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Tytuł :
Effects of CcpA against salt stress in Lactiplantibacillus plantarum as assessed by comparative transcriptional analysis.
Autorzy :
Chen C; School of Perfume and Aroma Technology, Shanghai Institute of Technology, Shanghai, People's Republic of China.
Huang K; School of Perfume and Aroma Technology, Shanghai Institute of Technology, Shanghai, People's Republic of China.
Li X; Shanghai Customs P. R. China Technical Center For Animal, Plant And Food Inspection And Quarantine, Shanghai, People's Republic of China.
Tian H; School of Perfume and Aroma Technology, Shanghai Institute of Technology, Shanghai, People's Republic of China.
Yu H; School of Perfume and Aroma Technology, Shanghai Institute of Technology, Shanghai, People's Republic of China.
Huang J; School of Perfume and Aroma Technology, Shanghai Institute of Technology, Shanghai, People's Republic of China.
Yuan H; School of Perfume and Aroma Technology, Shanghai Institute of Technology, Shanghai, People's Republic of China.
Zhao S; College of Agriculture, Hebei University of Engineering, Handan, People's Republic of China.
Shao L; School of Perfume and Aroma Technology, Shanghai Institute of Technology, Shanghai, People's Republic of China. .
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Źródło :
Applied microbiology and biotechnology [Appl Microbiol Biotechnol] 2021 May; Vol. 105 (9), pp. 3691-3704. Date of Electronic Publication: 2021 Apr 14.
Typ publikacji :
Journal Article
MeSH Terms :
Bacterial Proteins*/genetics
Bacterial Proteins*/metabolism
Repressor Proteins*/genetics
DNA-Binding Proteins/genetics ; Gene Expression Regulation, Bacterial ; Salt Stress
Czasopismo naukowe
Tytuł :
Influences of acid and ethanol stresses on Oenococcus oeni SD-2a and its proteomic and transcriptional responses.
Autorzy :
Yang K; College of Biological and Chemical Engineering, Anhui Polytechnic University, Wuhu, China.; College of Food Science and Engineering, Northwest A & F University, Yangling, China.; College of Life Sciences, China Jiliang University, Hangzhou, China.
Dai X; College of Life Sciences, China Jiliang University, Hangzhou, China.
Fan M; College of Food Science and Engineering, Northwest A & F University, Yangling, China.
Zhang G; College of Biological and Chemical Engineering, Anhui Polytechnic University, Wuhu, China.
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Źródło :
Journal of the science of food and agriculture [J Sci Food Agric] 2021 May; Vol. 101 (7), pp. 2892-2900. Date of Electronic Publication: 2020 Dec 01.
Typ publikacji :
Journal Article
MeSH Terms :
Transcription, Genetic*
Acids/*metabolism
Bacterial Proteins/*genetics
Ethanol/*metabolism
Oenococcus/*physiology
Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Fermentation ; Glutathione/metabolism ; Oenococcus/chemistry ; Oenococcus/genetics ; Proteomics ; Stress, Physiological ; Wine/analysis ; Wine/microbiology
SCR Organism :
Oenococcus oeni
Czasopismo naukowe
Tytuł :
Comparative proteomic analysis of outer membrane vesicles from Brucella suis, Brucella ovis, Brucella canis and Brucella neotomae.
Autorzy :
Socorro Ruiz-Palma MD; Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas (ENCB), Instituto Politécnico Nacional (IPN), Prol. Carpio y Plan de Ayala s/n, Col. Sto. Tomás, CP 11340, Mexico City, Mexico.; División Químico Biológicas, Universidad Tecnológica de Tecámac, Km. 37.5 Carretera Federal México-Pachuca, Predio Sierra Hermosa, CP 55740, Tecámac, Estado de México, Mexico.
Avila-Calderón ED; Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas (ENCB), Instituto Politécnico Nacional (IPN), Prol. Carpio y Plan de Ayala s/n, Col. Sto. Tomás, CP 11340, Mexico City, Mexico.; Departamento de Biología Celular, Centro de Investigación y de Estudios Avanzados, Instituto Politécnico Nacional, CINVESTAV-IPN, Avenida Instituto Politécnico Nacional 2508, Col. San Pedro Zacatenco, CP 07360, Mexico City, Mexico.
Aguilera-Arreola MG; Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas (ENCB), Instituto Politécnico Nacional (IPN), Prol. Carpio y Plan de Ayala s/n, Col. Sto. Tomás, CP 11340, Mexico City, Mexico.
López-Merino A; Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas (ENCB), Instituto Politécnico Nacional (IPN), Prol. Carpio y Plan de Ayala s/n, Col. Sto. Tomás, CP 11340, Mexico City, Mexico.
Ruiz EA; Departamento de Zoología, Escuela Nacional de Ciencias Biológicas (ENCB), Instituto Politécnico Nacional (IPN), México City, Mexico.
Morales-García MDR; Departamento de Investigación, CICATA Querétaro, Instituto Politécnico Nacional (IPN), Querétaro, Mexico.
López-Villegas EO; Departamento de Investigación, Central de Microscopía, Escuela Nacional de Ciencias Biológicas (ENCB), Instituto Politécnico Nacional (IPN), Prol. Carpio y Plan de Ayala S/N, Col. Sto. Tomás, CP 11340, Mexico City, Mexico.
