DOI: 10.1016/j.molcel.2006.07.027. Structure and Mechanism of the Phosphotyrosyl Phosphatase Activator

Structure and Mechanism of the Phosphotyrosyl Phosphatase Activator

10.1016/j.molcel.2006.07.027

Crossref journal-article

Elsevier BV

Molecular Cell (78)

Bibliography

Chao, Y., Xing, Y., Chen, Y., Xu, Y., Lin, Z., Li, Z., Jeffrey, P. D., Stock, J. B., & Shi, Y. (2006). Structure and Mechanism of the Phosphotyrosyl Phosphatase Activator. Molecular Cell, 23(4), 535â546.

Authors 9

Yang Chao (first)
Yongna Xing (additional)
Yu Chen (additional)
Yanhui Xu (additional)
Zheng Lin (additional)
Zhu Li (additional)
Philip D. Jeffrey (additional)
Jeffry B. Stock (additional)
Yigong Shi (additional)

References 35 Referenced 41

10.1111/j.1432-1033.1996.00548.x / Eur. J. Biochem. / 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 by Agostinis (1996)
10.1016/j.cell.2004.05.018 / Cell / Protein tyrosine phosphatases in the human genome by Alonso (2004)
10.1073/pnas.85.12.4252 / Proc. Natl. Acad. Sci. USA / Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes by Arino (1988)
10.1042/bj2560283 / Biochem. J. / Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics by Bialojan (1988)
10.1107/S0907444998003254 / Acta Crystallogr. D Biol. Crystallogr. / Crystallography and NMR system: a new software suite for macromolecular structure determination by Brunger (1998)
10.1021/bi00455a010 / Biochemistry / Isolation and characterization of a tyrosyl phosphatase activator from rabbit skeletal muscle and Xenopus laevis oocytes by Cayla (1990)
10.1016/S0021-9258(17)40733-2 / J. Biol. Chem. / Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A by Cayla (1994)
10.1016/0014-5793(90)81285-V / FEBS Lett. / Protein serine/threonine phosphatases; an expanding family by Cohen (1990)
10.1006/jmbi.1995.0667 / J. Mol. Biol. / Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate by Egloff (1995)
10.1101/gad.259903 / Genes Dev. / A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo by Fellner (2003)
10.1038/376745a0 / Nature / Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1 by Goldberg (1995)
10.1002/bip.1981.360201209 / Biopolymers / NMR studies of the rates of proline cis/trans isomerisation in oligopeptides by Grathwohl (1981)
10.1073/pnas.84.14.4880 / Proc. Natl. Acad. Sci. USA / Molecular cloning and sequence analysis of the catalytic subunit of bovine type 2A protein phosphatase by Green (1987)
10.1021/bi00465a002 / Biochemistry / Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure by Hemmings (1990)
10.1006/jmbi.1993.1489 / J. Mol. Biol. / Protein structure comparison by alignment of distance matrices by Holm (1993)
10.1016/0092-8674(95)90405-0 / Cell / Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling by Hunter (1995)
10.1042/bj3530417 / Biochem. J. / Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling by Janssens (2001)
