Search Results - "MESH: Sequence Alignment"

Two newly established and mutually related subfamilies GH13_48 and GH13_49 of the α-amylase family GH13

Authors: Mareček, Filip Terrapon, Nicolas Janeček, Štefan et al.

Contributors: Mareček, Filip Terrapon, Nicolas Janeček, Štefan et al.

Source: Appl Microbiol Biotechnol

Subject Terms: 0301 basic medicine, 0303 health sciences, MESH: Conserved Sequence, [SDV]Life Sciences [q-bio], Alpha-amylase family, MESH: Sequence Alignment, Structural comparison, MESH: Amino Acid Sequence, Evolutionary relatedness, [SDV] Life Sciences [q-bio], 03 medical and health sciences, MESH: alpha-Amylases, Unique sequence features, Amino Acid Sequence, alpha-Amylases, MESH: Phylogeny, Biotechnologically Relevant Enzymes and Proteins, Sequence Alignment, Phylogeny, Conserved Sequence, GH13 subfamilies

Access URL: https://pubmed.ncbi.nlm.nih.gov/38990377
https://hal.science/hal-04690683v1
https://doi.org/10.1007/s00253-024-13251-x

ICARUS: flexible protein structural alignment based on Protein Units

Authors: Cretin, Gabriel Périn, Charlotte Zimmermann, Nicolas et al.

Contributors: Cretin, Gabriel Périn, Charlotte Zimmermann, Nicolas et al.

Source: ISSN: 1367-4803.

Subject Terms: MESH: Algorithms, MESH: Biological Evolution, MESH: Protein Structure, Secondary, MESH: Proteins* / chemistry, MESH: Sequence Alignment, MESH: Software, [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]

Relation: info:eu-repo/semantics/altIdentifier/pmid/37498544; PUBMED: 37498544; PUBMEDCENTRAL: PMC10400377

Availability: https://hal.science/hal-05269266
https://hal.science/hal-05269266v1/document
https://hal.science/hal-05269266v1/file/btad459.pdf
https://doi.org/10.1093/bioinformatics/btad459

Comparative Virus-Host Protein Interactions of the Bluetongue Virus NS4 Virulence Factor

Authors: Fablet, Aurore Kundlacz, Cindy Dupré, Juliette et al.

Contributors: Fablet, Aurore Kundlacz, Cindy Dupré, Juliette et al.

Source: ISSN: 1999-4915 ; Viruses ; https://anses.hal.science/anses-03659032 ; Viruses, 2022, 14 (2), pp.182. ⟨10.3390/v14020182⟩.

Subject Terms: protein–protein interaction, WTAP, NS4, Bluetongue virus, MESH: Amino Acid Motifs, MESH: Amino Acid Sequence, MESH: Cattle Diseases, MESH: Host-Pathogen Interactions, MESH: Protein Binding, MESH: RNA Splicing Factors, MESH: Sequence Alignment, MESH: Viral Nonstructural Proteins, MESH: Virulence Factors, MESH: Virus Replication, MESH: Animals, MESH: Bluetongue, MESH: Bluetongue virus, MESH: Cattle, [SDV.BA.MVSA]Life Sciences [q-bio]/Animal biology/Veterinary medicine and animal Health

Relation: info:eu-repo/semantics/altIdentifier/pmid/35215776; PUBMED: 35215776; PUBMEDCENTRAL: PMC8878768; WOS: 000762069000001

Availability: https://anses.hal.science/anses-03659032
https://anses.hal.science/anses-03659032v1/document
https://anses.hal.science/anses-03659032v1/file/viruses-14-00182.pdf
https://doi.org/10.3390/v14020182

A novel SARS-CoV-2 related coronavirus in bats from Cambodia

Authors: Delaune, Deborah Hul, Vibol Karlsson, Erik, A. et al.

Contributors: Delaune, Deborah Hul, Vibol Karlsson, Erik, A. et al.

Source: ISSN: 2041-1723.