Gomez-Lunar Z; Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas (ENCB), Instituto Politécnico Nacional (IPN), Prol. Carpio y Plan de Ayala s/n, Col. Sto. Tomás, CP 11340, Mexico City, Mexico.
Arellano-Reynoso B; Departamento de Microbiología e Inmunología, Facultad de Medicina Veterinaria y Zootecnia, Universidad Nacional Autónoma de México (UNAM), Coyoacán, 04510, Mexico City, Mexico.
Contreras-Rodríguez A; Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas (ENCB), Instituto Politécnico Nacional (IPN), Prol. Carpio y Plan de Ayala s/n, Col. Sto. Tomás, CP 11340, Mexico City, Mexico. .
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Źródło :
Archives of microbiology [Arch Microbiol] 2021 May; Vol. 203 (4), pp. 1611-1626. Date of Electronic Publication: 2021 Jan 11.
Typ publikacji :
Comparative Study; Journal Article
MeSH Terms :
Antigens, Bacterial*/genetics
Antigens, Bacterial*/metabolism
Bacterial Proteins*/genetics
Bacterial Proteins*/metabolism
Brucella*/genetics
Brucella*/metabolism
Proteome*/genetics
Animals ; Brucella canis ; Brucella ovis ; Brucella suis ; Electrophoresis, Polyacrylamide Gel ; Proteomics
SCR Organism :
Brucella neotomae
Czasopismo naukowe
Tytuł :
FtsZ treadmilling is essential for Z-ring condensation and septal constriction initiation in Bacillus subtilis cell division.
Autorzy :
Whitley KD; Centre for Bacterial Cell Biology, Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, NE2 4AX, UK.; Department of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Van Der Maasweg 9, Delft, 2629 HZ, The Netherlands.
Jukes C; Centre for Bacterial Cell Biology, Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, NE2 4AX, UK.
Tregidgo N; Centre for Bacterial Cell Biology, Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, NE2 4AX, UK.
Karinou E; Centre for Bacterial Cell Biology, Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, NE2 4AX, UK.
Almada P; MRC Laboratory for Molecular Cell Biology, University College London, London, WC1E 6BT, UK.
Cesbron Y; Centre for Bacterial Cell Biology, Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, NE2 4AX, UK.
Henriques R; MRC Laboratory for Molecular Cell Biology, University College London, London, WC1E 6BT, UK.; Instituto Gulbenkian de Ciência, Oeiras, 2780-156, Portugal.
Dekker C; Department of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Van Der Maasweg 9, Delft, 2629 HZ, The Netherlands.
Holden S; Centre for Bacterial Cell Biology, Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, NE2 4AX, UK. .
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Źródło :
Nature communications [Nat Commun] 2021 Apr 27; Vol. 12 (1), pp. 2448. Date of Electronic Publication: 2021 Apr 27.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Bacillus subtilis/*metabolism
Bacterial Proteins/*metabolism
Cell Wall/*metabolism
Cytoskeletal Proteins/*metabolism
Guanosine Triphosphate/*metabolism
Bacillus subtilis/genetics ; Bacillus subtilis/growth & development ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Cell Division ; Cell Wall/ultrastructure ; Cytoskeletal Proteins/chemistry ; Cytoskeletal Proteins/genetics ; Gene Expression ; Hydrolysis ; Microfluidic Analytical Techniques ; Models, Biological ; Protein Transport
Czasopismo naukowe
Tytuł :
Structure of the far-red light utilizing photosystem I of Acaryochloris marina.
Autorzy :
Hamaguchi T; Biostructural Mechanism Laboratory, RIKEN SPring-8 Center, Sayo, Hyogo, Japan.
Kawakami K; Research Center for Artificial Photosynthesis (ReCAP), Osaka City University, Sumiyoshi-ku, Osaka, Japan. .; Biostructural Mechanism Laboratory, RIKEN SPring-8 Center, Sayo, Hyogo, Japan. .
Shinzawa-Itoh K; Graduate School of Life Science, University of Hyogo, Ako-gun, Hyogo, Japan.
Inoue-Kashino N; Graduate School of Life Science, University of Hyogo, Ako-gun, Hyogo, Japan.
Itoh S; Department of Physics, Graduate School of Science, Nagoya University, Nagoya, Japan.
Ifuku K; Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto, Japan.
Yamashita E; Laboratory of Supramolecular Crystallography, Institute for Protein Research, Osaka University, Suita, Osaka, Japan.
Maeda K; Graduate School of Life Science, University of Hyogo, Ako-gun, Hyogo, Japan.
Yonekura K; Biostructural Mechanism Laboratory, RIKEN SPring-8 Center, Sayo, Hyogo, Japan. .; Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Aoba-ku, Sendai, Japan. .
Kashino Y; Graduate School of Life Science, University of Hyogo, Ako-gun, Hyogo, Japan. .
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Źródło :
Nature communications [Nat Commun] 2021 Apr 20; Vol. 12 (1), pp. 2333. Date of Electronic Publication: 2021 Apr 20.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Bacterial Proteins/*chemistry
Cyanobacteria/*chemistry
Photosystem I Protein Complex/*chemistry
Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Chlorophyll/chemistry ; Chlorophyll/metabolism ; Cryoelectron Microscopy ; Cyanobacteria/genetics ; Cyanobacteria/metabolism ; Electron Transport ; Light ; Models, Molecular ; Oxygen/metabolism ; Photosynthesis ; Photosystem I Protein Complex/genetics ; Photosystem I Protein Complex/metabolism ; Protein Structure, Quaternary ; Protein Subunits ; Static Electricity
SCR Organism :
Acaryochloris marina
Czasopismo naukowe
Tytuł :
Structural and functional studies of SF1B Pif1 from Thermus oshimai reveal dimerization-induced helicase inhibition.