10.1016/j.gde.2004.12.004 / Curr. Opin. Genet. Dev. / PP2A: the expected tumor suppressor by Janssens (2005)
10.1107/S0108767390010224 / Acta Crystallogr. / Improved methods for building protein models in electron density maps and the location of errors in these models by Jones (1991)
10.1074/jbc.M507760200 / J. Biol. Chem. / The protein phosphatase 2A phosphatase activator is a novel peptidyl-prolyl cis/trans-isomerase by Jordens (2006)
{'key': '10.1016/j.molcel.2006.07.027_bib21', 'first-page': '23', 'article-title': 'Protein phosphatase type 1 and type 2A assays', 'volume': '93', 'author': 'Killilea', 'year': '1998', 'journal-title': 'Methods Mol. Biol.'} / Methods Mol. Biol. / Protein phosphatase type 1 and type 2A assays by Killilea (1998)
10.1107/S0021889891004399 / J. Appl. Crystallogr. / Molscript: a program to produce both detailed and schematic plots of protein structures by Kraulis (1991)
10.18388/abp.2001_3858 / Acta Biochim. Pol. / Protein phosphatase 2A: variety of forms and diversity of functions by Lechward (2001)
10.1042/bj20031643 / Biochem. J. / An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator by Longin (2004)
10.1074/jbc.C600100200 / J. Biol. Chem. / The crystal structure of a human PP2A phosphatase activator reveals a novel fold and highly conserved cleft implicated in protein-protein interactions by Magnusdottir (2006)
{'key': '10.1016/j.molcel.2006.07.027_bib26', 'first-page': '458', 'article-title': 'Likelihood-enhanced fast translation functions', 'volume': 'D61', 'author': 'McCoy', 'year': '2005', 'journal-title': 'Acta Crystallogr.'} / Acta Crystallogr. / Likelihood-enhanced fast translation functions by McCoy (2005)
10.1002/prot.340110407 / Proteins / Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons by Nicholls (1991)
10.1042/bj3430385 / Biochem. J. / A phosphotyrosine-containing quenched fluorogenic peptide as a novel substrate for protein tyrosine phosphatases by Nishikata (1999)
10.1016/S0076-6879(97)76066-X / Methods Enzymol. / Processing of X-ray diffraction data collected in oscillation mode by Otwinowski (1997)
10.1006/jmbi.1998.1770 / J. Mol. Biol. / Side-chain effects on peptidyl-prolyl cis/trans isomerisation by Reimer (1998)
10.1021/bi00397a003 / Biochemistry / Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A by Stone (1987)
10.1111/j.1432-1033.1994.00899.x / Eur. J. Biochem. / The phosphotyrosyl phosphatase activator of protein phosphatase 2A. A novel purification method, immunological and enzymic characterization by Van Hoof (1994)
10.1042/BJ20040887 / Biochem. J. / Specific interactions of PP2A and PP2A-like phosphatases with the yeast PTPA homologues, Ypa1 and Ypa2 by Van Hoof (2005)
10.1016/S0955-0674(99)00074-5 / Curr. Opin. Cell Biol. / Protein phosphatase 2A: a panoply of enzymes by Virshup (2000)
10.1074/jbc.M100174200 / J. Biol. Chem. / Formation of a stable heterodimer between Smad2 and Smad4 by Wu (2001)

