A common mechanism for recombinant human NGF, BDNF, NT-3, and murine NGF slow unfolding.

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Formation of cystine slipknots in dimeric proteins Self-assembly properties of a model RING domain

P2860

Q27312912-780F00AA-A34C-488B-BFB5-B410AD2712F0 Q33894328-0655A870-E02B-4CDE-B8C4-36ADFF07E80B

P2860

A common mechanism for recombinant human NGF, BDNF, NT-3, and murine NGF slow unfolding.

Item

http://www.wikidata.org/entity/Q41707315

description

1999 nî lūn-bûn

@nan

1999年の論文

@ja

1999年論文

@yue

1999年論文

@zh-hant

1999年論文

@zh-hk

1999年論文

@zh-mo

1999年論文

@zh-tw

1999年论文

@wuu

1999年论文

@zh

1999年论文

@zh-cn

name

A common mechanism for recombinant human NGF, BDNF, NT-3, and murine NGF slow unfolding.

@en

type

Item

label

A common mechanism for recombinant human NGF, BDNF, NT-3, and murine NGF slow unfolding.

@en

prefLabel

A common mechanism for recombinant human NGF, BDNF, NT-3, and murine NGF slow unfolding.

@en

P1476

A common mechanism for recombinant human NGF, BDNF, NT-3, and murine NGF slow unfolding.

@en

P2093

Burton LE

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

De Young LR

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

Schmelzer CH

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

P2860

Structure of the brain-derived neurotrophic factor/neurotrophin 3 heterodimer

Equilibrium denaturation studies of mouse beta-nerve growth factor.

Human beta-nerve growth factor gene sequence highly homologous to that of mouse.

The Trk family of neurotrophin receptors.

Activity and biospecificity of proteolyzed forms and dimeric combinations of recombinant human and murine nerve growth factor.

RhNGF slow unfolding is not due to proline isomerization: possibility of a cystine knot loop-threading mechanism.

Acid-induced unfolding of brain-derived neurotrophic factor results in the formation of a monomeric "a state".

Refolding of brain-derived neurotrophic factor from guanidine hydrochloride: kinetic trapping in a collapsed form which is incompetent for dimerization.

Mutagenesis identifies amino-terminal residues of nerve growth factor necessary for Trk receptor binding and biological activity.

Biochemical characterization of recombinant human nerve growth factor.

P304

2513-2518

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

P31

scholarly article

P356

10.1110/PS.8.11.2513

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

P433

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

P478

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

P577

1999-11-01T00:00:00Z

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

P5875

246913278

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

P698

10595557

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

P932

2144210

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

A common mechanism for recombinant human NGF, BDNF, NT-3, and murine NGF slow unfolding.

about

P2860

P2860

A common mechanism for recombinant human NGF, BDNF, NT-3, and murine NGF slow unfolding.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932