(Q33605186)

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Membrane-bound dynamic structure of an arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR.

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20550193%20AND%20SRC:MED&resulttype=core&format=json

5 February 2020

Membrane-bound dynamic structure of an arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR (English)

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5 February 2020

1

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5 February 2020

3

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5 February 2020

4

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5 February 2020

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Alan J Waring

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5 February 2020

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1 July 2010

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5 February 2020

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5 February 2020

49

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5 February 2020

29

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5 February 2020

6009-6020

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Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20550193%20AND%20SRC:MED&resulttype=core&format=json

5 February 2020

Real-time multidimensional NMR follows RNA folding with second resolution

1 reference

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Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy.

1 reference

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Roles of arginine and lysine residues in the translocation of a cell-penetrating peptide from (13)C, (31)P, and (19)F solid-state NMR.

1 reference

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Protein side-chain dynamics and residual conformational entropy

1 reference

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2D 1H-31P solid-state NMR studies of the dependence of inter-bilayer water dynamics on lipid headgroup structure and membrane peptides

1 reference

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Reversible sheet-turn conformational change of a cell-penetrating peptide in lipid bilayers studied by solid-state NMR

1 reference

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Polarization transfer over the water-protein interface in solids

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Asymmetric insertion of membrane proteins in lipid bilayers by solid-state NMR paramagnetic relaxation enhancement: a cell-penetrating Peptide example

1 reference

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1 reference

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Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes

1 reference

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Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR.

1 reference

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21 June 2018

Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR.

1 reference

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1 reference

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21 June 2018

Break on through to the other side-biophysics and cell biology shed light on cell-penetrating peptides

1 reference

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Interface connections of a transmembrane voltage sensor

1 reference

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Tat peptide-mediated cellular delivery: back to basics

1 reference

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Adaptive translocation: the role of hydrogen bonding and membrane potential in the uptake of guanidinium-rich transporters into cells

1 reference

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Recognition of transmembrane helices by the endoplasmic reticulum translocon.

1 reference

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21 June 2018

Penetratin-membrane association: W48/R52/W56 shield the peptide from the aqueous phase.

1 reference

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Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes.

1 reference

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Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles. Binding mechanism and thermodynamic analysis

1 reference

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21 June 2018

An innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies

1 reference

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Membrane protein folding and stability: physical principles

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Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results

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Experimentally determined hydrophobicity scale for proteins at membrane interfaces

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1 reference

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Effects of guanidinium-phosphate hydrogen bonding on the membrane-bound structure and activity of an arginine-rich membrane peptide from solid-state NMR spectroscopy

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1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein transduction domain of HIV-1 Tat protein promotes efficient delivery of DNA into mammalian cells

1 reference

https://pubmed.ncbi.nlm.nih.gov/20550193

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A Truncated HIV-1 Tat Protein Basic Domain Rapidly Translocates through the Plasma Membrane and Accumulates in the Cell Nucleus

1 reference

https://pubmed.ncbi.nlm.nih.gov/20550193

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1021/BI100642N

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20550193%20AND%20SRC:MED&resulttype=core&format=json

5 February 2020

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24 November 2022

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5 February 2020

PubMed publication ID

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Europe PubMed Central

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5 February 2020

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