Autorzy :
Dai YX; State Key Laboratory of Crop Stress Biology for Arid Areas and College of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, China.
Chen WF; State Key Laboratory of Crop Stress Biology for Arid Areas and College of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, China.
Liu NN; State Key Laboratory of Crop Stress Biology for Arid Areas and College of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, China.
Teng FY; State Key Laboratory of Crop Stress Biology for Arid Areas and College of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, China.
Guo HL; State Key Laboratory of Crop Stress Biology for Arid Areas and College of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, China.
Hou XM; State Key Laboratory of Crop Stress Biology for Arid Areas and College of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, China.
Dou SX; Beijing National Laboratory for Condensed Matter Physics and CAS Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.; School of Physical Sciences, University of Chinese Academy of Sciences, Beijing 100049, China.
Rety S; Univ. Lyon, ENS de Lyon, Univ. Claude Bernard CNRS UMR 5239, INSERM U1210, LBMC, 46 allée d'Italie Site Jacques Monod, F-69007, Lyon, France.
Xi XG; State Key Laboratory of Crop Stress Biology for Arid Areas and College of Life Sciences, Northwest A&F University, Yangling, Shaanxi 712100, China.; Laboratoire de Biologie et de Pharmacologie Appliquée (LBPA), UMR 8113 CNRS, Institut D'Alembert, École Normale Supérieure Paris-Saclay, Université Paris-Saclay, 4, Avenue des Sciences, 91190 Gif sur Yvette, France.
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Źródło :
Nucleic acids research [Nucleic Acids Res] 2021 Apr 19; Vol. 49 (7), pp. 4129-4143.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Bacterial Proteins*/chemistry
Bacterial Proteins*/metabolism
DNA Helicases*/chemistry
DNA Helicases*/metabolism
DNA, Single-Stranded/*metabolism
Thermus/*enzymology
Models, Molecular ; Molecular Structure ; Protein Binding ; Protein Conformation ; Protein Multimerization
SCR Organism :
Thermus oshimai
Czasopismo naukowe
Tytuł :
Structures of Neisseria gonorrhoeae MtrR-operator complexes reveal molecular mechanisms of DNA recognition and antibiotic resistance-conferring clinical mutations.
Autorzy :
Beggs GA; Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.
Ayala JC; Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322, USA.
Kavanaugh LG; Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322, USA.
Read TD; Department of Medicine, and the Emory Antibiotic Resistance Center, Emory University School of Medicine, Atlanta, GA 30322, USA.; Emory Antibiotic Resistance Center, Emory University School of Medicine, Atlanta, GA 30322, USA.
Hooks GM; Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.
Schumacher MA; Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.
Shafer WM; Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322, USA.; Emory Antibiotic Resistance Center, Emory University School of Medicine, Atlanta, GA 30322, USA.; Laboratories of Bacterial Pathogenesis, VA Medical Center, Decatur, GA 30033, USA.
Brennan RG; Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.
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Źródło :
Nucleic acids research [Nucleic Acids Res] 2021 Apr 19; Vol. 49 (7), pp. 4155-4170.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Bacterial Proteins*/genetics
Bacterial Proteins*/metabolism
Neisseria gonorrhoeae*/genetics
Neisseria gonorrhoeae*/metabolism
Repressor Proteins*/genetics
Repressor Proteins*/metabolism
DNA, Bacterial/*metabolism
Drug Resistance, Multiple, Bacterial/*genetics
Binding Sites ; Gene Expression Regulation, Bacterial ; Mutation ; Protein Binding
Czasopismo naukowe
Tytuł :
Fur-like proteins: Beyond the ferric uptake regulator (Fur) paralog.
Autorzy :
Sevilla E; Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Instituto de Biocomputación y Física de Sistemas Complejos (GBsC-CSIC and BIFI-IQFR Joint Units), Universidad de Zaragoza, Zaragoza, Spain.
Bes MT; Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Instituto de Biocomputación y Física de Sistemas Complejos (GBsC-CSIC and BIFI-IQFR Joint Units), Universidad de Zaragoza, Zaragoza, Spain.
Peleato ML; Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Instituto de Biocomputación y Física de Sistemas Complejos (GBsC-CSIC and BIFI-IQFR Joint Units), Universidad de Zaragoza, Zaragoza, Spain.
Fillat MF; Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Instituto de Biocomputación y Física de Sistemas Complejos (GBsC-CSIC and BIFI-IQFR Joint Units), Universidad de Zaragoza, Zaragoza, Spain. Electronic address: .