Subject Terms: MESH: Amino Acid Sequence, MESH: Animals, MESH: SARS-CoV-2, MESH: Sequence Alignment, MESH: Spike Glycoprotein, Coronavirus, MESH: COVID-19, MESH: Cambodia, MESH: Chiroptera, MESH: Evolution, Molecular, MESH: Genome, Viral, MESH: Phylogeny, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, [SDV.BID.SPT]Life Sciences [q-bio]/Biodiversity/Systematics, Phylogenetics and taxonomy

Relation: info:eu-repo/semantics/altIdentifier/pmid/34753934; PUBMED: 34753934; PUBMEDCENTRAL: PMC8578604

Availability: https://riip.hal.science/pasteur-03576361
https://riip.hal.science/pasteur-03576361v1/document
https://riip.hal.science/pasteur-03576361v1/file/s41467-021-26809-4.pdf
https://doi.org/10.1038/s41467-021-26809-4

The coordinated replication of Vibrio cholerae ’s two chromosomes required the acquisition of a unique domain by the RctB initiator

Authors: Fournes, Florian Niault, Theophile Czarnecki, Jakub et al.

Contributors: Fournes, Florian Niault, Theophile Czarnecki, Jakub et al.

Source: ISSN: 0305-1048.

Subject Terms: MESH: Amino Acid Sequence, MESH: Bacterial Proteins, MESH: Replication Origin, MESH: Sequence Alignment, MESH: Base Sequence, MESH: Sequence Homology, Amino Acid, MESH: Signal Transduction, MESH: Vibrio cholerae, MESH: Binding Sites, MESH: Binding, Competitive, MESH: Chromosomes, Bacterial, MESH: Cloning, Molecular, MESH: Gene Expression Regulation, MESH: DNA Replication, MESH: DNA, MESH: Escherichia coli, MESH: Genetic Vectors, MESH: Models, MESH: Protein Binding, MESH: Protein Conformation, alpha-Helical, beta-Strand, MESH: Protein Interaction Domains and Motifs, MESH: Recombinant Proteins, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology

Relation: info:eu-repo/semantics/altIdentifier/pmid/34643717; PUBMED: 34643717; PUBMEDCENTRAL: PMC8565311

Availability: https://hal.sorbonne-universite.fr/hal-03500868
https://hal.sorbonne-universite.fr/hal-03500868v1/document
https://hal.sorbonne-universite.fr/hal-03500868v1/file/gkab903.pdf
https://doi.org/10.1093/nar/gkab903

Programmable receptors enable bacterial biosensors to detect pathological biomarkers in clinical samples

Authors: Chang, Hung-Ju Zúñiga, Ana Conejero, Ismael et al.

Contributors: Chang, Hung-Ju Zúñiga, Ana Conejero, Ismael et al.

Source: ISSN: 2041-1723.

Subject Terms: MESH: Bacteria, MESH: Bile Acids and Salts, MESH: Escherichia coli, MESH: Gene Expression Regulation, Bacterial, MESH: Humans, MESH: Liver Transplantation, MESH: Metabolic Engineering, MESH: Pathology, Molecular, MESH: Sensitivity and Specificity, MESH: Sequence Alignment, MESH: Vibrio, MESH: Vibrio Infections, MESH: Biomarkers, MESH: Biosensing Techniques, MESH: Carrier Proteins, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology

Relation: info:eu-repo/semantics/altIdentifier/pmid/34471137; PUBMED: 34471137; PUBMEDCENTRAL: PMC8410942; WOS: 000692406100021

Availability: https://hal.science/hal-03641379
https://hal.science/hal-03641379v1/document
https://hal.science/hal-03641379v1/file/s41467-021-25538-y.pdf
https://doi.org/10.1038/s41467-021-25538-y

Camelid nanobodies used as crystallization chaperones for different constructs of PorM, a component of the type IX secretion system fromPorphyromonas gingivalis

Authors: Alain Roussel Thi Trang Nhung Trinh Aline Desmyter et al.

Contributors: Alain Roussel Thi Trang Nhung Trinh Aline Desmyter et al.

Source: Acta Crystallographica Section F Structural Biology Communications. 73:286-293

