Gramicidin channel kinetics under tension. - Wikidata - awgldk - TriplyDB

Gramicidin channel kinetics under tension.

Gramicidin channel kinetics under tension.

http://www.wikidata.org/entity/Q34167113

about

Hydrophobic mismatch between helices and lipid bilayers.Membrane-protein interactions in mechanosensitive channels Stretch-activated ion channels: what are they?Analytic models for mechanotransduction: gating a mechanosensitive channel Mechanically gated channel activity in cytoskeleton-deficient plasma membrane blebs and vesicles from Xenopus oocytes Mechanosensitive ion channels and the peptide inhibitor GsMTx-4: history, properties, mechanisms and pharmacology The Application of Micropipette Aspiration in Molecular Mechanics of Single Cells Electrostatically induced recruitment of membrane peptides into clusters requires ligand binding at both interfaces Structure and hydration of membranes embedded with voltage-sensing domains.Theoretical analysis of hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin.Small substrate transport and mechanism of a molybdate ATP binding cassette transporter in a lipid environment.Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes A one-dimensional continuum elastic model for membrane-embedded gramicidin dimer dissociation.Gramicidin A channels switch between stretch activation and stretch inactivation depending on bilayer thickness Simulation study of a gramicidin/lipid bilayer system in excess water and lipid. I. Structure of the molecular complex.Distinctly different interactions of anesthetic and nonimmobilizer with transmembrane channel peptides.Asymmetrical membranes and surface tension Gating gramicidin channels in lipid bilayers: reaction coordinates and the mechanism of dissociation.The influence of short-chain alcohols on interfacial tension, mechanical properties, area/molecule, and permeability of fluid lipid bilayers Osmotic stress mechanically perturbs chemoreceptors in Escherichia coli A consistent model for thermal fluctuations and protein-induced deformations in lipid bilayers Volatile anesthetics inhibit sodium channels without altering bulk lipid bilayer properties.How did cells get their size?Thiazolidinedione insulin sensitizers alter lipid bilayer properties and voltage-dependent sodium channel function: implications for drug discovery Emerging roles for lipids in shaping membrane-protein function.Contributions of Gaussian curvature and nonconstant lipid volume to protein deformation of lipid bilayers.Influence of hydrophobic mismatch on structures and dynamics of gramicidin a and lipid bilayers.Bioactive cell-like hybrids coassembled from (glyco)dendrimersomes with bacterial membranes Swimming through the hydrophobic sea: new insights in protein translocation.A general mechanism for drug promiscuity: Studies with amiodarone and other antiarrhythmics Membrane cholesterol content modulates activation of volume-regulated anion current in bovine endothelial cells.Assessing smectic liquid-crystal continuum models for elastic bilayer deformations.Toward understanding protocell mechanosensation.Divergent effects of anesthetics on lipid bilayer properties and sodium channel function.Dynamic Heterogeneous Dielectric Generalized Born (DHDGB): An implicit membrane model with a dynamically varying bilayer thickness.Effect of lipid characteristics on the structure of transmembrane proteins.Desformylgramicidin: a model channel with an extremely high water permeability.Voltage-dependent formation of gramicidin channels in lipid bilayers.Simultaneous optical and electrical recording of single gramicidin channels.Bilayer elasticity at the nanoscale: the need for new terms.

