نتائج البحث - "Viral Proteins chemistry"

المساهمون: Architecture et fonction des macromolécules biologiques (AFMB), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Department of Biochemical Sciences 'Rossi Fanelli', Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' [Rome], This work was supported by the CNRS. It was also partly supported by the European program H2020 under the EVAg Research Infrastructure (grant agreement 653316). F.T. is a recipient of a PhD fellowship from the Italo-French University., Architecture et fonction des macromolécules biologiques ( AFMB ), Centre National de la Recherche Scientifique ( CNRS ) -Aix Marseille Université ( AMU ) -Institut National de la Recherche Agronomique ( INRA ), Department of Biochemical Sciences, Università degli Studi di Roma 'La Sapienza' [Rome]-Réseau International des Instituts Pasteur ( RIIP ) -Institut Pasteur - Fondation Cenci Bolognetti, Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome] (UNIROMA)

المصدر: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2018, 16 (3), pp.2493-2507. ⟨10.1016/j.jmb.2017.11.012⟩
Journal of Molecular Biology, Elsevier, 2017, 〈10.1016/j.jmb.2017.11.012〉
Journal of Molecular Biology 430 (2018): 2493–2507. doi:10.1016/j.jmb.2017.11.012
info:cnr-pdr/source/autori:Bignon C.; Troilo F.; Gianni S.; Longhi S./titolo:Partner-Mediated Polymorphism of an Intrinsically Disordered Protein/doi:10.1016%2Fj.jmb.2017.11.012/rivista:Journal of Molecular Biology/anno:2018/pagina_da:2493/pagina_a:2507/intervallo_pagine:2493–2507/volume:430
Journal of Molecular Biology, Elsevier, 2017, ⟨10.1016/j.jmb.2017.11.012⟩
Journal of Molecular Biology, 2017, ⟨10.1016/j.jmb.2017.11.012⟩

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba1c6a3c7e170b3725e577eba7c71f08
https://hal.archives-ouvertes.fr/hal-01802951

View record from ScienceDirect

7

Deciphering the unconventional peptide binding to the PDZ domain of MAST2

المؤلفون: Florence Cordier, Nicolas Wolff, Henri Buc, Bertrand Raynal, Elouan Terrien, Muriel Delepierre, Alain Chaffotte, Florent Delhommel

المساهمون: Résonance Magnétique Nucléaire des Biomolécules, Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], Cellule Pasteur UPMC, Institut Pasteur [Paris]-Sorbonne Université (SU), Biophysique Moléculaire (Plate-forme), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris], This work was supported by the Institut Pasteur and Institut Carnot Pasteur Maladies Infectieuses [grant number 13/10/120], and the Ministère de l’Enseignement Supérieur [grant number 883/2013 (to F.D.)]., We thank Jane Hardy and Terence Strick for careful proofreading of the manuscript and Patrick England for valuable discussions., Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris] (IP)-Sorbonne Université (SU), Institut Pasteur [Paris] (IP)

المصدر: Biochemical Journal
Biochemical Journal, Portland Press, 2015, 469 (1), pp.159-168. ⟨10.1042/BJ20141198⟩
Biochemical Journal, 2015, 469 (1), pp.159-168. ⟨10.1042/BJ20141198⟩

مصطلحات موضوعية: Scaffold protein, MESH: Protein Structure, Quaternary, [SDV]Life Sciences [q-bio], Peptide binding, MESH: Protein Multimerization, Biochemistry, MESH: Protein Structure, Tertiary, MESH: Protein-Serine-Threonine Kinases / metabolism, 0302 clinical medicine, MESH: Nuclear Magnetic Resonance, Biomolecular, Tensin, MESH: Rabies virus / metabolism, MESH: Viral Proteins / chemistry, pre-steady-state kinetics, 0303 health sciences, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], biology, MESH: Molecular Dynamics Simulation, Cell biology, DLG1, Microtubule-Associated Proteins, Protein Binding, PDZ domain, MESH: Rabies virus / chemistry, protein–protein interactions, Molecular Dynamics Simulation, Protein Serine-Threonine Kinases, MESH: Protein-Serine-Threonine Kinases / chemistry, Viral Proteins, 03 medical and health sciences, MESH: Microtubule-Associated Proteins / chemistry, Humans, MESH: Protein Binding, PTEN, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Protein Structure, Quaternary, Nuclear Magnetic Resonance, Biomolecular, Molecular Biology, Protein kinase B, 030304 developmental biology, Serine/threonine-specific protein kinase, MESH: Humans, PDZ domains, Cell Biology, MESH: Viral Proteins / metabolism, Protein Structure, Tertiary, MESH: Microtubule-Associated Proteins / metabolism, Rabies virus, intradomain energetic connectivity, biology.protein, sense organs, Protein Multimerization, 030217 neurology & neurosurgery

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c4686c21e9c3b7509080eb7a4c0a244
https://doi.org/10.1042/bj20141198

8

Multiple Regions of Kaposi’s Sarcoma-Associated Herpesvirus ORF59 RNA are Required for Its Expression Mediated by Viral ORF57 and Cellular RBM15

المؤلفون: Vladimir Majerciak, Maria J. Massimelli, David J. Liewehr, Zhi-Ming Zheng, Seth M. Steinberg, Jeong-Gu Kang