Subject Terms: Models, Molecular, Protein Conformation, alpha-Helical, 0301 basic medicine, Gene Expression, MESH: Amino Acid Sequence, Crystallography, X-Ray, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, MESH: Recombinant Proteins, MESH: Protein Conformation, MESH: Genetic Vectors, MESH: Models, 5lmj, MESH: Animals, MESH: Sequence Homology, Cloning, Molecular, MESH: Bacterial Secretion Systems, MESH: Bacterial Proteins, [SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Bacterial Secretion Systems, MESH: Crystallization, [SDV.MHEP.ME] Life Sciences [q-bio]/Human health and pathology/Emerging diseases, [SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology, 5lmw, 0303 health sciences, [SDV.BIBS] Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], MESH: Kinetics, MESH: Escherichia coli, MESH: Crystallography, New World, MESH: Camelus, Amino Acid, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, [SDV.SP.PHARMA] Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, [SDV.MHEP.MI] Life Sciences [q-bio]/Human health and pathology/Infectious diseases, MESH: Porphyromonas gingivalis, nb02, MESH: Thermodynamics, MESH: Molecular Chaperones, nb01, Crystallization, Camelids, New World, Porphyromonas gingivalis, Protein Binding, MESH: Gene Expression, crystallization chaperones, Camelus, MESH: Cloning, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Genetic Vectors, MESH: Sequence Alignment, MESH: Single-Domain Antibodies, 03 medical and health sciences, Bacterial Proteins, Peptide Library, Escherichia coli, MESH: Protein Binding, nb130, Animals, 5fwo, Amino Acid Sequence, MESH: Camelids, [SDV.IMM.II] Life Sciences [q-bio]/Immunology/Innate immunity, nb19, MESH: Protein Interaction Domains and Motifs, Binding Sites, Molecular Biology/Structural Biology [q-bio.BM], alpha-Helical, [SDV.NEU.NB] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Molecular, [SDV.BIO] Life Sciences [q-bio]/Biotechnology, Kinetics, MESH: Binding Sites, X-Ray, beta-Strand, MESH: Peptide Library, PorM, [SDV.MP.BAC] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, camelid nanobodies, 5lz0, type IX secretion system, Molecular Chaperones

File Description: application/pdf

Access URL: https://europepmc.org/articles/pmc5417319?pdf=render
https://pubmed.ncbi.nlm.nih.gov/28471361
https://pubmed.ncbi.nlm.nih.gov/28471361/
http://journals.iucr.org/f/issues/2017/05/00/rl5131/rl5131.pdf
https://www.rcsb.org/structure/5LMW
https://www.ncbi.nlm.nih.gov/pubmed/28471361
https://www.onlinelibrary.wiley.com/doi/abs/10.1107/S2053230X17005969
https://europepmc.org/abstract/MED/28471361

Shedding Light on the Antimicrobial Peptide Arsenal of Terrestrial Isopods: Focus on Armadillidins, a New Crustacean AMP Family.

Authors: Becking, Thomas Delaunay, Carine Cordaux, Richard et al.

Contributors: Becking, Thomas Delaunay, Carine Cordaux, Richard et al.

Source: ISSN: 2073-4425 ; Genes ; https://hal.science/hal-03021726 ; Genes, 2020, 11 (1), ⟨10.3390/genes11010093⟩.

Subject Terms: transcriptomics, terrestrial isopods, malacostraca, innate immunity, glycine-rich peptides, crustacea, antimicrobial peptides, MESH: Amino Acid Sequence, MESH: Animals, MESH: Antimicrobial Cationic Peptides, MESH: Cloning, Molecular, MESH: Isopoda, MESH: Phylogeny, MESH: Sequence Alignment, MESH: Transcription Factors, [SDV]Life Sciences [q-bio]

Relation: info:eu-repo/semantics/altIdentifier/pmid/31947541; PUBMED: 31947541; PUBMEDCENTRAL: PMC7017220

Availability: https://hal.science/hal-03021726
https://hal.science/hal-03021726v1/document
https://hal.science/hal-03021726v1/file/88-Becking_2020_Genes.pdf
https://doi.org/10.3390/genes11010093

Novel ribonucleotide discrimination in the RNA polymerase-like two-barrel catalytic core of Family D DNA polymerases

Authors: Zatopek, Kelly Alpaslan, Ece Evans, Thomas, C et al.

Contributors: Zatopek, Kelly Alpaslan, Ece Evans, Thomas, C et al.

Source: ISSN: 0305-1048.

Subject Terms: MESH: Amino Acid Sequence, MESH: Archaeal Proteins, MESH: Genome, Archaeal, MESH: Histidine, MESH: Kinetics, MESH: Models, Molecular, MESH: Mutation, MESH: Protein Binding, MESH: Protein Conformation, alpha-Helical, beta-Strand, MESH: Protein Interaction Domains and Motifs, MESH: Recombinant Proteins, MESH: Binding Sites, MESH: Ribonucleotides, MESH: Sequence Alignment, MESH: Sequence Homology, Amino Acid, MESH: Substrate Specificity, MESH: Thermococcus, MESH: Catalytic Domain, MESH: Cloning, MESH: DNA Replication, MESH: DNA, MESH: DNA-Directed DNA Polymerase, MESH: Gene Expression, MESH: Gene Expression Regulation, [SDV.BBM]Life Sciences [q-bio]/Biochemistry