P2860

Q24537600-9D0C24EE-2C3D-4F5F-8E1F-08667FA46405 Q24538186-BF7F14B1-8019-4D85-91F7-AE2E77D5CF5B Q24630314-CF9365F0-1C48-469B-A31E-D7193E940028 Q24633961-FE5534ED-FC3D-4DFB-979C-175EB4F5B380 Q24651184-65184582-46F5-4205-B7CE-829C20B017A7 Q24683241-F332C5E9-C456-4E22-AF05-98B62ED8A3EB Q27002348-CB21C43A-4A2C-444F-95B5-0A011A123D5C Q31110240-412BE711-3509-4878-AB95-07777D6782E4 Q33516691-87CDFAFB-B522-418E-A712-4088034296CC Q33650410-60EBFB1D-BE65-4E71-9B96-88B91367C403 Q33652199-626DBA0D-3E6F-46DD-9FD9-2EDFCBF650E7 Q33743375-348E6984-DD43-4073-B5FB-87D21936108C Q33822097-251BFDE2-7256-4271-BB84-7EEE6F1DABC8 Q34047621-BE73046F-FC17-4377-BF9A-87EDF548511A Q34170178-2DC1249D-8EDA-4408-88E0-8177DD86FCBB Q34170976-61A52F5B-4CAF-47D5-A54C-2D1D994AF535 Q34178697-03B6C1CF-C76A-4FAE-8103-D6949AE62131 Q34184441-2FC1829F-1A4B-481E-BD30-EE0AD28531E0 Q34186540-14CBB186-62E7-40BD-8CA3-3D05C566E993 Q34270957-E7C38168-8302-4ADC-8305-ED08B89B3BD1 Q34354216-49B598A3-5165-475D-B7AD-7A924A765B9C Q34566656-1A87945F-956B-4D76-98EA-88CB48C02E9D Q34968961-2D0B8E59-F5D6-4F3B-8AA1-FD0F6BA6B3BC Q35146426-E263B13F-4D1A-4CB7-8587-64337C250F76 Q35203586-08C8621E-BBC8-4030-938E-A234F4FDD63E Q35606801-ECF40616-B0F7-4FCD-8639-5D0E67BEAF1D Q35866803-046678FF-6303-4BD2-B852-5F5FCCDC43EA Q35925587-BF4AF472-A477-4239-B305-F8FCA2D864DE Q36184669-BFC7645E-DDBD-4C49-BC7F-129B9F66EE8C Q36333201-DFC48E12-7D22-42D8-9E9E-C7D08298D359 Q36444953-B9D85E4A-1E11-40C9-89DF-123115C7F1A8 Q37061604-E385384A-2BFA-474D-9A8F-67431AC6C326 Q37809771-B04AC3DB-896C-4C6E-874A-7EAD033D0AA4 Q39427465-9BEB8C99-939E-4C3C-A0A2-68BFB8CCF196 Q39740337-AE25D793-D317-4763-9E9E-49ECE97094FC Q40128431-9E8921AD-8168-4FB1-8B7E-7FCD2B239810 Q40173545-4ACECEF1-5D52-4CF7-80A5-F692EEAF7DE7 Q40187614-A31A2C03-FEA2-428F-B0CA-19ACAFF38FCA Q40227721-8DF25DBB-9A49-4A2F-B23F-6FDBB780ADEF Q41329418-F5A3AD50-A12C-4BAF-B72B-80DD17B3D230

P2860

Gramicidin channel kinetics under tension.

http://www.wikidata.org/entity/Q34167113

description

1998 nî lūn-bûn

@nan

1998 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի հունվարին հրատարակված գիտական հոդված

@hy

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

Gramicidin channel kinetics under tension.

@ast

Gramicidin channel kinetics under tension.

@en

Gramicidin channel kinetics under tension.

@nl

type

label

Gramicidin channel kinetics under tension.

@ast

Gramicidin channel kinetics under tension.

@en

Gramicidin channel kinetics under tension.

@nl

prefLabel

Gramicidin channel kinetics under tension.

@ast

Gramicidin channel kinetics under tension.

@en

Gramicidin channel kinetics under tension.

