Fluorescence approaches for determining protein conformations, interactions and mechanisms at membranes.
about
ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formationRicin A chain insertion into endoplasmic reticulum membranes is triggered by a temperature increase to 37 {degrees}CFunctional reconstitution of ESCRT-III assembly and disassembly.Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysinsDisulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel.Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission.Label-free measuring and mapping of binding kinetics of membrane proteins in single living cellsGenetic selection for a highly functional cysteine-less membrane protein using site saturation mutagenesisCellular mechanisms of membrane protein folding.Efficient isolation of Pseudomonas aeruginosa type III secretion translocators and assembly of heteromeric transmembrane pores in model membranes.Interaction of the Spo20 membrane-sensor motif with phosphatidic acid and other anionic lipids, and influence of the membrane environmentConformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.α-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding.Stepwise insertion and inversion of a type II signal anchor sequence in the ribosome-Sec61 translocon complex.Polytopic membrane protein folding at L17 in the ribosome tunnel initiates cyclical changes at the transloconTransmembrane segments of nascent polytopic membrane proteins control cytosol/ER targeting during membrane integrationArginine changes the conformation of the arginine attenuator peptide relative to the ribosome tunnelFluorescent resonance energy transfer: A tool for probing molecular cell-biomaterial interactions in three dimensionsThe expanding role of the ER translocon in membrane protein folding.Fluorescence spectroscopy of protein oligomerization in membranes.Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides.Determination of the Membrane Translocation pK of the pH-Low Insertion Peptide.The two sides of a lipid-protein story.Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta.Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system.tBid elicits a conformational alteration in membrane-bound Bcl-2 such that it inhibits Bax pore formationReal-time detection reveals that effectors couple dynamin's GTP-dependent conformational changes to the membrane.The biochemical characterization, stabilization studies and the antiproliferative effect of bromelain against B16F10 murine melanoma cells.Time-of-flight ion mobility spectrometry in combination with laser-induced fluorescence detection system.
P2860
Q24629620-BDA68A17-ED6D-49C2-A700-19B6180954C1Q24647411-FA3A3433-FF89-4329-88E1-0E47E4129D9BQ27935900-91E5A23B-AF34-41CF-A2C1-7AE5F78CA0F0Q30153399-9452F43E-596A-46BD-BC0D-380B72FC650BQ30155117-06695A0A-FDE6-4A93-96B0-A589D037336FQ30491655-EAAD4442-7826-4E46-BD54-FB511F916EF0Q30539992-6829C07C-9EEB-4451-9B2A-73EC942DF19AQ33283772-03AEC778-38D3-4470-A551-D9B8F8E16330Q33624056-6F6FB344-854A-41A0-B57C-6FD76A798E2CQ33965276-C89DD9BB-08CB-4EB7-9680-FA3C9B22DEB8Q34449682-2EAB6650-CCDF-4DD4-821B-2AA452BF95AFQ34635171-8ADC42DD-B148-4C5F-8F07-736E55950EDAQ35102466-7257488F-B25F-411F-9422-3AF5468DD9EEQ35235093-F3E15810-C36A-48CA-BADF-0E5C41D970FAQ35276847-E7CB06D9-1AA8-4D8A-9B54-D5E9504631CEQ35276891-122034E4-D51C-4386-B3B1-EB3DF87DD0C8Q36600266-CDBA1ACE-65CC-4521-93D2-CADEEC85BD5DQ36725463-AB76F8AB-B6DE-4269-82EA-A42CF122C4FFQ37048115-D1F9DA2B-0106-4E6D-81A0-5218B5702D95Q37725710-7D0D8FB9-DF68-4126-BD75-9CDF2C57F284Q37876360-315BA18B-15B8-4F1B-ABCA-57F82A5EF2D7Q38611561-D76F9D77-2852-4FEE-A2A0-EA2D2351E3BBQ39310476-5A4C3B35-1EF9-415D-9C9D-F91A7B804E28Q41276700-884638D2-A2D2-493D-9394-F39BC6D4A0EEQ41785201-73DF3377-5A8F-400D-A3D7-5488E2AC43A2Q42222161-6D861B88-D2E4-4A42-ACD3-00A97D95D242Q42963198-A7300E01-3188-476F-9686-CAEC432931C7Q43356634-40A5C71B-D854-43A7-A1F1-E3DACC8A96C8Q47914104-226EC33B-7712-4A1B-B42E-7E3F26E200CE
P2860
Fluorescence approaches for determining protein conformations, interactions and mechanisms at membranes.
description
2005 nî lūn-bûn
@nan
2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
name
Fluorescence approaches for de ...... s and mechanisms at membranes.
@ast
Fluorescence approaches for de ...... s and mechanisms at membranes.
@en
Fluorescence approaches for de ...... s and mechanisms at membranes.
@nl
type
label
Fluorescence approaches for de ...... s and mechanisms at membranes.
@ast
Fluorescence approaches for de ...... s and mechanisms at membranes.
@en
Fluorescence approaches for de ...... s and mechanisms at membranes.
@nl
prefLabel
Fluorescence approaches for de ...... s and mechanisms at membranes.
@ast
Fluorescence approaches for de ...... s and mechanisms at membranes.
@en
Fluorescence approaches for de ...... s and mechanisms at membranes.
@nl
P1433
P1476
Fluorescence approaches for de ...... s and mechanisms at membranes.
@en
P2093
Arthur E Johnson
P304
P356
10.1111/J.1600-0854.2005.00340.X
P577
2005-12-01T00:00:00Z