Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles. Binding mechanism and thermodynamic analysis.
about
Inhibition of mitochondrial neural cell death pathways by protein transduction of Bcl-2 family proteinsEnhanced cell-permeant Cre protein for site-specific recombination in cultured cellsCationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMRMolecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes.Single quantum dot tracking reveals that an individual multivalent HIV-1 Tat protein transduction domain can activate machinery for lateral transport and endocytosis.A critical reassessment of penetratin translocation across lipid membranesOrientation, dynamics, and lipid interaction of an antimicrobial arylamide investigated by 19F and 31P solid-state NMR spectroscopy.Membrane-bound dynamic structure of an arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR.Viewing membrane-bound molecular umbrellas by parallax analyses.A new family of peptide-nucleic acid nanostructures with potent transfection activities.Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR.Label-free probe of HIV-1 TAT peptide binding to mimetic membranes.Interaction of the protein transduction domain of HIV-1 TAT with heparan sulfate: binding mechanism and thermodynamic parameters.Cell-penetrating peptide induces leaky fusion of liposomes containing late endosome-specific anionic lipid.Translocation of HIV TAT peptide and analogues induced by multiplexed membrane and cytoskeletal interactions.Electrochemical impedimetric biosensor based on a nanostructured polycarbonate substrate.HIV-1 Tat membrane interactions probed using X-ray and neutron scattering, CD spectroscopy and MD simulationsBreak on through to the other side-biophysics and cell biology shed light on cell-penetrating peptides.Bioconjugate-based molecular umbrellas.Alternative mechanisms for the interaction of the cell-penetrating peptides penetratin and the TAT peptide with lipid bilayers.Relevance of biophysical interactions of nanoparticles with a model membrane in predicting cellular uptake: study with TAT peptide-conjugated nanoparticles.Cell penetrating peptides: how do they do it?Arginine-rich cell-penetrating peptides.Stability of peptides and therapeutic success in cancer.Exploring transduction mechanisms of protein transduction domains (PTDs) in living cells utilizing single-quantum dot tracking (SQT) technologyIntracellular transduction and potential of Tat PTD and its analogs: from basic drug delivery mechanism to application.Amphiphilic macromolecules on cell membranes: from protective layers to controlled permeabilization.Intranasal and intravenous administration of octa-arginine modified poly(lactic-co-glycolic acid) nanoparticles facilitates central nervous system delivery of loperamide.Cell-Penetrating Peptides-Mechanisms of Cellular Uptake and Generation of Delivery Systems.Single particle tracking confirms that multivalent Tat protein transduction domain-induced heparan sulfate proteoglycan cross-linkage activates Rac1 for internalization.Analysis of the selective advantage conferred by a C-E1 fusion protein synthesized by rubella virus DI RNAs.Temperature-, concentration- and cholesterol-dependent translocation of L- and D-octa-arginine across the plasma and nuclear membrane of CD34+ leukaemia cells.Comparison of NMR structures and model-membrane interactions of 15-residue antimicrobial peptides derived from bovine lactoferricin.Novel human-derived cell-penetrating peptides for specific subcellular delivery of therapeutic biomolecules.Peptide-linked molecular beacons for efficient delivery and rapid mRNA detection in living cells.Receptor/transporter-independent targeting of functional peptides across the plasma membrane.Effect of lipid headgroup charge and pH on the stability and membrane insertion potential of calcium condensed gene complexes.Modulation of muscle contraction by a cell-permeable peptide.Global structural rearrangement of the cell penetrating ribonuclease colicin E3 on interaction with phospholipid membranes.Molecular dynamics studies of transportan 10 (tp10) interacting with a POPC lipid bilayer.