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Źródło :
Archives of biochemistry and biophysics [Arch Biochem Biophys] 2021 Apr 15; Vol. 701, pp. 108770. Date of Electronic Publication: 2021 Jan 29.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't; Review
MeSH Terms :
Bacteria*/genetics
Bacteria*/metabolism
Bacteria*/pathogenicity
Bacterial Physiological Phenomena*
Bacterial Proteins*/genetics
Bacterial Proteins*/metabolism
Host-Pathogen Interactions*
Repressor Proteins*/genetics
Repressor Proteins*/metabolism
Iron/*metabolism
Humans
Czasopismo naukowe
Tytuł :
Isolation, Structure Elucidation and In Silico Prediction of Potential Drug-Like Flavonoids from Onosma chitralicum Targeted towards Functionally Important Proteins of Drug-Resistant Bad Bugs.
Autorzy :
Khan SA; Department of Chemistry, Kohat University of Science & Technology, Kohat 26000, Pakistan.
Khan SU; School of Pharmacy, Monash University, Bandar Sunway, Subang Jaya 47500, Malaysia.; Department of Pharmacy, Abasyn University, Ring Road, Peshawar 25120, Pakistan.
Fozia; Biochemistry Department, KMU Institute of Medical Sciences, Kohat 26000, Pakistan.
Ullah N; Department of Biochemistry, Bahauddin Zakariya University, Multan 60800, Pakistan.
Shah M; Department of Biochemistry, Bahauddin Zakariya University, Multan 60800, Pakistan.
Ullah R; Department of Pharmacognosy, College of Pharmacy, King Saud University Riyadh Saudi Arabia, Riyadh 11495, Saudi Arabia.
Ahmad I; Department of Chemistry, Kohat University of Science & Technology, Kohat 26000, Pakistan.
Alotaibi A; Basic Science Department, College of Medicine, Princess Nourah bint Abdulrahman University, Riyadh 11671, Saudi Arabia.
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Źródło :
Molecules (Basel, Switzerland) [Molecules] 2021 Apr 02; Vol. 26 (7). Date of Electronic Publication: 2021 Apr 02.
Typ publikacji :
Journal Article
MeSH Terms :
Computer Simulation*
Drug Resistance, Bacterial*/drug effects
Bacterial Proteins/*antagonists & inhibitors
Boraginaceae/*chemistry
Flavonoids/*chemistry
Flavonoids/*isolation & purification
Salmonella typhi/*drug effects
Staphylococcus aureus/*drug effects
Antifungal Agents/chemistry ; Antifungal Agents/pharmacology ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Binding Sites ; Drug Evaluation, Preclinical ; Flavonoids/pharmacology ; Microbial Sensitivity Tests ; Molecular Docking Simulation ; Salmonella typhi/metabolism ; Staphylococcus aureus/metabolism ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
Immunogenicity and protective ability of RpoE against Streptococcus suis serotype 2.
Autorzy :
Yi L; College of Life Science, Luoyang Normal University, Luoyang, China.; Key Laboratory of Molecular Pathogen and Immunology of Animal of Luoyang, Luoyang, China.
Du Y; Key Laboratory of Molecular Pathogen and Immunology of Animal of Luoyang, Luoyang, China.; College of Animal Science and Technology, Henan University of Science and Technology, Luoyang, China.
Mao C; Key Laboratory of Molecular Pathogen and Immunology of Animal of Luoyang, Luoyang, China.; College of Animal Science and Technology, Henan University of Science and Technology, Luoyang, China.
Li J; Key Laboratory of Molecular Pathogen and Immunology of Animal of Luoyang, Luoyang, China.; College of Animal Science and Technology, Henan University of Science and Technology, Luoyang, China.
Jin M; Key Laboratory of Molecular Pathogen and Immunology of Animal of Luoyang, Luoyang, China.; College of Animal Science and Technology, Henan University of Science and Technology, Luoyang, China.
Sun L; Key Laboratory of Molecular Pathogen and Immunology of Animal of Luoyang, Luoyang, China.; College of Animal Science and Technology, Henan University of Science and Technology, Luoyang, China.
Wang Y; Key Laboratory of Molecular Pathogen and Immunology of Animal of Luoyang, Luoyang, China.; College of Animal Science and Technology, Henan University of Science and Technology, Luoyang, China.
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Źródło :
Journal of applied microbiology [J Appl Microbiol] 2021 Apr; Vol. 130 (4), pp. 1075-1083. Date of Electronic Publication: 2020 Oct 14.
Typ publikacji :
Journal Article
MeSH Terms :
Bacterial Proteins/*immunology
Sigma Factor/*immunology
Streptococcal Infections/*prevention & control
Streptococcal Vaccines/*immunology
Streptococcus suis/*immunology
Animals ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Female ; Immunization ; Mice ; Recombinant Proteins/genetics ; Recombinant Proteins/immunology ; Recombinant Proteins/metabolism ; Serogroup ; Sigma Factor/genetics ; Sigma Factor/metabolism ; Streptococcal Infections/microbiology ; Streptococcal Vaccines/administration & dosage ; Streptococcus suis/genetics ; Vaccines, Subunit/administration & dosage ; Vaccines, Subunit/immunology
Czasopismo naukowe
Tytuł :
An Antifungal Chitosanase from Bacillus subtilis SH21.
Autorzy :
Pang Y; Key Laboratory of Agricultural Product Detection and Control of Spoilage Organisms and Pesticides, Beijing Laboratory for Food Quality and Safety, Beijing Engineering Laboratory of Probiotics Key Technology Development, Beijing Engineering Technology Research Center of Food Safety Immune Rapid Detection, Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China.