Dates

Type	When
Created	19 years ago (Aug. 18, 2006, 7:13 a.m.)
Deposited	1 year, 3 months ago (May 11, 2024, 3:05 a.m.)
Indexed	1 month ago (Aug. 5, 2025, 9:09 a.m.)
Issued	19 years, 1 month ago (Aug. 1, 2006)
Published	19 years, 1 month ago (Aug. 1, 2006)
Published Print	19 years, 1 month ago (Aug. 1, 2006)

Funders 0

None

BibTeX

@article{Chao_2006, title={Structure and Mechanism of the Phosphotyrosyl Phosphatase Activator}, volume={23}, ISSN={1097-2765}, url={http://dx.doi.org/10.1016/j.molcel.2006.07.027}, DOI={10.1016/j.molcel.2006.07.027}, number={4}, journal={Molecular Cell}, publisher={Elsevier BV}, author={Chao, Yang and Xing, Yongna and Chen, Yu and Xu, Yanhui and Lin, Zheng and Li, Zhu and Jeffrey, Philip D. and Stock, Jeffry B. and Shi, Yigong}, year={2006}, month=aug, pages={535–546} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        8,
        5
      ]
    ],
    "date-time": "2025-08-05T13:09:29Z",
    "timestamp": 1754399369779
  },
  "reference-count": 35,
  "publisher": "Elsevier BV",
  "issue": "4",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            2006,
            8,
            1
          ]
        ],
        "date-time": "2006-08-01T00:00:00Z",
        "timestamp": 1154390400000
      },
      "content-version": "tdm",
      "delay-in-days": 0,
      "URL": "https://www.elsevier.com/tdm/userlicense/1.0/"
    },
    {
      "start": {
        "date-parts": [
          [
            2006,
            8,
            1
          ]
        ],
        "date-time": "2006-08-01T00:00:00Z",
        "timestamp": 1154390400000
      },
      "content-version": "tdm",
      "delay-in-days": 0,
      "URL": "https://www.elsevier.com/legal/tdmrep-license"
    },
    {
      "start": {
        "date-parts": [
          [
            2013,
            7,
            17
          ]
        ],
        "date-time": "2013-07-17T00:00:00Z",
        "timestamp": 1374019200000
      },
      "content-version": "vor",
      "delay-in-days": 2542,
      "URL": "http://www.elsevier.com/open-access/userlicense/1.0/"
    },
    {
      "start": {
        "date-parts": [
          [
            2006,
            8,
            1
          ]
        ],
        "date-time": "2006-08-01T00:00:00Z",
        "timestamp": 1154390400000
      },
      "content-version": "stm-asf",
      "delay-in-days": 0,
      "URL": "https://doi.org/10.15223/policy-017"
    },
    {
      "start": {
        "date-parts": [
          [
            2006,
            8,
            1
          ]
        ],
        "date-time": "2006-08-01T00:00:00Z",
        "timestamp": 1154390400000
      },
      "content-version": "stm-asf",
      "delay-in-days": 0,
      "URL": "https://doi.org/10.15223/policy-037"
    },
    {
      "start": {
        "date-parts": [
          [
            2006,
            8,
            1
          ]
        ],
        "date-time": "2006-08-01T00:00:00Z",
        "timestamp": 1154390400000
      },
      "content-version": "stm-asf",
      "delay-in-days": 0,
      "URL": "https://doi.org/10.15223/policy-012"
    },
    {
      "start": {
        "date-parts": [
          [
            2006,
            8,
            1
          ]
        ],
        "date-time": "2006-08-01T00:00:00Z",
        "timestamp": 1154390400000
      },
      "content-version": "stm-asf",
      "delay-in-days": 0,
      "URL": "https://doi.org/10.15223/policy-029"
    },
    {
      "start": {
        "date-parts": [
          [
            2006,
            8,
            1
          ]
        ],
        "date-time": "2006-08-01T00:00:00Z",
        "timestamp": 1154390400000
      },
      "content-version": "stm-asf",
      "delay-in-days": 0,
      "URL": "https://doi.org/10.15223/policy-004"
    }
  ],
  "content-domain": {
    "domain": [
      "cell.com",
      "elsevier.com",
      "sciencedirect.com"
    ],
    "crossmark-restriction": true
  },
  "published-print": {
    "date-parts": [
      [
        2006,
        8
      ]
    ]
  },
  "DOI": "10.1016/j.molcel.2006.07.027",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2006,
        8,
        18
      ]
    ],
    "date-time": "2006-08-18T11:13:23Z",
    "timestamp": 1155899603000
  },
  "page": "535-546",
  "update-policy": "http://dx.doi.org/10.1016/elsevier_cm_policy",
  "source": "Crossref",
  "is-referenced-by-count": 41,
  "title": "Structure and Mechanism of the Phosphotyrosyl Phosphatase Activator",
  "prefix": "10.1016",
  "volume": "23",
  "author": [
    {
      "given": "Yang",
      "family": "Chao",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "Yongna",
      "family": "Xing",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Yu",
      "family": "Chen",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Yanhui",
      "family": "Xu",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Zheng",
      "family": "Lin",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Zhu",
      "family": "Li",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Philip D.",
      "family": "Jeffrey",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Jeffry B.",