P2860
Q24324220-23B953E2-A172-4A52-B98D-FA644205BADDQ24797478-D3EE9C54-09DD-4D79-A937-355DEFC717BEQ26830018-DF10DE0C-73F6-47E9-8C8D-7393E82D3E53Q30482157-9232C1F2-EBBC-4D1C-9B53-0ADE68D28DE9Q30541727-CADED247-B92F-42B3-A9DD-CD4085231C03Q33220250-863E148A-1173-4921-94C1-4B38BD2C76FDQ33599984-ECAC02B5-9170-4E09-9AE0-7FDAC4041CC6Q33605186-9C4B20D8-B92B-4058-B58A-55E13ACEB465Q33656504-4DFB65A3-F824-4F08-955E-1358005D6DF9Q33793286-0747B922-AC0F-42D5-8593-72D829DD0E56Q33827462-C66EDEE4-8C08-4B2E-9888-E47405D5F116Q34144630-AC1C9C14-6211-41C2-ACCF-B290F6A7622EQ34184281-45DC0CF8-0AFB-486A-8DEB-07C825756BC6Q34202149-CA12A05B-FCB6-42D5-B38F-7FEBEE7FC984Q35345277-4CEA7406-C354-43F2-AC22-F05DF64D4E72Q35679874-249BE839-0FE6-4ECF-9F3B-94DC54CBB004Q36175053-7748B44B-1332-4804-AF61-DF111A4685D2Q36299512-42FB0E0E-B664-4C0A-BB64-2340E6F82EEAQ37171368-8860A222-7CA5-4E64-BE73-CFF72E6DD25BQ37263388-6996FE0C-E71F-479E-9813-5BDE5C9B1A15Q37376298-215E6B0E-C43D-40DA-9DE8-CA9D32FB6DE2Q37577592-4998AB80-E308-436D-A267-2F6F315290F0Q37635334-DECCF712-4D5A-405B-974A-6BB3C8C7DDADQ37860343-C65742C7-27D3-4B2E-8DD3-F23BE721B245Q37988482-0487B3B9-95A1-4E64-BDB4-C8B76181ED24Q37995239-EF133D9E-FA6E-4CB2-A962-FFA6FFFE6235Q38218038-7196B4D9-6E47-43F1-9968-05536CC53399Q38927932-388AF514-0CE0-44B8-80CB-8280DC126257Q38974236-7E233A59-D44E-4B27-BDD3-799F670BF747Q39797374-13F714E8-21A3-4BB4-8BD3-908E5429B6ACQ40094395-A707AF6F-D58E-4DE4-92D1-CCF0A317ADF4Q40184296-603415A2-C813-4C5E-B9E6-06A04C028D0FQ40293709-00DE6F14-210E-4826-9B75-27B17741577FQ40429544-F94EE3E7-007F-43F1-A696-BDC3DB77267FQ40566768-9ED8531E-DB1C-44F8-9D7B-D9011DE411C9Q40603207-A76D7EBB-597E-4BB7-8F67-C6BD91C6AE38Q41229373-DB07FFDB-FAE6-4619-BFE3-568779412960Q42122403-C6ABDD26-FFB3-4CDC-80D4-C77BD41938F9Q42264439-6F2FE87F-5DC4-4D33-BBB1-4EC9DFEFA599Q42604173-C6BA7656-AE46-48BE-9CF3-2C0D53554746
P2860
Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles. Binding mechanism and thermodynamic analysis.
description
2003 nî lūn-bûn
@nan
2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Protein transduction domains o ...... sm and thermodynamic analysis.
@ast
Protein transduction domains o ...... sm and thermodynamic analysis.
@en
type
label
Protein transduction domains o ...... sm and thermodynamic analysis.
@ast
Protein transduction domains o ...... sm and thermodynamic analysis.
@en
prefLabel
Protein transduction domains o ...... sm and thermodynamic analysis.
@ast
Protein transduction domains o ...... sm and thermodynamic analysis.
@en
P2093
P356
P1433
P1476
Protein transduction domains o ...... sm and thermodynamic analysis.
@en
P2093
André Ziegler
Anna Seelig
Joachim Seelig
Xiaochun Li Blatter
P304
P356
10.1021/BI0346805
P407
P577
2003-08-01T00:00:00Z