Yang J; Key Laboratory of Agricultural Product Detection and Control of Spoilage Organisms and Pesticides, Beijing Laboratory for Food Quality and Safety, Beijing Engineering Laboratory of Probiotics Key Technology Development, Beijing Engineering Technology Research Center of Food Safety Immune Rapid Detection, Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China.
Chen X; Key Laboratory of Agricultural Product Detection and Control of Spoilage Organisms and Pesticides, Beijing Laboratory for Food Quality and Safety, Beijing Engineering Laboratory of Probiotics Key Technology Development, Beijing Engineering Technology Research Center of Food Safety Immune Rapid Detection, Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China.
Jia Y; Key Laboratory of Agricultural Product Detection and Control of Spoilage Organisms and Pesticides, Beijing Laboratory for Food Quality and Safety, Beijing Engineering Laboratory of Probiotics Key Technology Development, Beijing Engineering Technology Research Center of Food Safety Immune Rapid Detection, Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China.
Li T; Key Laboratory of Agricultural Product Detection and Control of Spoilage Organisms and Pesticides, Beijing Laboratory for Food Quality and Safety, Beijing Engineering Laboratory of Probiotics Key Technology Development, Beijing Engineering Technology Research Center of Food Safety Immune Rapid Detection, Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China.
Jin J; Key Laboratory of Agricultural Product Detection and Control of Spoilage Organisms and Pesticides, Beijing Laboratory for Food Quality and Safety, Beijing Engineering Laboratory of Probiotics Key Technology Development, Beijing Engineering Technology Research Center of Food Safety Immune Rapid Detection, Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China.
Liu H; Key Laboratory of Agricultural Product Detection and Control of Spoilage Organisms and Pesticides, Beijing Laboratory for Food Quality and Safety, Beijing Engineering Laboratory of Probiotics Key Technology Development, Beijing Engineering Technology Research Center of Food Safety Immune Rapid Detection, Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China.
Jiang L; Key Laboratory of Agricultural Product Detection and Control of Spoilage Organisms and Pesticides, Beijing Laboratory for Food Quality and Safety, Beijing Engineering Laboratory of Probiotics Key Technology Development, Beijing Engineering Technology Research Center of Food Safety Immune Rapid Detection, Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China.
Hao Y; Key Laboratory of Functional Dairy Science of Beijing and Chinese Ministry of Education, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
Zhang H; Key Laboratory of Agricultural Product Detection and Control of Spoilage Organisms and Pesticides, Beijing Laboratory for Food Quality and Safety, Beijing Engineering Laboratory of Probiotics Key Technology Development, Beijing Engineering Technology Research Center of Food Safety Immune Rapid Detection, Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China.
Xie Y; Key Laboratory of Agricultural Product Detection and Control of Spoilage Organisms and Pesticides, Beijing Laboratory for Food Quality and Safety, Beijing Engineering Laboratory of Probiotics Key Technology Development, Beijing Engineering Technology Research Center of Food Safety Immune Rapid Detection, Food Science and Engineering College, Beijing University of Agriculture, Beijing 102206, China.
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Źródło :
Molecules (Basel, Switzerland) [Molecules] 2021 Mar 25; Vol. 26 (7). Date of Electronic Publication: 2021 Mar 25.
Typ publikacji :
Journal Article
MeSH Terms :
Antifungal Agents*/chemistry
Antifungal Agents*/isolation & purification
Antifungal Agents*/pharmacology
Bacterial Proteins*/chemistry
Bacterial Proteins*/isolation & purification
Bacterial Proteins*/pharmacology
Glycoside Hydrolases*/chemistry
Glycoside Hydrolases*/isolation & purification
Glycoside Hydrolases*/pharmacology
Bacillus subtilis/*enzymology
Fusarium/*growth & development
SCR Organism :
Fusarium solani
Czasopismo naukowe
Tytuł :
Molecular Basis for Bordetella pertussis Interference with Complement, Coagulation, Fibrinolytic, and Contact Activation Systems: the Cryo-EM Structure of the Vag8-C1 Inhibitor Complex.
Autorzy :
Dhillon A; Sir William Dunn School of Pathology, Oxford, United Kingdom.
Deme JC; Sir William Dunn School of Pathology, Oxford, United Kingdom.; Central Oxford Structural Molecular Imaging Centre, Oxford, United Kingdom.
Furlong E; Sir William Dunn School of Pathology, Oxford, United Kingdom.
Roem D; Sanquin Research, Department of Immunopathology, and Landsteiner Laboratory, Amsterdam University Medical Centre, Amsterdam Infection and Immunity Institute, Amsterdam, the Netherlands.
Jongerius I; Sanquin Research, Department of Immunopathology, and Landsteiner Laboratory, Amsterdam University Medical Centre, Amsterdam Infection and Immunity Institute, Amsterdam, the Netherlands.; Department of Pediatric Immunology, Rheumatology, and Infectious Diseases, Emma Children's Hospital, Amsterdam University Medical Centre, Amsterdam, the Netherlands.
Johnson S; Sir William Dunn School of Pathology, Oxford, United Kingdom .
Lea SM; Sir William Dunn School of Pathology, Oxford, United Kingdom .; Central Oxford Structural Molecular Imaging Centre, Oxford, United Kingdom.
