Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions?
about
Positioning of proteins in membranes: a computational approachStructure of lipid bilayersEcophysiology of omega Fatty acids: a lid for every jarInositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae.Interactions of cholesterol with lipid bilayers: the preferred configuration and fluctuationsInfluence of a lipid interface on protein dynamics in a fungal lipase.Abnormal aortic fatty acid composition and small artery function in offspring of rats fed a high fat diet in pregnancyHydrophobic mismatch and lipid sorting near OmpA in mixed bilayers: atomistic and coarse-grained simulations.Membrane thickness varies around the circumference of the transmembrane protein BtuB.Membrane hydrocarbon thickness modulates the dynamics of a membrane transport protein.Molecular dynamics study of MscL interactions with a curved lipid bilayer.Influence of trifluoroethanol on membrane interfacial anchoring interactions of transmembrane alpha-helical peptides.Interpretation of 2H-NMR experiments on the orientation of the transmembrane helix WALP23 by computer simulations.The gating mechanism of the bacterial mechanosensitive channel MscL revealed by molecular dynamics simulations: from tension sensing to channel openingCholesterol-induced protein sorting: an analysis of energetic feasibilitySimulations of a membrane-anchored peptide: structure, dynamics, and influence on bilayer properties.Transmembrane peptide-induced lipid sorting and mechanism of Lalpha-to-inverted phase transition using coarse-grain molecular dynamics.Spin-labeled gramicidin a: channel formation and dissociation.Lipid bilayer perturbations around a transmembrane nanotube: a coarse grain molecular dynamics study.Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers.Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: the role of dangerous unchaperoned molecules.The holin of bacteriophage lambda forms rings with large diameter.Construction of a yeast-based signaling biosensor for human angiotensin II type 1 receptor via functional coupling between Asn295-mutated receptor and Gpa1/Gi3 chimeric Gα.Model answers to lipid membrane questionsProtein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring.Synthetic peptides as models for intrinsic membrane proteins.Lipids, curvature, and nano-medicineEffects of antimicrobial peptides on methanogenic archaea.Changes of the membrane lipid organization characterized by means of a new cholesterol-pyrene probe.Membrane-protein interactions in a generic coarse-grained model for lipid bilayersMembrane protein integration into the endoplasmic reticulum.Selectivity in lipid binding to the bacterial outer membrane protein OmpF.Recent Progress in Advanced Nanobiological Materials for Energy and Environmental ApplicationsThe Ubiquitination of PINK1 Is Restricted to Its Mature 52-kDa Form.Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum.Segregation of photosystems in thylakoid membranes as a critical phenomenon.Analyzing heat capacity profiles of peptide-containing membranes: cluster formation of gramicidin A.Dependence of M13 major coat protein oligomerization and lateral segregation on bilayer composition.Quantification of Protein-Lipid Selectivity using FRET: Application to the M13 Major Coat Protein.Lipid bilayer topology of the transmembrane alpha-helix of M13 Major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy.
P2860
Q24647761-F9F12C5F-0FD7-4959-A2DD-2AE52324B20DQ24650796-C8988C02-8031-4FD9-8273-BFFEA841A7FEQ26859035-D5E8343E-E746-4BF0-879F-C245DE652EFEQ27932494-AE9AAD8E-81F9-4456-90CA-486D982441FDQ28344481-75C2ADCF-55AE-477D-82C3-7119AD86DE46Q28365099-061E18CD-47E0-48B2-B348-68136F01FC0AQ28366940-54A98357-94D7-4492-BDD1-749EC259D279Q30155297-1F14D251-807D-476F-B954-78E1A8319781Q30155833-B002C17F-0613-4A02-8FE5-0FB9E5900E0BQ30157654-733AD73A-20A0-4E4D-90B8-AD362A54064DQ30354792-D2380746-5576-4088-956D-AB21F28E06ABQ30364886-784ECA4B-314A-4406-9F3F-907816975A17Q30393287-D2E99D01-D4EA-41E8-9739-EFEF538F698AQ30423526-A6F23B1E-45D5-4C35-90E7-EFFD87707484Q34180735-A8CDFAF7-D193-4A35-9577-C9A4216A3E25Q34185967-A037018A-3548-4A10-AB05-D8AF2BAF2837Q34187229-19E7C5CE-BAA5-4BD2-B8B1-02A8A459EF4AQ34187789-3F73D5B1-EAFE-4DAA-9231-16FB21635D63Q34190585-502B7D6F-C00D-4F88-96E9-9D847B5735A1Q34385274-3B204C25-D4CE-4D91-A84C-FF7A3EF56D72Q34775436-FDC9B521-FA2F-445C-9818-1DA8049CE30DQ34826283-8A2E05BF-C7BB-4A72-B984-3FB4896D0739Q35180359-F43E981F-3356-4E1C-A39B-5B5885655A1BQ35234631-6C6A47FD-BEB5-4008-B6B6-3C42A329A895Q35567804-4C33234E-49A0-49EA-9062-22B7D7028A58Q35590020-3A3CFA0C-B9A9-4554-91A5-F0081204B157Q35590501-998C2973-45F3-411D-BDAC-1D6942145DBFQ36171501-78119F1D-5F8C-4109-B3D3-36293B1DBBEEQ36175900-593C584D-1AB9-4B78-85EB-6EDAD2FC4DF3Q37260324-C091657C-7D07-4CDB-8265-F63623C73F79Q37876968-DD0E439D-21B4-41D9-935F-909E6B5C2BE7Q38307751-0A024323-4877-4080-BD20-1C104A11DA62Q38633925-26E61E1C-2533-44D2-A719-1DA07484401CQ38690882-C5A4CDE7-8393-4A19-BCF3-B9C6D9CAF3ACQ39994820-654B8ACF-A7C5-4194-9D62-859273DCB30BQ40203784-0499E85F-DBA9-4817-A023-2082C1956C6BQ40233673-ABDC5000-C109-4C9D-823B-977C404A60EEQ40256279-A86FAB49-2792-4D42-A64A-C069E5852B6AQ40287991-D3C9A5F3-1160-4D5B-95A7-6F7933FF1B0FQ40295258-AEF5AF7E-6F92-4988-86F6-0FE774FC166B
P2860
Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions?
description
1999 nî lūn-bûn
@nan
1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Is the protein/lipid hydrophob ...... ne organization and functions?
@ast
Is the protein/lipid hydrophob ...... ne organization and functions?
@en
type
label
Is the protein/lipid hydrophob ...... ne organization and functions?
@ast
Is the protein/lipid hydrophob ...... ne organization and functions?
@en
prefLabel
Is the protein/lipid hydrophob ...... ne organization and functions?
@ast
Is the protein/lipid hydrophob ...... ne organization and functions?
@en
P2093
P2860
P1433
P1476
Is the protein/lipid hydrophob ...... ne organization and functions?
@en
P2093
P2860
P304
P356
10.1016/S0014-5793(99)01148-5
P407
P577
1999-09-01T00:00:00Z