Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.

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Quantification of Membrane Protein-Detergent Complex Interactions.Detergent Desorption of Membrane Proteins Exhibits Two Kinetic Phases.Understanding antibiotic resistance via outer membrane permeability.

P2860

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P2860

Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.

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http://www.wikidata.org/entity/Q47789965

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2017 nî lūn-bûn

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2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

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2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Aberrantly Large Single-Channe ...... -Containing Protein Nanopores.

@en

Aberrantly Large Single-Channe ...... -Containing Protein Nanopores.

@nl

type

Item

label

Aberrantly Large Single-Channe ...... -Containing Protein Nanopores.

@en

Aberrantly Large Single-Channe ...... -Containing Protein Nanopores.

@nl

prefLabel

Aberrantly Large Single-Channe ...... -Containing Protein Nanopores.

@en

Aberrantly Large Single-Channe ...... -Containing Protein Nanopores.

@nl

P1476

Aberrantly Large Single-Channe ...... -Containing Protein Nanopores.

@en

P2093

Avinash Kumar Thakur

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

Kristin Gooden

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

Motahareh Ghahari Larimi

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

P2860

Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA

Active transport of an antibiotic rifamycin derivative by the outer-membrane protein FhuA

Crystal structure of the anti-His tag antibody 3D5 single-chain fragment complexed to its antigen

Toward Understanding the Outer Membrane Uptake of Small Molecules by Pseudomonas aeruginosa

Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides

Structure-based engineering of a minimal porin reveals loop-independent channel closure

Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes

Kinetic states and modes of single large-conductance calcium-activated potassium channels in cultured rat skeletal muscle

Membrane protein folding and stability: physical principles

Outer membrane protein design.

P304

4895-4905

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P31

scholarly article

P356

10.1021/ACS.BIOCHEM.7B00577

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P407

English

P433

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

P478

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

P50

Liviu Movileanu

P577

2017-08-16T00:00:00Z

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

P698

28812882

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P932

5595664

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Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.

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P2860

P2860

Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932