Structure and mechanism of the phosphotyrosyl phosphatase activator (Q24300049)

GOA release 2020-03-11

ATPase activity

1 reference

GOA release 2020-03-11

author

Yigong Shi

9

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author name string

Yang Chao

1

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Yongna Xing

2

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Yu Chen

3

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Yanhui Xu

4

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Zheng Lin

5

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Zhu Li

6

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Philip D Jeffrey

7

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Jeffry B Stock

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

8

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language of work or name

English

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publication date

August 2006

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published in

Molecular Cell

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volume

23

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issue

4

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page(s)

535-46

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cites work

1 reference

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Protein structure comparison by alignment of distance matrices

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Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate

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Side-chain effects on peptidyl-prolyl cis/trans isomerisation.

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Protein serine/threonine phosphatases; an expanding family

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Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling

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Protein tyrosine phosphatases in the human genome

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PP2A: the expected tumor suppressor

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Processing of X-ray diffraction data collected in oscillation mode

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Protein phosphatase 2A: a panoply of enzymes.

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Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A.

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Isolation and characterization of a tyrosyl phosphatase activator from rabbit skeletal muscle and Xenopus laevis oocytes

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alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure

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Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1

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A phosphotyrosine-containing quenched fluorogenic peptide as a novel substrate for protein tyrosine phosphatases

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Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling

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An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator

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Specific interactions of PP2A and PP2A-like phosphatases with the yeast PTPA homologues, Ypa1 and Ypa2.

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Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics

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Molecular cloning and sequence analysis of the catalytic subunit of bovine type 2A protein phosphatase

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Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes

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The crystal structure of a human PP2A phosphatase activator reveals a novel fold and highly conserved cleft implicated in protein-protein interactions.

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Formation of a stable heterodimer between Smad2 and Smad4

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The protein phosphatase 2A phosphatase activator is a novel peptidyl-prolyl cis/trans-isomerase.

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A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo.

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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The phosphotyrosyl phosphatase activator of protein phosphatase 2A. A novel purification method, immunological and enzymic characterization

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A comparative study of the phosphotyrosyl phosphatase specificity of protein phosphatase type 2A and phosphotyrosyl phosphatase type 1B using phosphopeptides and the phosphoproteins p50/HS1, c-Fgr and Lyn.

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

release_s2ftiqvfqnbjtd4et7zk6pd5lu

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/s2ftiqvfqnbjtd4et7zk6pd5lu

24 November 2022

mapped directly with Wikidata item

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Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

16916641

1 reference

Consolidated OpenCitations Corpus – April 2017