A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases (Q24797714)

GOA release 2020-03-11

Tripeptidyl peptidase I

1 reference

GOA release 2020-03-11

molecular model

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14609438

31 March 2024

1

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author name string

Mi Li

3

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Hiroshi Oyama

4

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Kohei Oda

5

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Stewart R. Durell

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14609438

31 March 2024

Ben M. Dunn

6

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14609438

full work available at URL

31 March 2024

language of work or name

English

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publication date

11 November 2003

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https://bmcstructbiol.biomedcentral.com/track/pdf/10.1186/1472-6807-3-8

file format

Portable Document Format

online access status

open access

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14609438

https://europepmc.org/articles/PMC280685

31 March 2024

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14609438

https://europepmc.org/articles/PMC280685?pdf=render

31 March 2024

file format

Portable Document Format

online access status

open access

content deliverer

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14609438

https://scigraph.springernature.com/pub.10.1186/1472-6807-3-8

31 March 2024

published in

BMC Structural Biology

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volume

3

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issue

1

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page(s)

8

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exact match

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cites work

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280685

Tripeptidyl peptidase I, the late infantile neuronal ceroid lipofuscinosis gene product, initiates the lysosomal degradation of subunit c of ATP synthase

7 April 2017

1 reference

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7 April 2017

The Protein Data Bank

1 reference

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Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder

7 April 2017

1 reference

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The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools

7 April 2017

1 reference

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

7 April 2017

1 reference

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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

7 April 2017

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Initial sequencing and comparative analysis of the mouse genome

7 April 2017

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Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs

7 April 2017

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The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase

7 April 2017

1 reference

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Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase

7 April 2017

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Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes

7 April 2017

1 reference

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Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280685

Sequence comparisons using multiple sequences detect three times as many remote homologues as pairwise methods

7 April 2017

1 reference

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SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

7 April 2017

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On the size of the active site in proteases. I. Papain

7 April 2017

1 reference

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Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280685

Structural and enzymatic characterization of physarolisin (formerly physaropepsin) proves that it is a unique serine-carboxyl proteinase

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280685

Collagenolytic serine-carboxyl proteinase from Alicyclobacillus sendaiensis strain NTAP-1: purification, characterization, gene cloning, and heterologous expression

28 September 2017

1 reference

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Lysosomal degradation of cholecystokinin-(29-33)-amide in mouse brain is dependent on tripeptidyl peptidase-I: implications for the degradation and storage of peptides in classical late-infantile neuronal ceroid lipofuscinosis

28 September 2017

1 reference

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Aorsin, a novel serine proteinase with trypsin-like specificity at acidic pH.

28 September 2017

1 reference

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Purification and characterisation of a tripeptidyl aminopeptidase I from rat spleen.

30 May 2018

1 reference

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Molecular modeling of the HIV-1 protease and its substrate binding site

30 May 2018

1 reference

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Studies on the serial extraction of pituitary proteins.

30 May 2018

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Mouse gene knockout models for the CLN2 and CLN3 forms of ceroid lipofuscinosis

28 November 2018

1 reference

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The specificity of lysosomal tripeptidyl peptidase-I determined by its action on angiotensin-II analogues

28 November 2018

1 reference

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Partial purification and characterization of an ovarian tripeptidyl peptidase: a lysosomal exopeptidase that sequentially releases collagen-related (Gly-Pro-X) triplets

28 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/14609438

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

1 reference

https://pubmed.ncbi.nlm.nih.gov/14609438