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Źródło :
MBio [mBio] 2021 Mar 23; Vol. 12 (2). Date of Electronic Publication: 2021 Mar 23.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Immune Evasion*
Bacterial Proteins/*metabolism
Bordetella pertussis/*pathogenicity
Complement C1 Inhibitor Protein/*metabolism
Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Binding Sites ; Blood Coagulation ; Bordetella pertussis/chemistry ; Bordetella pertussis/metabolism ; Complement C1 Inhibitor Protein/chemistry ; Complement System Proteins/metabolism ; Cryoelectron Microscopy ; Fibrinolysis ; Models, Molecular ; Mutation ; Protein Binding ; Protein Domains ; Type V Secretion Systems/genetics ; Type V Secretion Systems/metabolism ; Virulence
Czasopismo naukowe
Tytuł :
Two Key Amino Acids Variant of α-l-arabinofuranosidase from Bacillus subtilis Str. 168 with Altered Activity for Selective Conversion Ginsenoside Rc to Rd.
Autorzy :
Zhang R; College of Materials and Chemical Engineering, Hunan Institute of Engineering, Xiangtan 411104, China.; Hunan International Joint Laboratory of Animal Intestinal Ecology and Health, Laboratory of Animal Nutrition and Human Health, College of Life Sciences, Hunan Normal University, Changsha 410081, China.
Tan SQ; College of Materials and Chemical Engineering, Hunan Institute of Engineering, Xiangtan 411104, China.
Zhang BL; College of Materials and Chemical Engineering, Hunan Institute of Engineering, Xiangtan 411104, China.
Guo ZY; College of Materials and Chemical Engineering, Hunan Institute of Engineering, Xiangtan 411104, China.
Tian LY; College of Materials and Chemical Engineering, Hunan Institute of Engineering, Xiangtan 411104, China.
Weng P; College of Materials and Chemical Engineering, Hunan Institute of Engineering, Xiangtan 411104, China.
Luo ZY; Molecular Biology Research Center, School of Life Sciences, Central South University, Changsha 410078, China.
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Źródło :
Molecules (Basel, Switzerland) [Molecules] 2021 Mar 19; Vol. 26 (6). Date of Electronic Publication: 2021 Mar 19.
Typ publikacji :
Journal Article
MeSH Terms :
Amino Acid Substitution*
Bacillus subtilis*/enzymology
Bacillus subtilis*/genetics
Bacterial Proteins*/chemistry
Bacterial Proteins*/genetics
Glycoside Hydrolases*/chemistry
Glycoside Hydrolases*/genetics
Mutagenesis, Site-Directed*
Ginsenosides/*chemistry
Mutation, Missense ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/genetics
Czasopismo naukowe
Tytuł :
Biochemical and structural analyses reveal critical residues in δ subunit affecting its bindings to β' subunit of Staphylococcus aureus RNA polymerase.
Autorzy :
Lin Z; Department of Microbiology and Immunology, School of Medicine & Holistic Integrative Medicine, Nanjing University of Chinese Medicine, Nanjing, China.
Wang F; Department of Microbiology and Immunology, School of Medicine & Holistic Integrative Medicine, Nanjing University of Chinese Medicine, Nanjing, China.
Shang Z; Department of Microbiology and Immunology, School of Medicine & Holistic Integrative Medicine, Nanjing University of Chinese Medicine, Nanjing, China; Jiangsu Collaborative Innovation Center of Chinese Medicinal Resources Industrialization, Nanjing, 210023, China. Electronic address: .
Lin W; Department of Microbiology and Immunology, School of Medicine & Holistic Integrative Medicine, Nanjing University of Chinese Medicine, Nanjing, China; State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing, China; Jiangsu Collaborative Innovation Center of Chinese Medicinal Resources Industrialization, Nanjing, 210023, China. Electronic address: .
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Źródło :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2021 Mar 19; Vol. 545, pp. 98-104. Date of Electronic Publication: 2021 Feb 03.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Bacterial Proteins/*chemistry
DNA-Directed RNA Polymerases/*chemistry
Staphylococcus aureus/*enzymology
Amino Acid Sequence ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; DNA-Directed RNA Polymerases/genetics ; DNA-Directed RNA Polymerases/metabolism ; Genes, Bacterial ; Humans ; Models, Molecular ; Mutagenesis, Site-Directed ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Subunits ; Sequence Homology, Amino Acid ; Staphylococcus aureus/genetics ; Transcription, Genetic
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 :
In Silico Investigation of Potential Applications of Gamma Carbonic Anhydrases as Catalysts of CO 2 Biomineralization Processes: A Visit to the Thermophilic Bacteria Persephonella hydrogeniphila, Persephonella marina, Thermosulfidibacter takaii, and Thermus thermophilus .
Autorzy :
Manyumwa CV; Research Unit in Bioinformatics (RUBi), Department of Biochemistry and Microbiology, Rhodes University, Makhanda 6140, South Africa.
Bishop ÖT; Research Unit in Bioinformatics (RUBi), Department of Biochemistry and Microbiology, Rhodes University, Makhanda 6140, South Africa.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Mar 11; Vol. 22 (6). Date of Electronic Publication: 2021 Mar 11.