المصدر: Viruses, Vol 7, Iss 2, Pp 496-510 (2015)
Viruses
Massimelli, MJ; Majerciak, V; Kang, JG; Liewehr, DJ; Steinberg, SM; & Zheng, ZM. (2015). Multiple regions of Kaposi’s Sarcoma-associated herpesvirus ORF59 RNA are required for its expression mediated by viral ORF57 and cellular RBM15. Viruses, 7(2), 496-510. doi: 10.3390/v7020496. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/92x0j507
Viruses, vol 7, iss 2
Viruses, 7(2), 496-510. Multidisciplinary Digital Publishing Institute (MDPI)

مصطلحات موضوعية: lcsh:QR1-502, RNA, Viral/chemistry, RNA Transport, lcsh:Microbiology, ORF57, ORF59, Transcription (biology), Viral Regulatory and Accessory Proteins, Viral, Cells, Cultured, Herpesvirus 8, Human/genetics, Cultured, Human/genetics, Communication, Herpesviridae Infections/metabolism, RNA-Binding Proteins, Viral Proteins/chemistry, Herpesviridae Infections, Non-coding RNA, RNA silencing, Infectious Diseases, RNA accumulation, RNA editing, Herpesvirus 8, Human, RNA, Viral, Human, Gene Expression Regulation, Viral, RNA export, Cells, Molecular Sequence Data, RNA-dependent RNA polymerase, RBM15, KSHV, Biology, Response Elements, Microbiology, Cell Line, Viral Regulatory and Accessory Proteins/chemistry, Viral Proteins, Genetic, Virology, Genetics, RNA polymerase I, Viral/chemistry, Humans, Herpesvirus 8, Base Sequence, Intron, RNA, Epistasis, Genetic, Molecular biology, Gene Expression Regulation, Protein Biosynthesis, Epistasis, Nucleic Acid Conformation, RNA-Binding Proteins/metabolism

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5751d7aa4bce0b95e77b67ded904cb70
http://www.mdpi.com/1999-4915/7/2/496

Find this article in full text from ProQuest

9

DNA-Interacting Characteristics of the Archaeal Rudiviral Protein SIRV2_Gp1

المؤلفون: Clare Rollie, Eveline Peeters, M. Boon, Tessa E. F. Quax, Malcolm F. White, Rob Lavigne, Marleen Voet, David Prangishvili, Ronnie Willaert

المساهمون: Molecular Microbiology, BBSRC, University of St Andrews. School of Biology, University of St Andrews. Biomedical Sciences Research Complex, Department of Bio-engineering Sciences, Structural Biology Brussels, Microbiology, Faculty of Sciences and Bioengineering Sciences

المصدر: Viruses, Vol 9, Iss 7, p 190 (2017)
Viruses
Viruses, 9(7):190. MDPI AG
Viruses; Volume 9; Issue 7; Pages: 190

مصطلحات موضوعية: 0301 basic medicine, QH301 Biology, lcsh:QR1-502, Rudiviridae, Rudiviridae/genetics, Genome, SIRV2, lcsh:Microbiology, chemistry.chemical_compound, Sulfolobus/virology, Virus Release, helix-turn-helix domain, Helix-turn-helix doman, Host cell surface, biology, Viral Proteins/chemistry, Archaeal Viruses, Sulfolobus, Cell biology, DNA-Binding Proteins, Infectious Diseases, QR355 Virology, DNA-Binding Proteins/chemistry, Archaeal virus, archaea, Protein domain, NDAS, Genome, Viral, Solfolobus, Article, Microbiology, QH301, 03 medical and health sciences, Viral Proteins, Protein Domains, Virology, DNA binding, DNA/chemistry, Gene, QR355, Virion, DNA, archaeal virus, biology.organism_classification, Archaea, 030104 developmental biology, chemistry, Nucleic Acid Conformation

وصف الملف: Electronic; application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::770953151d28ef2e4964d26684b2e25b
https://www.mdpi.com/1999-4915/9/7/190

Find this article in full text from ProQuest

10

Molecular modeling studies demonstrate key mutations that could affect the ligand recognition by influenza AH1N1 neuraminidase

المؤلفون: Saúl Rojas-Hernández, Gema Lizbeth Ramírez-Salinas, Mirko Zimic, Verónica Briz, Miguel Quiliano, José Correa-Basurto, Jazmín García-Machorro

المصدر: Journal of Molecular Modeling. 21

مصطلحات موضوعية: Models, Molecular, Influenza A H1N1, Oseltamivir, purl.org/pe-repo/ocde/ford#1.06.03 [https], Protein Data Bank (RCSB PDB), Neuraminidase, Computational biology, Molecular Dynamics Simulation, Ligands, Molecular Docking Simulation, Catalysis, Docking, Inorganic Chemistry, Viral Proteins, chemistry.chemical_compound, Influenza A Virus, H1N1 Subtype, Point Mutation, Amino Acid Sequence, Homology modeling, Physical and Theoretical Chemistry, Principal Component Analysis, Binding Sites, Multiple sequence alignment, biology, Molecular dynamics simulations, Point mutation, Organic Chemistry, Influenza A Virus, H1N1 Subtype/enzymology, Viral Proteins/chemistry, Neuraminidase/chemistry, Protein Structure, Tertiary, Computer Science Applications, Crystallography, Computational Theory and Mathematics, chemistry, Docking (molecular), biology.protein, Mutations

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a2f217f05835e6364872c46452a0cf8
https://doi.org/10.1007/s00894-015-2835-6

Find this article in full text from Springer Verlag.

تنقيح النتائج