      "family": "Stock",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Yigong",
      "family": "Shi",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "78",
  "reference": [
    {
      "key": "10.1016/j.molcel.2006.07.027_bib1",
      "doi-asserted-by": "crossref",
      "first-page": "548",
      "DOI": "10.1111/j.1432-1033.1996.00548.x",
      "article-title": "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",
      "volume": "236",
      "author": "Agostinis",
      "year": "1996",
      "journal-title": "Eur. J. Biochem."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib2",
      "doi-asserted-by": "crossref",
      "first-page": "699",
      "DOI": "10.1016/j.cell.2004.05.018",
      "article-title": "Protein tyrosine phosphatases in the human genome",
      "volume": "117",
      "author": "Alonso",
      "year": "2004",
      "journal-title": "Cell"
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib3",
      "doi-asserted-by": "crossref",
      "first-page": "4252",
      "DOI": "10.1073/pnas.85.12.4252",
      "article-title": "Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes",
      "volume": "85",
      "author": "Arino",
      "year": "1988",
      "journal-title": "Proc. Natl. Acad. Sci. USA"
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib4",
      "doi-asserted-by": "crossref",
      "first-page": "283",
      "DOI": "10.1042/bj2560283",
      "article-title": "Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics",
      "volume": "256",
      "author": "Bialojan",
      "year": "1988",
      "journal-title": "Biochem. J."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib5",
      "doi-asserted-by": "crossref",
      "first-page": "905",
      "DOI": "10.1107/S0907444998003254",
      "article-title": "Crystallography and NMR system: a new software suite for macromolecular structure determination",
      "volume": "54",
      "author": "Brunger",
      "year": "1998",
      "journal-title": "Acta Crystallogr. D Biol. Crystallogr."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib6",
      "doi-asserted-by": "crossref",
      "first-page": "633",
      "DOI": "10.1021/bi00455a010",
      "article-title": "Isolation and characterization of a tyrosyl phosphatase activator from rabbit skeletal muscle and Xenopus laevis oocytes",
      "volume": "29",
      "author": "Cayla",
      "year": "1990",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib7",
      "doi-asserted-by": "crossref",
      "first-page": "15668",
      "DOI": "10.1016/S0021-9258(17)40733-2",
      "article-title": "Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A",
      "volume": "269",
      "author": "Cayla",
      "year": "1994",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib8",
      "doi-asserted-by": "crossref",
      "first-page": "355",
      "DOI": "10.1016/0014-5793(90)81285-V",
      "article-title": "Protein serine/threonine phosphatases; an expanding family",
      "volume": "268",
      "author": "Cohen",
      "year": "1990",
      "journal-title": "FEBS Lett."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib9",
      "doi-asserted-by": "crossref",
      "first-page": "942",
      "DOI": "10.1006/jmbi.1995.0667",
      "article-title": "Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate",
      "volume": "254",
      "author": "Egloff",
      "year": "1995",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib10",
      "doi-asserted-by": "crossref",
      "first-page": "2138",
      "DOI": "10.1101/gad.259903",
      "article-title": "A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo",
      "volume": "17",
      "author": "Fellner",
      "year": "2003",
      "journal-title": "Genes Dev."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib11",
      "doi-asserted-by": "crossref",
      "first-page": "745",
      "DOI": "10.1038/376745a0",
      "article-title": "Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1",
      "volume": "376",
      "author": "Goldberg",
      "year": "1995",
      "journal-title": "Nature"
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib12",
      "doi-asserted-by": "crossref",
      "first-page": "2623",
      "DOI": "10.1002/bip.1981.360201209",
      "article-title": "NMR studies of the rates of proline cis/trans isomerisation in oligopeptides",
      "volume": "20",
      "author": "Grathwohl",
      "year": "1981",
      "journal-title": "Biopolymers"
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib13",
      "doi-asserted-by": "crossref",
      "first-page": "4880",
      "DOI": "10.1073/pnas.84.14.4880",
      "article-title": "Molecular cloning and sequence analysis of the catalytic subunit of bovine type 2A protein phosphatase",
      "volume": "84",
      "author": "Green",
      "year": "1987",
      "journal-title": "Proc. Natl. Acad. Sci. USA"
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib14",
      "doi-asserted-by": "crossref",
      "first-page": "3166",
      "DOI": "10.1021/bi00465a002",
      "article-title": "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure",
