نتائج البحث - "Lawrence P. McIntosh"

1

Ligand- and pH-Induced Structural Transition of Gypsy Moth Lymantria dispar Pheromone-Binding Protein 1 (LdisPBP1)

المؤلفون: Mark Okon, Lawrence P. McIntosh, Mailyn Terrado, Erika Plettner

المصدر: Biochemistry. 59:3411-3426

مصطلحات موضوعية: 0303 health sciences, 010405 organic chemistry, Chemistry, Stereochemistry, Stereoisomerism, Plasma protein binding, Nuclear magnetic resonance spectroscopy, Ligand (biochemistry), 01 natural sciences, Biochemistry, 0104 chemical sciences, 03 medical and health sciences, Protein structure, Helix, Pheromone binding protein, Heteronuclear single quantum coherence spectroscopy, 030304 developmental biology

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::3154d579ff3494a180a7dfd6451aaf8e
https://doi.org/10.1021/acs.biochem.0c00592

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2

Phase separation and clustering of an ABC transporter in Mycobacterium tuberculosis

المؤلفون: Mang Zhu, Thibault Mayor, Yeou Mei Ling, Lawrence P. McIntosh, Lok Tin Hui, Yossef Av-Gay, Joshua M. Scurll, Libin Abraham, Joseph D. Chao, Jennifer M. Bui, Keng C. Chou, Mary Ko, Florian Heinkel, Michael R. Gold, Haoran Li, Horacio Bach, Jason C. Rogalski, Jörg Gsponer

المصدر: Proceedings of the National Academy of Sciences. 116:16326-16331

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fb3ab37c0efec29483efd20faade945
https://doi.org/10.1073/pnas.1820683116

3

Peptidoglycan binding by a pocket on the accessory NTF2-domain of Pgp2 directs helical cell shape of Campylobacter jejuni

المؤلفون: Martin E. Tanner, Jacob A. Brockerman, Chang Sheng-Huei Lin, Jean-Pierre Simorre, Erin C. Gaynor, Jenny Vermeulen, Lawrence P. McIntosh, Anson C. K. Chan, Arvind Soni, Michael E. P. Murphy

المساهمون: Department of Microbiology and Immunology [Vancouver] (UBC Microbiology), University of British Columbia (UBC), Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)

المصدر: Journal of Biological Chemistry
Journal of Biological Chemistry, 2021, 296, pp.100528. ⟨10.1016/j.jbc.2021.100528⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2021, 296, pp.100528. ⟨10.1016/j.jbc.2021.100528⟩
The Journal of Biological Chemistry

مصطلحات موضوعية: 0301 basic medicine, Nucleocytoplasmic Transport Proteins, Protein Conformation, bacterial cell shape, Mutant, MESH: Catalytic Domain, Peptide, Carboxypeptidases, peptidoglycan, Biochemistry, chemistry.chemical_compound, MESH: Protein Conformation, Catalytic Domain, MESH: Bacterial Proteins, chemistry.chemical_classification, biology, NTF2 domain, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], MESH: Nucleocytoplasmic Transport Proteins, MESH: Peptidoglycan, PG, peptidoglycan, carboxypeptidase, HPLC, high performance liquid chromatography, docking, Peptidoglycan binding, Research Article, crystal structure, nuclear magnetic resonance (NMR), Campylobacter jejuni, MESH: Campylobacter jejuni, 03 medical and health sciences, Bacterial Proteins, Humans, Molecular Biology, MESH: Humans, 030102 biochemistry & molecular biology, Active site, Campylobacter, Cell Biology, Periplasmic space, biology.organism_classification, AIR, ambiguous interaction restraint, CSP, chemical shift perturbation, Carboxypeptidase, 030104 developmental biology, chemistry, biology.protein, Biophysics, Peptidoglycan, MESH: Carboxypeptidases

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d0e0e23388d36bc0f74269c64db3c73
https://hal.science/hal-03328690

4

A Multipronged Screening Approach Targeting Inhibition of ETV6 PNT Domain Polymerization

المؤلفون: Chloe A. N. Gerak, Si Miao Zhang, Aruna D. Balgi, Michel Roberge, Lawrence P. McIntosh, Richard B. Sessions, Ivan Sadowski