Relation: info:eu-repo/semantics/altIdentifier/pmid/33137176; PUBMED: 33137176; PUBMEDCENTRAL: PMC7708050

Availability: https://pasteur.hal.science/pasteur-03086156
https://pasteur.hal.science/pasteur-03086156v1/document
https://pasteur.hal.science/pasteur-03086156v1/file/gkaa986.pdf
https://doi.org/10.1093/nar/gkaa986

Homozygous mutation of PLCZ1 leads to defective human oocyte activation and infertility that is not rescued by the WW-binding protein PAWP

Authors: Escoffier, Jessica Lee, Hoi Chang Yassine, Sandra et al.

Contributors: Escoffier, Jessica Lee, Hoi Chang Yassine, Sandra et al.

Source: Human Molecular Genetics, Vol. 25, No 5 (2016) pp. 878-891

Subject Terms: Male, Models, Molecular, 0301 basic medicine, MESH: Sperm-Ovum Interactions, MESH: Amino Acid Sequence, MESH: Base Sequence, 7. Clean energy, Mice, Phosphoinositide Phospholipase C, MESH: Models, MESH: Animals, ddc:576.5, MESH: Embryo Loss, 0303 health sciences, [SDV.BIBS] Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], MESH: Spermatozoa, Homozygote, MESH: Sperm Motility, MESH: Gene Expression Regulation, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Embryo Loss, Female, MESH: Seminal Plasma Proteins, MESH: Homozygote, Adult, MESH: Protein Transport, MESH: Mutation, Molecular Sequence Data, MESH: Sequence Alignment, MESH: Carrier Proteins, MESH: Calcium Signaling, MESH: Oocytes, 03 medical and health sciences, MESH: Phosphoinositide Phospholipase C, Animals, Humans, MESH: Infertility, Amino Acid Sequence, Calcium Signaling, MESH: Mice, Infertility, Male, MESH: Humans, MESH: In Vitro Oocyte Maturation Techniques, MESH: Molecular Sequence Data, Base Sequence, Molecular, MESH: Adult, MESH: Male, MESH: Siblings, In Vitro Oocyte Maturation Techniques, Gene Expression Regulation, Mutation, Oocytes, Carrier Proteins, MESH: Female

Access URL: https://academic.oup.com/hmg/article-pdf/25/5/878/18527014/ddv617.pdf
https://pubmed.ncbi.nlm.nih.gov/26721930
http://europepmc.org/articles/PMC4754041
https://archive-ouverte.unige.ch/unige:86826
https://pubmed.ncbi.nlm.nih.gov/26721930/
https://academic.oup.com/hmg/article/25/5/878/2384541
https://www.scholars.northwestern.edu/en/publications/homozygous-mutation-of-plcz1-leads-to-defective-human-oocyte-acti
http://www.ncbi.nlm.nih.gov/pubmed/26721930
https://hal.science/hal-01877966v1
https://doi.org/10.1093/hmg/ddv617
https://archive-ouverte.unige.ch/unige:86826

Tetramerization and interdomain flexibility of the replication initiation controller YabA enables simultaneous binding to multiple partners

Authors: Alexandre Bazin Franck Molina Laurent Terradot et al.

Contributors: Alexandre Bazin Franck Molina Laurent Terradot et al.

Source: Nucleic Acids Res
'Nucleic Acids Research ', vol: 44, pages: 449-463 (2016)
Nucleic Acids Research 1 (44), 449-463. (2016)
Nucleic Acids Research
Europe PubMed Central

Subject Terms: Models, Molecular, 0301 basic medicine, Protein Conformation, [SDV]Life Sciences [q-bio], Amino Acid Motifs, Intracellular Space, MESH: DNA Replication, MESH: Amino Acid Sequence, MESH: Zinc, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, MESH: Amino Acid Motifs, MESH: Protein Conformation, MESH: Structure-Activity Relationship, interdomain flexibility, Tetramerization, Structural Biology, MESH: Models, Protein Interaction Mapping, MESH: Bacterial Proteins, 0303 health sciences, MESH: Protein Multimerization, [SDV] Life Sciences [q-bio], DNA-Binding Proteins, Protein Transport, MESH: Intracellular Space, Bacillus subtilis, Protein Binding, DNA Replication, MESH: Protein Transport, MESH: Mutation, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Molecular Sequence Data, MESH: Sequence Alignment, 03 medical and health sciences, Bacterial Proteins, MESH: Protein Binding, Position-Specific Scoring Matrices, Protein Interaction Domains and Motifs, Amino Acid Sequence, MESH: Protein Interaction Domains and Motifs, MESH: Molecular Sequence Data, Binding Sites, Molecular Biology/Structural Biology [q-bio.BM], MESH: Protein Interaction Mapping, Molecular, MESH: Position-Specific Scoring Matrices, MESH: Multiprotein Complexes, MESH: Bacillus subtilis, MESH: Binding Sites, Multiprotein Complexes, Mutation, Protein Multimerization, Sequence Alignment, MESH: DNA-Binding Proteins

