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Cited by 252

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Structural basis for protein phosphatase 1 regulation and specificity

Open access
Peti, Wolfgang, Nairn, Angus C., Page, Rebecca·2013·The FEBS Journal
DOI 10.1111/j.1742-4658.2012.08509.x
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Abstract

The ubiquitous serine/threonine protein phosphatase 1 (PP1) regulates diverse, essential cellular processes such as cell cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling. However, the free catalytic subunit of PP1, while an effective enzyme, lacks substrate specificity. Instead, it depends on a diverse set of regulatory proteins (≥ 200) to confer specificity towards distinct substrates. Here, we discuss recent advances in structural studies of PP1 holoenzyme complexes and summarize the new insights these studies have provided into the molecular basis of PP1 regulation and specificity.

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Metadata

Authors
Peti, W., Nairn, A. C., & Page, R.
Venue
The FEBS Journal
Publisher
Wiley
Published
2012-02-24
Volume
280
Issue
2
Pages
596-611
ISSN
  • 1742-464X (ISSN-L)
  • 1742-4658
DOI
10.1111/j.1742-4658.2012.08509.x
OpenAlex
W1568601491
Cited by
252
References
5
FWCI
6.74
Type
journal article
Language
en
Open access
bronze
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.