@nl

P1433

Q34167113-BBDADF9C-B503-4824-AA16-BA507B7E4C40

P1476

Q34167113-C579D301-01EE-428B-BD06-2081E92E4D90

P2093

Q34167113-2369E58C-0319-4F8D-85DA-BDCDD2E4E8B8

Q34167113-3316C28F-85DF-407B-9ADB-0EE29FC187FF

Q34167113-9F1C5595-C994-4F50-93E3-1D5572DB18A8

Q34167113-C2286A1D-EA89-4DB2-BA88-A6BD945F2304

Q34167113-CFF51695-B0A4-4211-BD02-57E42D8E612B

Q34167113-D9C18F1C-4F9E-496C-98F7-9FA03FB43D61

P2860

Q34167113-04420CE1-8538-4CEA-8527-911010A97B15

Q34167113-0C46957A-E4FC-4130-83AC-42C79B883841

Q34167113-1DD32351-2F8C-4B4E-AA88-EE2F6F1C5D54

Q34167113-2847B26E-AF7F-47BE-B16B-262DA9769BEA

Q34167113-284F0A13-20D5-454A-B4B3-9FDB55DFC2AB

Q34167113-28C13DA6-1285-4C29-A8B6-3CFAD19D6D4C

Q34167113-3B4CE7E5-0C92-4410-8740-8FF20E8A9858

Q34167113-40658A66-5B9F-43A3-844E-57D8B288E2EB

Q34167113-40B45F66-5B62-4710-942D-BF0417F2F92F

Q34167113-4B6919D2-076D-4C28-888A-E28419BC4FF2

P304

Q34167113-745ADA98-620E-48EA-A6B9-6334BCF00BD9

P31

Q34167113-9DDA7ADB-A76C-4655-9010-F16C70E503D8

P356

Q34167113-ECBE2426-1E0E-42EE-A4E5-777152671A27

P407

Q34167113-9CC90A82-F006-43C5-8C77-D3E1CB37D250

P433

Q34167113-7EE020FB-3E35-4D49-85D7-163ABA36B876

P478

Q34167113-C587ABED-B236-46EA-A040-81539E3822AE

P577

Q34167113-01DDD1C6-874F-47C9-AFA5-E6DFA338A58D

P5875

Q34167113-03AFFFB6-05D7-4DD2-A946-0C1BF0326B7D

P698

Q34167113-C68040A6-FDA0-46A2-AC95-805A08196E3E

P932

Q34167113-F140C283-B964-4F30-9032-105040C2E1A5

P356

S0006-3495(98)77790-2

P1433

Biophysical Journal

P1476

Gramicidin channel kinetics under tension.

@en

P2093

A Libchaber

http://www.w3.org/2001/XMLSchema#string

C Nielsen

http://www.w3.org/2001/XMLSchema#string

D K Fygenson

http://www.w3.org/2001/XMLSchema#string

M Goulian

http://www.w3.org/2001/XMLSchema#string

O N Mesquita

http://www.w3.org/2001/XMLSchema#string

O S Andersen

http://www.w3.org/2001/XMLSchema#string

P2860

Lipid bilayer electrostatic energy, curvature stress, and assembly of gramicidin channels.

Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles.

On the supramolecular organization of gramicidin channels. The elementary conducting unit is a dimer

Transduction of membrane tension by the ion channel alamethicin.

Calculation of deformation energies and conformations in lipid membranes containing gramicidin channels.

Ion movement through gramicidin A channels. Single-channel measurements at very high potentials.

Thermoelasticity of large lecithin bilayer vesicles.

Deformation free energy of bilayer membrane and its effect on gramicidin channel lifetime

Lysophospholipids modulate channel function by altering the mechanical properties of lipid bilayers

Simultaneous fluorescence and conductance studies of planar bilayer membranes containing a highly active and fluorescent analog of gramicidin A.

P304

328-337

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/S0006-3495(98)77790-2

http://www.w3.org/2001/XMLSchema#string

P407

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

74

http://www.w3.org/2001/XMLSchema#string

P577

1998-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

13782045

http://www.w3.org/2001/XMLSchema#string

P698

9449333

http://www.w3.org/2001/XMLSchema#string

P932

1299385

http://www.w3.org/2001/XMLSchema#string