File Description: application/pdf

Access URL: https://academic.oup.com/nar/article-pdf/44/1/449/18786601/gkv1318.pdf
https://pubmed.ncbi.nlm.nih.gov/26615189
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:44420
http://prodinra.inra.fr/record/351843
https://hal.univ-grenoble-alpes.fr/hal-01991824v1/document
https://hal.univ-grenoble-alpes.fr/hal-01991824v1
https://doi.org/10.1093/nar/gkv1318
http://europepmc.org/articles/PMC4705661

Crystal Structure of the Vaccinia Virus Uracil-DNA Glycosylase in Complex with DNA

Authors: Christophe N. Peyrefitte Nicolas Tarbouriech Céline Contesto-Richefeu et al.

Contributors: Christophe N. Peyrefitte Nicolas Tarbouriech Céline Contesto-Richefeu et al.

Source: Journal of Biological Chemistry. 290:17923-17934

Subject Terms: 0301 basic medicine, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Protein Conformation, Molecular Sequence Data, MESH: Sequence Alignment, Vaccinia virus, MESH: Amino Acid Sequence, Crystallography, X-Ray, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, 03 medical and health sciences, MESH: Protein Conformation, MESH: Vaccinia virus, MESH: Molecular Docking Simulation, Vaccinia, Humans, Amino Acid Sequence, Uracil-DNA Glycosidase, MESH: Uracil-DNA Glycosidase, 0303 health sciences, MESH: Humans, MESH: Molecular Sequence Data, Molecular Biology/Structural Biology [q-bio.BM], MESH: Crystallography, MESH: DNA, DNA, MESH: Vaccinia, 3. Good health, Molecular Docking Simulation, MESH: Nucleic Acid Conformation, 13. Climate action, X-Ray, Nucleic Acid Conformation, Sequence Alignment

Access URL: http://www.jbc.org/content/290/29/17923.full.pdf
https://pubmed.ncbi.nlm.nih.gov/26045555
https://europepmc.org/article/MED/26045555
http://www.rcsb.org/pdb/explore/explore.do?structureId=4YIG
https://www.rcsb.org/structure/4YGM
https://www.jbc.org/content/290/29/17923.full.pdf
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4505040/
https://www.sciencedirect.com/science/article/pii/S0021925820423907
https://hal.univ-grenoble-alpes.fr/hal-01219729v1

Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter

Authors: Reguera, Juan Mudgal, Gaurav Santiago, César et al.

Contributors: Reguera, Juan Mudgal, Gaurav Santiago, César et al.

Source: Cell

Subject Terms: Models, Molecular, Orthobunyavirus, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], MESH: Promoter Regions, MESH: Sequence Alignment, MESH: Catalytic Domain, MESH: Orthobunyavirus, MESH: Amino Acid Sequence, Crystallography, X-Ray, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Article, Genetic, MESH: RNA, Catalytic Domain, MESH: Models, Viral, Amino Acid Sequence, Promoter Regions, Genetic, Molecular Biology/Structural Biology [q-bio.BM], Biochemistry, Genetics and Molecular Biology(all), MESH: Crystallography, Molecular, RNA-Dependent RNA Polymerase, 3. Good health, MESH: Ribonucleoproteins, Ribonucleoproteins, X-Ray, RNA, Viral, MESH: RNA Replicase, Sequence Alignment

Access URL: http://www.cell.com/article/S009286741500553X/pdf
https://pubmed.ncbi.nlm.nih.gov/26004069
https://pubmed.ncbi.nlm.nih.gov/26004069/
https://www.sciencedirect.com/science/article/abs/pii/S009286741500553X
https://www.rcsb.org/structure/5AMQ
http://www.ncbi.nlm.nih.gov/pubmed/26004069
http://europepmc.org/articles/PMC4459711
http://europepmc.org/abstract/MED/26004069

Culex pipiens crossing type diversity is governed by an amplified and polymorphic operon of Wolbachia

Authors: Fabienne Justy Mathieu Sicard Martin Cohen-Gonsaud et al.

