The MAPK signaling cascade is a central hub in the regulation of cell cycle, apoptosis and cytoskeleton remodeling by tripeptidyl-peptidase II. (Q42536776)

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scientific article published on 24 November 2008

Language	Label	Description	Also known as
English	The MAPK signaling cascade is a central hub in the regulation of cell cycle, apoptosis and cytoskeleton remodeling by tripeptidyl-peptidase II.	scientific article published on 24 November 2008

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

1 November 2017

The MAPK signaling cascade is a central hub in the regulation of cell cycle, apoptosis and cytoskeleton remodeling by tripeptidyl-peptidase II. (English)

1 reference

Europe PubMed Central

PMC publication ID

1 November 2017

0 references

4

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Europe PubMed Central

PMC publication ID

1 November 2017

author name string

Ramakrishna Sompallae

1

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Europe PubMed Central

PMC publication ID

1 November 2017

Vaia Stavropoulou

2

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Europe PubMed Central

PMC publication ID

1 November 2017

Mathieu Houde

3

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Europe PubMed Central

PMC publication ID

1 November 2017

publication date

24 November 2008

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Europe PubMed Central

PMC publication ID

1 November 2017

Gene Regulation and Systems Biology

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Europe PubMed Central

PMC publication ID

1 November 2017

2

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Europe PubMed Central

PMC publication ID

1 November 2017

253-265

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Europe PubMed Central

PMC publication ID

1 November 2017

Activation of cellular death programs associated with immunosenescence-like phenotype in TPPII knockout mice

1 reference

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Extracellular matrix-regulated gene expression requires cooperation of SWI/SNF and transcription factors

1 reference

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Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation

1 reference

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TPPII promotes genetic instability by allowing the escape from apoptosis of cells with activated mitotic checkpoints.

1 reference

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Centrosomes in cellular regulation

1 reference

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1 reference

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1 reference

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Structure-function studies of recombinant murine tripeptidyl-peptidase II: the extra domain which is subject to alternative splicing is involved in complex formation

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Tripeptidyl peptidase II in haemolysates and liver homogenates of various species

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Identifiers

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

1 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

1 November 2017

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