Increased Hydrophobic Block Length of PTDMs Promotes Protein Internalization.

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ROMP- and RAFT-Based Guanidinium-Containing Polymers as Scaffolds for Protein Mimic Synthesis.

P2860

Q48331952-D0D30EB6-3B3B-465D-BC9C-8B32FAD23A46

P2860

Increased Hydrophobic Block Length of PTDMs Promotes Protein Internalization.

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http://www.wikidata.org/entity/Q44090492

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年學術文章

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2016年學術文章

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Increased Hydrophobic Block Length of PTDMs Promotes Protein Internalization.

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Increased Hydrophobic Block Length of PTDMs Promotes Protein Internalization.

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Item

label

Increased Hydrophobic Block Length of PTDMs Promotes Protein Internalization.

@en

Increased Hydrophobic Block Length of PTDMs Promotes Protein Internalization.

@nl

prefLabel

Increased Hydrophobic Block Length of PTDMs Promotes Protein Internalization.

@en

Increased Hydrophobic Block Length of PTDMs Promotes Protein Internalization.

@nl

P1476

Increased Hydrophobic Block Length of PTDMs Promotes Protein Internalization.

@en

P2093

Federica Sgolastra

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

Gregory N Tew

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

Lisa Minter

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

Ronja Otter

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

Toshihide Takeuchi

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

P2860

Mechanisms of cellular uptake of cell-penetrating peptides

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Applications and Challenges for Use of Cell-Penetrating Peptides as Delivery Vectors for Peptide and Protein Cargos

Cellular uptake of the tat protein from human immunodeficiency virus

Experimentally determined hydrophobicity scale for proteins at membrane interfaces

Interactions of amphipathic carrier peptides with membrane components in relation with their ability to deliver therapeutics.

Structure and dynamics of the two amphipathic arginine-rich peptides RW9 and RL9 in a lipid environment investigated by solid-state NMR and MD simulations.

Cell-Penetrating, Guanidinium-Rich Oligophosphoesters: Effective and Versatile Molecular Transporters for Drug and Probe Delivery.

Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery.

The preference of tryptophan for membrane interfaces.

P304

7514-7521

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

P31

scholarly article

P356

10.1039/C6PY01615D

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

P433

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

P478

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

P50

Shiroh Futaki

Coralie M Backlund

P577

2016-11-14T00:00:00Z

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

P698

29093759

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

P921

hydrophobicity

P932

5661863

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

Increased Hydrophobic Block Length of PTDMs Promotes Protein Internalization.

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P2860

P2860

Increased Hydrophobic Block Length of PTDMs Promotes Protein Internalization.

description

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932