Contributors: Fabienne Justy Mathieu Sicard Martin Cohen-Gonsaud et al.

Source: Nat Commun
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)

Subject Terms: Male, 0301 basic medicine, [SDV]Life Sciences [q-bio], MESH: Amino Acid Sequence, MESH: Base Sequence, MESH: Animals, MESH: Sequence Homology, MESH: Bacterial Proteins, 2. Zero hunger, 0303 health sciences, MESH: Symbiosis, Bacterial, Toxin-Antitoxin Systems, 3. Good health, [SDV] Life Sciences [q-bio], Amino Acid, Culex, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Drosophila melanogaster, MESH: Wolbachia, Female, Wolbachia, MESH: Operon, MESH: Host Specificity, Science, MESH: Sequence Alignment, MESH: Culex, Article, Host Specificity, MESH: Drosophila melanogaster, 03 medical and health sciences, Genetic, Bacterial Proteins, Operon, Animals, MESH: Genome, Amino Acid Sequence, Symbiosis, MESH: Polymorphism, [SDV.MP] Life Sciences [q-bio]/Microbiology and Parasitology, Crosses, Genetic, Polymorphism, Genetic, Base Sequence, Sequence Homology, Amino Acid, MESH: Crosses, MESH: Male, MESH: Female, Sequence Alignment, Genome, Bacterial, MESH: Toxin-Antitoxin Systems

File Description: application/pdf

Access URL: https://www.nature.com/articles/s41467-017-02749-w.pdf
https://pubmed.ncbi.nlm.nih.gov/29358578
https://doaj.org/article/4e14c93f8e4b4de493fed325b276122c
https://riip.hal.science/pasteur-01728878v1
https://riip.hal.science/pasteur-01728878v1/document
https://doi.org/10.1038/s41467-017-02749-w

Deep mutational scanning comprehensively maps how Zika envelope protein mutations affect viral growth and antibody escape

Authors: Matthew J. Evans Carina H. Storrs Daniel J. P. Lawrence et al.

Contributors: Matthew J. Evans Carina H. Storrs Daniel J. P. Lawrence et al.

Source: Journal of Virology. 93

Subject Terms: Models, Molecular, 0301 basic medicine, Protein Conformation, MESH: Virus Internalization, MESH: Amino Acid Sequence, virus entry, Antibodies, Viral, Zika virus, Epitopes, MESH: Protein Conformation, Viral Envelope Proteins, MESH: Chlorocebus aethiops, Sequence Analysis, Protein, MESH: Models, Monoclonal, Chlorocebus aethiops, MESH: Animals, MESH: Immune Evasion, Viral, Neutralizing, MESH: High-Throughput Nucleotide Sequencing, glycoproteins, [SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology, Antibodies, Monoclonal, High-Throughput Nucleotide Sequencing, 3. Good health, MESH: HEK293 Cells, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, mutagenesis, MESH: Mutation, MESH: Epitopes, MESH: Sequence Alignment, MESH: Glycoproteins, MESH: Vero Cells, MESH: Zika Virus, MESH: Sequence Analysis, 03 medical and health sciences, MESH: Zika Virus Infection, Animals, Humans, neutralizing antibodies, Amino Acid Sequence, Vero Cells, Glycoproteins, Immune Evasion, MESH: Humans, Protein, MESH: Antibodies, Molecular, Virus Internalization, Antibodies, Neutralizing, HEK293 Cells, MESH: Viral Envelope Proteins, Mutation, Sequence Alignment

Access URL: https://www.biorxiv.org/content/biorxiv/early/2019/08/05/725556.full.pdf
https://europepmc.org/articles/pmc6854493?pdf=render
https://pubmed.ncbi.nlm.nih.gov/31511387
https://www.biorxiv.org/content/biorxiv/early/2019/08/05/725556.full.pdf
https://www.biorxiv.org/content/10.1101/725556v1
https://journals.asm.org/doi/pdf/10.1128/JVI.01291-19
https://www.ncbi.nlm.nih.gov/pubmed/31511387
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6854493
https://pubmed.ncbi.nlm.nih.gov/31511387/
https://europepmc.org/article/MED/31511387

NS2 proteases from hepatitis C virus and related hepaciviruses share composite active sites and previously unrecognized intrinsic proteolytic activities

Authors: Boukadida, Célia Fritz, Matthieu Blumen, Brigitte et al.

