Proteins/*genetics
Pneumococcal Infections/*genetics
Streptococcus pneumoniae/*genetics
Bacterial Proteins/chemistry ; Bacterial Proteins/ultrastructure ; Calcium/metabolism ; Calcium Signaling/genetics ; Cytoskeletal Proteins/chemistry ; Cytoskeletal Proteins/ultrastructure ; Gene Expression Regulation, Bacterial ; Humans ; Microscopy, Electron ; Pneumococcal Infections/microbiology ; Protein Binding/genetics ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Streptococcus pneumoniae/metabolism ; Streptococcus pneumoniae/ultrastructure
Czasopismo naukowe
Tytuł:
The complex structure of bile salt hydrolase from Lactobacillus salivarius reveals the structural basis of substrate specificity.
Autorzy:
Xu F; Department of Animal Science, The University of Tennessee, Knoxville, TN, 37996, USA.; Institute of Animal Science and Veterinary Medicine, Beijing Academy of Agriculture and Forestry Sciences, Beijing, China.
Hu XJ; State Key Laboratory of Genetic Engineering, School of Life Sciences, Collaborative Innovative Centre of Genetics and Development, Fudan University, Shanghai, 200438, China. .
Singh W; Molecular Therapeutics, School of Pharmacy, Medical Biology Centre, Queen's University Belfast, BT9 7BL, Northern Ireland, United Kingdom.
Geng W; Department of Animal Science, The University of Tennessee, Knoxville, TN, 37996, USA.
Tikhonova IG; Molecular Therapeutics, School of Pharmacy, Medical Biology Centre, Queen's University Belfast, BT9 7BL, Northern Ireland, United Kingdom. .
Lin J; Department of Animal Science, The University of Tennessee, Knoxville, TN, 37996, USA. .
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Źródło:
Scientific reports [Sci Rep] 2019 Aug 27; Vol. 9 (1), pp. 12438. Date of Electronic Publication: 2019 Aug 27.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms:
Molecular Dynamics Simulation*
Amidohydrolases/*chemistry
Bacterial Proteins/*chemistry
Ligilactobacillus salivarius/*enzymology
Protein Domains ; Protein Structure, Secondary ; Substrate Specificity
Czasopismo naukowe
Tytuł:
Structural characterization of Treponema pallidum Tp0225 reveals an unexpected leucine-rich repeat architecture.
Autorzy:
Ramaswamy R; Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8P 5C2, Canada.
Houston S; Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8P 5C2, Canada.
Loveless B; Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8P 5C2, Canada.
Cameron CE; Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8P 5C2, Canada.
Boulanger MJ; Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8P 5C2, Canada.
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Źródło:
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2019 Jul 01; Vol. 75 (Pt 7), pp. 489-495. Date of Electronic Publication: 2019 Jun 26.
Typ publikacji:
Journal Article
MeSH Terms:
Bacterial Proteins/*chemistry
Proteins/*chemistry
Treponema pallidum/*metabolism
Binding Sites ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Leucine-Rich Repeat Proteins ; Phylogeny ; Protein Domains ; Protein Structure, Secondary
Czasopismo naukowe
Tytuł:
Structural insights into the substrate specificity of SP_0149, the substrate-binding protein of a methionine ABC transporter from Streptococcus pneumoniae.
Autorzy:
Jha B; Structural and Functional Biology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110 067, India.
Vyas R; Structural and Functional Biology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110 067, India.
Bhushan J; Molecular Immunology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110 067, India.
Sehgal D; Molecular Immunology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110 067, India.
Biswal BK; Structural and Functional Biology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110 067, India.
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Źródło:
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2019 Jul 01; Vol. 75 (Pt 7), pp. 520-528. Date of Electronic Publication: 2019 Jul 04.
Typ publikacji:
Journal Article
MeSH Terms:
ATP-Binding Cassette Transporters/*chemistry
ATP-Binding Cassette Transporters/*metabolism
Bacterial Proteins/*chemistry
Bacterial Proteins/*metabolism
Methionine/*metabolism
Streptococcus pneumoniae/*metabolism
Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Models, Molecular ; Protein Structure, Secondary ; Structural Homology, Protein ; Substrate Specificity
Czasopismo naukowe

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