نتائج البحث - "Membrane biology"

1

Free energies of membrane stalk formation from a lipidomics perspective

المؤلفون: Katharina C. Scherer, Jochen S. Hub, Chetan Poojari

المصدر: Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
Nature Communications

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea26e599b00d647cf44c11ef1ede8e80
https://doaj.org/article/7fe956e3d14d44cb821553921bcbe0b9

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2

Substitutions that lock and unlock the proton-coupled folate transporter (PCFT-SLC46A1) in an inward-open conformation

المؤلفون: Rongbao Zhao, Daniel Sanghoon Shin, Kai Lin, Andras Fiser, I. David Goldman, Srinivas Aluri

المصدر: J Biol Chem
The Journal of biological chemistry, vol 294, iss 18

مصطلحات موضوعية: 0301 basic medicine, Biochemistry & Molecular Biology, K), GXXXDXXGR(R, Protein Conformation, membrane transport, Glycine, proton-coupled folate transporter, folate, Medical and Health Sciences, Biochemistry, Intestinal absorption, folate malabsorption disease, Cell membrane, 03 medical and health sciences, Membrane Biology, medicine, Humans, Cysteine, Homology modeling, protein motif, Structural motif, Molecular Biology, structural model, 030102 biochemistry & molecular biology, Chemistry, solute carrier family 46 member 1, Transporter, Cell Biology, Biological Sciences, Membrane transport, GXXXDXXGR(R/K), Kinetics, Transmembrane domain, 030104 developmental biology, medicine.anatomical_structure, Hela Cells, transporter, Chemical Sciences, Mutation, Biophysics, Generic health relevance, Proton-Coupled Folate Transporter, Intracellular, HeLa Cells

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::607294eda5c98afb5c0e4647cfb75cf3
https://doi.org/10.1074/jbc.ra118.005533

3

Phosphoserine acidic cluster motifs bind distinct basic regions on the μ subunits of clathrin adaptor protein complexes

المؤلفون: Richard T. Wyatt, Christopher Lim, Rajendra Singh, Charlotte A. Stoneham, Joel O. Wertheim, John C. Guatelli, Xiaofei Jia, Javier Guenaga, Yong Xiong

المصدر: Journal of Biological Chemistry
The Journal of biological chemistry, vol 293, iss 40

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Phosphatidylinositol 4,5-Diphosphate, Protein Conformation, alpha-Helical, Protein Conformation, Amino Acid Motifs, Human Immunodeficiency Virus Proteins, Sequence Homology, Gene Expression, acidic cluster, nef Gene Products, host-pathogen interaction, Biochemistry, Medical and Health Sciences, medium subunit, chemistry.chemical_compound, Jurkat Cells, Phosphoserine, Models, Receptors, Viral Regulatory and Accessory Proteins, Cloning, Molecular, Furin, Mammals, Membrane Glycoproteins, biology, human immunodeficiency virus, Chemistry, Serinc3, phosphorylation, membrane trafficking, Signal transducing adaptor protein, Biological Sciences, Transmembrane protein, Recombinant Proteins, Cell biology, Neoplasm Proteins, Phosphatidylinositol 4, Amino Acid, Infectious Diseases, 5-Diphosphate, Cell Surface, Casein kinase 2, Infection, Protein Binding, Biochemistry & Molecular Biology, protein chemistry, Endosome, Protein subunit, 1.1 Normal biological development and functioning, Adaptor Protein Complex 1, Adaptor Protein Complex 2, Receptors, Cell Surface, Clathrin, 03 medical and health sciences, clathrin, Underpinning research, Membrane Biology, Escherichia coli, Animals, Humans, Protein Interaction Domains and Motifs, nef Gene Products, Human Immunodeficiency Virus, Molecular Biology, Binding Sites, Sequence Homology, Amino Acid, protein complex, alpha-Helical, HIV-1 Vpu, Virion, Molecular, Cell Biology, Kinetics, Protein Subunits, 030104 developmental biology, Chemical Sciences, biology.protein, HIV-1, beta-Strand, Protein Conformation, beta-Strand, Sequence Alignment, Cloning, adaptor protein

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a684e54e7fffd361573395d82fc20d28

4

Modulation of non-bilayer lipid phases and the structure and functions of thylakoid membranes: effects on the water-soluble enzyme violaxanthin de-epoxidase

المؤلفون: Václav Karlický, Sashka Krumova, Primož Šket, Irena Kurasová, Uroš Javornik, Ondřej Dlouhý, Bettina Ughy, Győző Garab, Janez Plavec, Nia Petrova, Vladimír Špunda

المصدر: Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-13 (2020)