Contributors: Boukadida, Célia Fritz, Matthieu Blumen, Brigitte et al.

Source: ISSN: 1553-7366.

Subject Terms: Polypeptides, Crystal structure, Cofactors (biochemistry), Precursor cells, Proteases, Sequence alignment, Hepacivirus, Hepatitis C virus, MESH: Amino Acid Sequence, MESH: Animals, MESH: Catalytic Domain* / genetics, MESH: Chiroptera, MESH: Hepacivirus, MESH: Horses, MESH: Humans, MESH: Peptide Hydrolases / chemistry, MESH: Peptide Hydrolases / genetics, MESH: Peptide Hydrolases / metabolism, MESH: Phylogeny, MESH: Protein Domains / genetics, MESH: Proteolysis, MESH: Rodentia, MESH: Sequence Alignment, MESH: Viral Nonstructural Proteins / chemistry, MESH: Viral Nonstructural Proteins / genetics, MESH: Viral Nonstructural Proteins / metabolism, [SDV]Life Sciences [q-bio]

Relation: info:eu-repo/semantics/altIdentifier/pmid/29415072; PUBMED: 29415072; PUBMEDCENTRAL: PMC5819835

Availability: https://pasteur.hal.science/pasteur-02896778
https://pasteur.hal.science/pasteur-02896778v1/document
https://pasteur.hal.science/pasteur-02896778v1/file/NS2%20proteases%20from%20hepatitis%20C%20virus%20and%20related%20hepaciviruses.pdf
https://doi.org/10.1371/journal.ppat.1006863

The steroid derivative 6-aminocholestanol inhibits the DEAD-box helicase eIF4A (LieIF4A) from the Trypanosomatid parasite Leishmania by perturbing the RNA and ATP binding sites

Authors: Abdelkrim, Yosser Zina Harigua-Souiai, Emna Barhoumi, Mourad et al.

Contributors: Abdelkrim, Yosser Zina Harigua-Souiai, Emna Barhoumi, Mourad et al.

Source: ISSN: 0166-6851 ; Molecular and Biochemical Parasitology ; https://pasteur.hal.science/pasteur-02528567 ; Molecular and Biochemical Parasitology, 2018, 226, pp.9-19. ⟨10.1016/j.molbiopara.2018.10.001⟩.

Subject Terms: Leishmania infantum, RNA helicase, Translation-initiation factor, Drug design, Hippuristanol, MESH: Adenosine Triphosphate, MESH: Amino Acid Sequence, MESH: Conserved Sequence, MESH: Drug Repositioning, MESH: Protein Binding, MESH: Eukaryotic Initiation Factor-4A, MESH: Gene Expression, MESH: Genetic Vectors, MESH: Humans, MESH: Kinetics, MESH: Leishmania infantum, MESH: Mice, MESH: Sequence Homology, Amino Acid, MESH: Protein Interaction Domains and Motifs, MESH: Animals, MESH: Protein Structure, Secondary, MESH: Protozoan Proteins, MESH: RNA, Helminth, MESH: Recombinant Proteins, MESH: Sequence Alignment, MESH: Trypanocidal Agents, MESH: Escherichia coli

Relation: info:eu-repo/semantics/altIdentifier/pmid/30365976; PUBMED: 30365976

Availability: https://pasteur.hal.science/pasteur-02528567
https://pasteur.hal.science/pasteur-02528567v1/document
https://pasteur.hal.science/pasteur-02528567v1/file/Zina_MBP_manuscript_20-acc.pdf
https://doi.org/10.1016/j.molbiopara.2018.10.001

FcpB Is a Surface Filament Protein of the Endoflagellum Required for the Motility of the Spirochete Leptospira

Authors: Wunder, Elsio, A. Jr Slamti, Leyla Suwondo, David, N et al.

Contributors: Wunder, Elsio, A. Jr Slamti, Leyla Suwondo, David, N et al.

Source: ISSN: 2235-2988 ; Frontiers in Cellular and Infection Microbiology ; https://pasteur.hal.science/pasteur-02100036 ; Frontiers in Cellular and Infection Microbiology, 2018, 8, pp.130. ⟨10.3389/fcimb.2018.00130⟩.

