Conformational dynamics of cathepsin D and binding to a small-molecule BACE1 inhibitor.

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Proton-Coupled Conformational Allostery Modulates the Inhibitor Selectivity for β-Secretase.

P2860

Q48053583-074A27E5-4E4A-470C-9470-5AAB91F16E8A

P2860

Conformational dynamics of cathepsin D and binding to a small-molecule BACE1 inhibitor.

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http://www.wikidata.org/entity/Q48333250

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2017年学术文章

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Conformational dynamics of cathepsin D and binding to a small-molecule BACE1 inhibitor.

@en

Conformational dynamics of cathepsin D and binding to a small-molecule BACE1 inhibitor.

@nl

type

Item

label

Conformational dynamics of cathepsin D and binding to a small-molecule BACE1 inhibitor.

@en

Conformational dynamics of cathepsin D and binding to a small-molecule BACE1 inhibitor.

@nl

prefLabel

Conformational dynamics of cathepsin D and binding to a small-molecule BACE1 inhibitor.

@en

Conformational dynamics of cathepsin D and binding to a small-molecule BACE1 inhibitor.

@nl

P1476

Conformational dynamics of cathepsin D and binding to a small-molecule BACE1 inhibitor.

@en

P2093

Christopher R Ellis

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

Fang-Yu Lin

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

P2860

BLAST+: architecture and applications

Canonical dynamics: Equilibrium phase-space distributions

Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design

CHARMM general force field: A force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields

Balancing solvation and intramolecular interactions: toward a consistent generalized Born force field

CHARMM: the biomolecular simulation program

Crystal Structure of an Active Form of BACE1, an Enzyme Responsible for Amyloid Protein Production

Robust central reduction of amyloid-β in humans with an orally available, non-peptidic β-secretase inhibitor

Discovery of a series of efficient, centrally efficacious BACE1 inhibitors through structure-based drug design

Conformational switching in an aspartic proteinase

P304

1260-1269

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P31

scholarly article

P356

10.1002/JCC.24719

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P433

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

P478

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

P50

Cheng-Chieh Tsai

Jana Shen

P577

2017-04-02T00:00:00Z

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P698

28370344

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P932

5403572

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Conformational dynamics of cathepsin D and binding to a small-molecule BACE1 inhibitor.

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P2860

P2860

Conformational dynamics of cathepsin D and binding to a small-molecule BACE1 inhibitor.

description

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932