Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.

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Interactions of the proteins of neuronal ceroid lipofuscinosis: clues to function Activatable Optical Probes for the Detection of Enzymes.

P2860

Q28289653-BC95D907-D084-43B2-A213-756497FCD4FC Q36697462-5F652473-A1E7-4330-BD74-27B0891424AA

P2860

Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.

Item

http://www.wikidata.org/entity/Q53617221

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2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年学术文章

@wuu

2006年学术文章

@zh-cn

2006年学术文章

@zh-hans

2006年学术文章

@zh-my

2006年学术文章

@zh-sg

2006年學術文章

@yue

2006年學術文章

@zh

2006年學術文章

@zh-hant

name

Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.

@en

Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.

@nl

type

Item

label

Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.

@en

Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.

@nl

prefLabel

Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.

@en

Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.

@nl

P1476

Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.

@en

P2093

Jutta Gärtner

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

Robert Steinfeld

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

P2860

Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis

The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH

Mutations in classical late infantile neuronal ceroid lipofuscinosis disrupt transport of tripeptidyl-peptidase I to lysosomes

Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis

A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases

A mouse model of classical late-infantile neuronal ceroid lipofuscinosis based on targeted disruption of the CLN2 gene results in a loss of tripeptidyl-peptidase I activity and progressive neurodegeneration

Determination of the substrate specificity of tripeptidyl-peptidase I using combinatorial peptide libraries and development of improved fluorogenic substrates.

A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation.

Purification and characterization of tripeptidylpeptidase-II from post-mortem human brain.

Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII.

P304

991-996

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P31

scholarly article

P356

10.1369/JHC.5A6900.2006

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

P433

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

P478

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

P50

Jens Fuhrmann

P577

2006-06-16T00:00:00Z

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

P698

16782851

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Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.

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P2860

P2860

Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698