المصدر: Gerak, C A N, Zhang, S M, Balgi, A D, Sadowski, I J, Sessions, R B, McIntosh, L P & Roberge, M 2020, ' A Multipronged Screening Approach Targeting Inhibition of ETV6 PNT Domain Polymerization ', SLAS Discovery . https://doi.org/10.1177/2472555220979599

مصطلحات موضوعية: cell-based assays, Mutant, protein-protein interactions, cancer and cancer drugs, 01 natural sciences, Biochemistry, Analytical Chemistry, Protein–protein interaction, 03 medical and health sciences, Transactivation, Structure-Activity Relationship, Protein-fragment complementation assay, Genes, Reporter, Drug Discovery, Humans, Luciferase, Protein Interaction Domains and Motifs, 030304 developmental biology, 0303 health sciences, Proto-Oncogene Proteins c-ets, 010405 organic chemistry, Chemistry, Autophosphorylation, Cooperative binding, computational chemistry, 0104 chemical sciences, Cell biology, Repressor Proteins, Docking (molecular), Molecular Medicine, Biological Assay, Drug Screening Assays, Antitumor, Protein Multimerization, Biotechnology, Protein Binding, yeast screening

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::834898b7b1063b5ea7d889a508beb87b
https://research-information.bris.ac.uk/en/publications/f052f786-df0e-48e7-b4b7-a9a5a7ddb4be

5

Ligand- and pH-Induced Structural Transition of Gypsy Moth

المؤلفون: Mailyn, Terrado, Mark, Okon, Lawrence P, McIntosh, Erika, Plettner

المصدر: Biochemistry. 59(37)

مصطلحات موضوعية: Protein Conformation, Animals, Insect Proteins, Stereoisomerism, Hydrogen-Ion Concentration, Moths, Carrier Proteins, Ligands, Pheromones, Protein Binding

URL الوصول: https://explore.openaire.eu/search/publication?articleId=pmid________::8bbe39c109c3a12bb0974ad4297177ef
https://pubmed.ncbi.nlm.nih.gov/32877603

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6

Biophysical characterization of the ETV6 PNT domain polymerization interfaces

المؤلفون: Mark Okon, Michael E. P. Murphy, Lawrence P. McIntosh, Michel Roberge, Chloe A. N. Gerak, Sophia Y. Cho, Maxim Kolesnikov, Richard B. Sessions

المصدر: The Journal of Biological Chemistry
et al. 2021, ' Biophysical characterization of the ETV6 PNT domain polymerization interfaces ', Journal of Biological Chemistry, vol. 296, 100284 . https://doi.org/10.1016/j.jbc.2021.100284

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Protein Conformation, alpha-Helical, Transcription, Genetic, Gene Expression, Crystallography, X-Ray, Biochemistry, protein-protein interaction, RMSD, root mean square deviation, Molecular dynamics, chemistry.chemical_compound, 0302 clinical medicine, biophysics, Surface plasmon resonance, Cloning, Molecular, 0303 health sciences, Alanine, PTK, protein tyrosine kinase, RCI-S2, random coil index-squared order parameter, Drug discovery, ETS, E26 transformation specific, Valine, Nuclear magnetic resonance spectroscopy, Alanine scanning, MD, molecular dynamics, Small molecule, Recombinant Proteins, hydrogen-deuterium exchange, SAM domain, ETS transcription factor family, 030220 oncology & carcinogenesis, EN, ETV6-NTRK3 fusion oncoprotein, Thermodynamics, Protein Binding, Research Article, Genetic Vectors, Glutamic Acid, SPR, surface plasmon resonance, HX, hydrogen exchange, Domain (software engineering), Protein–protein interaction, RMSF, root mean square fluctuation, 03 medical and health sciences, Escherichia coli, Humans, cancer, Protein Interaction Domains and Motifs, crystallography, Molecular Biology, 030304 developmental biology, Aspartic Acid, Binding Sites, 030102 biochemistry & molecular biology, Proto-Oncogene Proteins c-ets, alanine scanning mutagenesis, Mutagenesis, Cell Biology, PC, principal component, CSP, chemical shift perturbation, PF, protection factor, molecular dynamics, Repressor Proteins, nuclear magnetic resonance, 030104 developmental biology, Amino Acid Substitution, Polymerization, chemistry, Protein kinase domain, Mutation, Mutagenesis, Site-Directed, Biophysics, Protein Conformation, beta-Strand, Protein Multimerization, DNA