Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species.

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Proteasome-targeted nanobodies alleviate pathology and functional decline in an α-synuclein-based Parkinson's disease model

P2860

Q58722552-5CBA5BA4-312C-466A-A416-71714EADB334

P2860

Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species.

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http://www.wikidata.org/entity/Q40968608

description

2017 nî lūn-bûn

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2017年の論文

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2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

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2017年論文

@zh-tw

2017年论文

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2017年论文

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2017年论文

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name

Nanobodies raised against mono ...... lize toxic oligomeric species.

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type

Item

label

Nanobodies raised against mono ...... lize toxic oligomeric species.

@en

prefLabel

Nanobodies raised against mono ...... lize toxic oligomeric species.

@en

P1476

Nanobodies raised against mono ...... lize toxic oligomeric species.

@en

P2093

Clare E Bryant

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

Craig D Hughes

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

David Klenerman

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

Erwin De Genst

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

Liu Hong

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

Marija Iljina

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

Mathew H Horrocks

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

Minee L Choi

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

Sonia Gandhi

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

Steven F Lee

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

P2860

Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brain

Immunotherapy in Parkinson's Disease: Micromanaging Alpha-Synuclein Aggregation

Structure and properties of a complex of α-synuclein and a single-domain camelid antibody

A Nanobody Binding to Non-Amyloidogenic Regions of the Protein Human Lysozyme Enhances Partial Unfolding but Inhibits Amyloid Fibril Formation

Naturally occurring antibodies devoid of light chains

Antibodies against alpha-synuclein reduce oligomerization in living cells

Single domain camel antibodies: current status.

Inhibiting aggregation of alpha-synuclein with human single chain antibody fragments.

Determination of the fraction and stoichiometry of femtomolar levels of biomolecular complexes in an excess of monomer using single-molecule, two-color coincidence detection.

Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicity

P2888

s12915-017-0390-6

P304

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P31

scholarly article

P356

10.1186/S12915-017-0390-6

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P433

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

P478

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

P50

Chris Dobson

Michele Vendruscolo

Francesco Simone Ruggeri

Alexander K Buell

Ji-Eun Lee

Marthe H Ludtmann

P577

2017-07-03T00:00:00Z

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

P6179

1090274809

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P698

28673288

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P921

Synuclein

P932

5496350

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

Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species.

about

P2860

P2860

Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P6179

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P6179

P698

P921

P932