Typ publikacji :
Journal Article
MeSH Terms :
Biomineralization*
Bacterial Proteins/*metabolism
Carbon Dioxide/*metabolism
Carbonic Anhydrases/*metabolism
Amino Acid Sequence ; Bacteria/enzymology ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Carbon Dioxide/chemistry ; Carbonic Anhydrases/chemistry ; Carbonic Anhydrases/genetics ; Catalysis ; Catalytic Domain ; Computer Simulation ; Hot Springs/microbiology ; Hydrothermal Vents/microbiology ; Molecular Dynamics Simulation ; Protein Conformation ; Sequence Homology, Amino Acid ; Temperature ; Thermus thermophilus/enzymology
SCR Organism :
Persephonella hydrogeniphila; Persephonella marina; Thermosulfidibacter takaii
Czasopismo naukowe
Tytuł :
Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation.
Autorzy :
Miletic S; University Medical Center Hamburg-Eppendorf (UKE), Institute of Structural and Systems Biology, Hamburg, Germany.; Centre for Structural Systems Biology (CSSB), Hamburg, Germany.; Deutsches Elektronen-Synchrotron Zentrum (DESY), Hamburg, Germany.; Institute of Molecular Biotechnology GmbH (IMBA), Austrian Academy of Sciences, Vienna, Austria.; Research Institute of Molecular Pathology (IMP), Vienna, Austria.
Fahrenkamp D; University Medical Center Hamburg-Eppendorf (UKE), Institute of Structural and Systems Biology, Hamburg, Germany.; Centre for Structural Systems Biology (CSSB), Hamburg, Germany.; Deutsches Elektronen-Synchrotron Zentrum (DESY), Hamburg, Germany.
Goessweiner-Mohr N; University Medical Center Hamburg-Eppendorf (UKE), Institute of Structural and Systems Biology, Hamburg, Germany.; Deutsches Elektronen-Synchrotron Zentrum (DESY), Hamburg, Germany.; Institute of Molecular Biotechnology GmbH (IMBA), Austrian Academy of Sciences, Vienna, Austria.; Research Institute of Molecular Pathology (IMP), Vienna, Austria.
Wald J; University Medical Center Hamburg-Eppendorf (UKE), Institute of Structural and Systems Biology, Hamburg, Germany.; Centre for Structural Systems Biology (CSSB), Hamburg, Germany.; Deutsches Elektronen-Synchrotron Zentrum (DESY), Hamburg, Germany.; Institute of Molecular Biotechnology GmbH (IMBA), Austrian Academy of Sciences, Vienna, Austria.; Research Institute of Molecular Pathology (IMP), Vienna, Austria.
Pantel M; University Medical Center Hamburg-Eppendorf (UKE), Institute of Structural and Systems Biology, Hamburg, Germany.; Centre for Structural Systems Biology (CSSB), Hamburg, Germany.; Deutsches Elektronen-Synchrotron Zentrum (DESY), Hamburg, Germany.
Vesper O; University Medical Center Hamburg-Eppendorf (UKE), Institute of Structural and Systems Biology, Hamburg, Germany.; Centre for Structural Systems Biology (CSSB), Hamburg, Germany.; Deutsches Elektronen-Synchrotron Zentrum (DESY), Hamburg, Germany.; Institute of Molecular Biotechnology GmbH (IMBA), Austrian Academy of Sciences, Vienna, Austria.; Research Institute of Molecular Pathology (IMP), Vienna, Austria.
Kotov V; University Medical Center Hamburg-Eppendorf (UKE), Institute of Structural and Systems Biology, Hamburg, Germany.; Centre for Structural Systems Biology (CSSB), Hamburg, Germany.; Deutsches Elektronen-Synchrotron Zentrum (DESY), Hamburg, Germany.; Institute of Molecular Biotechnology GmbH (IMBA), Austrian Academy of Sciences, Vienna, Austria.; Research Institute of Molecular Pathology (IMP), Vienna, Austria.
Marlovits TC; University Medical Center Hamburg-Eppendorf (UKE), Institute of Structural and Systems Biology, Hamburg, Germany. .; Centre for Structural Systems Biology (CSSB), Hamburg, Germany. .; Deutsches Elektronen-Synchrotron Zentrum (DESY), Hamburg, Germany. .; Institute of Molecular Biotechnology GmbH (IMBA), Austrian Academy of Sciences, Vienna, Austria. .; Research Institute of Molecular Pathology (IMP), Vienna, Austria. .
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Źródło :
Nature communications [Nat Commun] 2021 Mar 09; Vol. 12 (1), pp. 1546. Date of Electronic Publication: 2021 Mar 09.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Bacterial Proteins/*chemistry
Bacterial Proteins/*metabolism
Protein Transport/*physiology
Salmonella typhimurium/*metabolism
Type III Secretion Systems/*chemistry
Type III Secretion Systems/*metabolism
Antigens, Bacterial/chemistry ; Antigens, Bacterial/genetics ; Antigens, Bacterial/metabolism ; Bacterial Proteins/genetics ; Cryoelectron Microscopy ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Models, Molecular ; Protein Conformation, alpha-Helical ; Salmonella enterica/metabolism ; Salmonella typhimurium/genetics ; Type III Secretion Systems/genetics
Czasopismo naukowe
Tytuł :
Probing Interdomain Linkers and Protein Supertertiary Structure In Vitro and in Live Cells with Fluorescent Protein Resonance Energy Transfer.
Autorzy :
Basak S; Department of Physiology & Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA.