مصطلحات موضوعية: 0106 biological sciences, 0301 basic medicine, Magnetic Resonance Spectroscopy, Light, Lipid Bilayers, Biophysics, Membrane biology, lcsh:Medicine, Xanthophylls, Thylakoids, Biochemistry, 01 natural sciences, Violaxanthin de-epoxidase, Article, 03 medical and health sciences, chemistry.chemical_compound, Spinacia oleracea, Polymorphism (biophysics), lcsh:Science, Multidisciplinary, Calorimetry, Differential Scanning, Chemistry, Bilayer, lcsh:R, Temperature, Water, Biological membrane, Hydrogen-Ion Concentration, Lipids, Kinetics, 030104 developmental biology, Membrane, Solubility, Thylakoid, Epoxy Compounds, lcsh:Q, lipids (amino acids, peptides, and proteins), Oxidoreductases, Plant sciences, Structural biology, 010606 plant biology & botany, Violaxanthin

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a131951b4b9189e3f3e6a255b2a5f530
https://doi.org/10.1038/s41598-020-68854-x

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5

Nanomolar ATP binding to single myosin cross-bridges in rigor: a molecular approach to studying myosin ATP kinetics using single human cardiomyocytes

المؤلفون: Roger Cooke, Elvis Pandzic, Amy Li, Christian A. Morkel, Cristobal G. dos Remedios, Renee Whan

المصدر: Biophys Rev

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8564528c393351656cb5e7b52d83070d
https://pubmed.ncbi.nlm.nih.gov/32648209

6

The protein-surfactant stoichiometry governs the conformational switching and amyloid nucleation kinetics of tau K18

المؤلفون: Anjali Giri, Jaspreet Kaur, Mily Bhattacharya

المصدر: European biophysics journal : EBJ. 49(6)

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc0140c3081e7aaea2f9f6c1ff2d1610
https://pubmed.ncbi.nlm.nih.gov/32691116

7

The human Golgi protein TMEM165 transports calcium and manganese in yeast and bacterial cells

المؤلفون: Philippe Goffin, Louise Thines, Antoine Deschamps, Pierre Morsomme, Jiri Stribny

المساهمون: UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology

المصدر: J Biol Chem
The Journal of Biological Chemistry, Vol. 295, no. 12, p. 3865-3874 (2020)

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d83cb35728bf7baec9c10c34235dc54
https://europepmc.org/articles/PMC7086029/

8

Kinetics of irreversible pore formation under constant electrical tension in giant unilamellar vesicles

المؤلفون: Marzuk Ahmed, Md. Kabir Ahamed, Shareef Ahammed, Mohammad Abu Sayem Karal

المصدر: European biophysics journal : EBJ. 49(5)

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfef87c192a88882813c7dee930395e9
https://pubmed.ncbi.nlm.nih.gov/32591856

9

A twin histidine motif is the core structure for high-affinity substrate selection in plant ammonium transporters

المؤلفون: Benjamin Neuhäuser, Nils Stührwohldt, Toyosi Ijato, Pascal Ganz, Uwe Ludewig, Romano Porras-Murrilo

المصدر: J Biol Chem

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d362eecec981f428a489ad38eb072a68
https://europepmc.org/articles/PMC7062152/

10

Cry6Aa1, a Bacillus thuringiensis nematocidal and insecticidal toxin, forms pores in planar lipid bilayers at extremely low concentrations and without the need of proteolytic processing

المؤلفون: Xiaoping Xu, David McCaskill, Vimbai M. Chikwana, Sek Yee Tan, Thimothy Hey, Eva Fortea, Léna Potvin, Jean-Louis Schwartz, Vincent Vachon, Vincent Lemieux, Samantha Griffin, Kenneth E. Narva

المصدر: Journal of Biological Chemistry. 292:13122-13132

مصطلحات موضوعية: 0301 basic medicine, Insecticides, medicine.medical_treatment, Lipid Bilayers, Bacillus thuringiensis, Biology, medicine.disease_cause, Membrane Fusion, Biochemistry, Activation, Metabolic, Hemolysin Proteins, 03 medical and health sciences, Bacterial Proteins, Membrane Biology, medicine, Animals, Mode of action, Molecular Biology, Pore-forming toxin, Protease, Bacillus thuringiensis Toxins, Microvilli, 030102 biochemistry & molecular biology, Toxin, Antinematodal Agents, Midgut, Cell Biology, Hydrogen-Ion Concentration, Trypsin, biology.organism_classification, Recombinant Proteins, Coleoptera, Endotoxins, Kinetics, 030104 developmental biology, Membrane, Solubility, Larva, Proteolysis, Insect Proteins, Digestion, Porosity, Peptide Hydrolases, medicine.drug

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abd68c2a459a1af13c96fd8e4ca5c7a4
https://doi.org/10.1074/jbc.m116.765941

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