Subject Terms: Leptospira, spirochetes, flagella, motility, flagellar system, MESH: Amino Acid Sequence, MESH: Cell Movement, MESH: Sequence Deletion, MESH: Cryoelectron Microscopy, MESH: DNA Transposable Elements, MESH: Flagella, MESH: Flagellin, MESH: Leptospira, MESH: Microscopy, Video, MESH: Phenotype, MESH: Sequence Alignment, [SDV]Life Sciences [q-bio], [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology

Relation: info:eu-repo/semantics/altIdentifier/pmid/29868490; PRODINRA: 430556; PUBMED: 29868490; PUBMEDCENTRAL: PMC5953323; WOS: 000431685800001

Availability: https://pasteur.hal.science/pasteur-02100036
https://pasteur.hal.science/pasteur-02100036v1/document
https://pasteur.hal.science/pasteur-02100036v1/file/PMID%2029868490.pdf
https://doi.org/10.3389/fcimb.2018.00130

Species-specific host factors rather than virus-intrinsic virulence determine primate lentiviral pathogenicity

Authors: Joas, Simone Parrish, Erica, H Gnanadurai, Clement, W et al.

Contributors: Joas, Simone Parrish, Erica, H Gnanadurai, Clement, W et al.

Source: ISSN: 2041-1723.

Subject Terms: MESH: Amino Acid Sequence, MESH: Animals, MESH: Female, MESH: Gene Expression Regulation, MESH: Humans, MESH: HIV-1, MESH: Host Specificity, MESH: Human Immunodeficiency Virus Proteins, MESH: Lentiviruses, Primate, MESH: Lymphocyte Activation, MESH: NF-kappa B, MESH: Sequence Alignment, MESH: Viral Load, MESH: Signal Transduction, MESH: Simian Immunodeficiency Virus, MESH: Transcription, Genetic, MESH: Viral Regulatory and Accessory Proteins, MESH: Bone Marrow Stromal Antigen 2, MESH: Virulence, MESH: Virus Replication, MESH: nef Gene Products, Human Immunodeficiency Virus, MESH: CD3 Complex, MESH: Cercopithecus aethiops, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, [SDV.IMM]Life Sciences [q-bio]/Immunology, [SDV.BA]Life Sciences [q-bio]/Animal biology

Relation: info:eu-repo/semantics/altIdentifier/pmid/29636452; PUBMED: 29636452; PUBMEDCENTRAL: PMC5893559

Availability: https://pasteur.hal.science/pasteur-01959320
https://pasteur.hal.science/pasteur-01959320v1/document
https://pasteur.hal.science/pasteur-01959320v1/file/species-specific-host-factors-rather-than-virus-intrinsic-virulence-determine-primate-lentiviral-pathogenicity.pdf
https://doi.org/10.1038/s41467-018-03762-3

Molecular basis of agonist docking in a humanGPR103 homology model by site‐directed mutagenesis and structure–activity relationship studies

Authors: Neveu, Cindy Dulin, Fabienne Lefranc, Benjamin et al.

Contributors: Neveu, Cindy Dulin, Fabienne Lefranc, Benjamin et al.

Source: British Journal of Pharmacology. 171:4425-4439

Subject Terms: Models, Molecular, 0301 basic medicine, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Molecular Sequence Data, MESH: Sequence Alignment, MESH: Cricetinae, beta-2, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, CHO Cells, MESH: Neuropeptides, Receptors, G-Protein-Coupled, G-Protein-Coupled, Structure-Activity Relationship, 03 medical and health sciences, MESH: Structure-Activity Relationship, Cricetulus, MESH: Cricetulus, MESH: CHO Cells, Cricetinae, MESH: Models, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Receptors, Site-Directed, Animals, Humans, MESH: Animals, Amino Acid Sequence, MESH: Mutagenesis, 2. Zero hunger, 0303 health sciences, MESH: Humans, MESH: Molecular Sequence Data, Neuropeptides, Molecular, Adrenergic, MESH: Oligopeptides, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Mutagenesis, Site-Directed, Receptors, Adrenergic, beta-2, Oligopeptides, Sequence Alignment

Access URL: https://bpspubs.onlinelibrary.wiley.com/doi/pdfdirect/10.1111/bph.12808
https://pubmed.ncbi.nlm.nih.gov/24913445
https://bpspubs.onlinelibrary.wiley.com/doi/pdf/10.1111/bph.12808
https://www.ncbi.nlm.nih.gov/pubmed/24913445
https://pubmed.ncbi.nlm.nih.gov/24913445/
https://bpspubs.onlinelibrary.wiley.com/doi/full/10.1111/bph.12808
http://europepmc.org/articles/PMC4209149
http://onlinelibrary.wiley.com/doi/10.1111/bph.12808/abstract