Sakia N; Department of Physics and Astronomy, Clemson University, Clemson, SC 29634-0978, USA.
Dougherty L; Department of Physiology & Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA.
Guo Z; Department of Physiology & Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA.
Wu F; Department of Physiology & Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA.
Mindlin F; Department of Physiology & Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA.
Lary JW; National Analytical Ultracentrifugation Facility, University of Connecticut, Storrs, CT 06269, USA.
Cole JL; National Analytical Ultracentrifugation Facility, University of Connecticut, Storrs, CT 06269, USA; Department of Molecular and Cell Biology, and Department of Chemistry, University of Connecticut, Storrs, CT 06269, USA.
Ding F; Department of Physics and Astronomy, Clemson University, Clemson, SC 29634-0978, USA.
Bowen ME; Department of Physiology & Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA. Electronic address: .
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Źródło :
Journal of molecular biology [J Mol Biol] 2021 Mar 05; Vol. 433 (5), pp. 166793. Date of Electronic Publication: 2021 Jan 01.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Molecular Dynamics Simulation*
Bacterial Proteins/*chemistry
Green Fluorescent Proteins/*chemistry
Luminescent Proteins/*chemistry
Recombinant Fusion Proteins/*chemistry
Animals ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; CHO Cells ; Cricetulus ; Fluorescence Resonance Energy Transfer ; Gene Expression ; Genes, Reporter ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Models, Molecular ; Polyethylene Glycols/chemistry ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Protein Isoforms/chemistry ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Single Molecule Imaging ; Sodium Chloride/chemistry ; Urea/chemistry
Czasopismo naukowe
Tytuł :
Structural basis for self-cleavage prevention by tag:anti-tag pairing complementarity in type VI Cas13 CRISPR systems.
Autorzy :
Wang B; State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 200031, China.
Zhang T; State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 200031, China.
Yin J; State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 200031, China.
Yu Y; Structural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Xu W; State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 200031, China.
Ding J; State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 200031, China. Electronic address: .
Patel DJ; Structural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA. Electronic address: .
Yang H; State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 200031, China. Electronic address: .
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Źródło :
Molecular cell [Mol Cell] 2021 Mar 04; Vol. 81 (5), pp. 1100-1115.e5. Date of Electronic Publication: 2021 Jan 19.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
CRISPR-Cas Systems*
Bacterial Proteins/*chemistry
CRISPR-Associated Proteins/*chemistry
Endodeoxyribonucleases/*chemistry
Leptotrichia/*genetics
RNA, Guide/*chemistry
Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Base Pairing ; Base Sequence ; Binding Sites ; CRISPR-Associated Proteins/genetics ; CRISPR-Associated Proteins/metabolism ; Cloning, Molecular ; Cryoelectron Microscopy ; Endodeoxyribonucleases/genetics ; Endodeoxyribonucleases/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Leptotrichia/metabolism ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Interaction Domains and Motifs ; RNA Cleavage ; RNA, Guide/genetics ; RNA, Guide/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Substrate Specificity
SCR Organism :
Leptotrichia shahii
Czasopismo naukowe
Tytuł :
Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences.
Autorzy :
Green AG; Department of Systems Biology, Harvard Medical School, Boston, MA, 02115, USA.
Elhabashy H; Biomolecular Interactions, Max Planck Institute for Developmental Biology, 72076, Tübingen, Germany.; Institute for Bioinformatics and Medical Informatics, University of Tübingen, Sand 14, 72076, Tübingen, Germany.; Department of Computer Science, University of Tübingen, WSI/ZBIT, Sand 14, 72076, Tübingen, Germany.
Brock KP; Department of Systems Biology, Harvard Medical School, Boston, MA, 02115, USA.
Maddamsetti R; Department of Systems Biology, Harvard Medical School, Boston, MA, 02115, USA.
Kohlbacher O; Biomolecular Interactions, Max Planck Institute for Developmental Biology, 72076, Tübingen, Germany. .; Institute for Bioinformatics and Medical Informatics, University of Tübingen, Sand 14, 72076, Tübingen, Germany. .; Department of Computer Science, University of Tübingen, WSI/ZBIT, Sand 14, 72076, Tübingen, Germany. .; Quantitative Biology Center, University of Tübingen, Auf der Morgenstelle 8, 72076, Tübingen, Germany. .; Institute for Translational Bioinformatics, University Hospital Tübingen, Sand 14, 72076, Tübingen, Germany. .
Marks DS; Institute for Bioinformatics and Medical Informatics, University of Tübingen, Sand 14, 72076, Tübingen, Germany. .; Broad Institute of Harvard and MIT, Cambridge, MA, 02142, USA. .
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Źródło :
Nature communications [Nat Commun] 2021 Mar 02; Vol. 12 (1), pp. 1396. Date of Electronic Publication: 2021 Mar 02.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Evolution, Molecular*
Genome, Bacterial*
Protein Interaction Mapping*
Amino Acids/*genetics
Bacterial Proteins/*genetics
Bacterial Proteins/*metabolism
Bacterial Proteins/chemistry ; Base Sequence ; Escherichia coli/genetics ; Eukaryotic Cells/metabolism ; Membrane Proteins/metabolism ; Molecular Docking Simulation ; Protein Binding ; Proteome/metabolism
Czasopismo naukowe

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