      "volume": "29",
      "author": "Hemmings",
      "year": "1990",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib15",
      "doi-asserted-by": "crossref",
      "first-page": "123",
      "DOI": "10.1006/jmbi.1993.1489",
      "article-title": "Protein structure comparison by alignment of distance matrices",
      "volume": "233",
      "author": "Holm",
      "year": "1993",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib16",
      "doi-asserted-by": "crossref",
      "first-page": "225",
      "DOI": "10.1016/0092-8674(95)90405-0",
      "article-title": "Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling",
      "volume": "80",
      "author": "Hunter",
      "year": "1995",
      "journal-title": "Cell"
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib17",
      "doi-asserted-by": "crossref",
      "first-page": "417",
      "DOI": "10.1042/bj3530417",
      "article-title": "Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling",
      "volume": "353",
      "author": "Janssens",
      "year": "2001",
      "journal-title": "Biochem. J."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib18",
      "doi-asserted-by": "crossref",
      "first-page": "34",
      "DOI": "10.1016/j.gde.2004.12.004",
      "article-title": "PP2A: the expected tumor suppressor",
      "volume": "15",
      "author": "Janssens",
      "year": "2005",
      "journal-title": "Curr. Opin. Genet. Dev."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib19",
      "doi-asserted-by": "crossref",
      "first-page": "110",
      "DOI": "10.1107/S0108767390010224",
      "article-title": "Improved methods for building protein models in electron density maps and the location of errors in these models",
      "volume": "A47",
      "author": "Jones",
      "year": "1991",
      "journal-title": "Acta Crystallogr."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib20",
      "doi-asserted-by": "crossref",
      "first-page": "6349",
      "DOI": "10.1074/jbc.M507760200",
      "article-title": "The protein phosphatase 2A phosphatase activator is a novel peptidyl-prolyl cis/trans-isomerase",
      "volume": "281",
      "author": "Jordens",
      "year": "2006",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib21",
      "first-page": "23",
      "article-title": "Protein phosphatase type 1 and type 2A assays",
      "volume": "93",
      "author": "Killilea",
      "year": "1998",
      "journal-title": "Methods Mol. Biol."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib22",
      "doi-asserted-by": "crossref",
      "first-page": "946",
      "DOI": "10.1107/S0021889891004399",
      "article-title": "Molscript: a program to produce both detailed and schematic plots of protein structures",
      "volume": "24",
      "author": "Kraulis",
      "year": "1991",
      "journal-title": "J. Appl. Crystallogr."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib23",
      "doi-asserted-by": "crossref",
      "first-page": "921",
      "DOI": "10.18388/abp.2001_3858",
      "article-title": "Protein phosphatase 2A: variety of forms and diversity of functions",
      "volume": "48",
      "author": "Lechward",
      "year": "2001",
      "journal-title": "Acta Biochim. Pol."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib24",
      "doi-asserted-by": "crossref",
      "first-page": "111",
      "DOI": "10.1042/bj20031643",
      "article-title": "An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator",
      "volume": "380",
      "author": "Longin",
      "year": "2004",
      "journal-title": "Biochem. J."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib25",
      "doi-asserted-by": "crossref",
      "DOI": "10.1074/jbc.C600100200",
      "article-title": "The crystal structure of a human PP2A phosphatase activator reveals a novel fold and highly conserved cleft implicated in protein-protein interactions",
      "author": "Magnusdottir",
      "year": "2006",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib26",
      "first-page": "458",
      "article-title": "Likelihood-enhanced fast translation functions",
      "volume": "D61",
      "author": "McCoy",
      "year": "2005",
      "journal-title": "Acta Crystallogr."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib27",
      "doi-asserted-by": "crossref",
      "first-page": "281",
      "DOI": "10.1002/prot.340110407",
      "article-title": "Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons",
      "volume": "11",
      "author": "Nicholls",
      "year": "1991",
      "journal-title": "Proteins"
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib28",
      "doi-asserted-by": "crossref",
      "first-page": "385",
      "DOI": "10.1042/bj3430385",
      "article-title": "A phosphotyrosine-containing quenched fluorogenic peptide as a novel substrate for protein tyrosine phosphatases",
      "volume": "343",
      "author": "Nishikata",
      "year": "1999",
      "journal-title": "Biochem. J."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib29",
      "doi-asserted-by": "crossref",
      "first-page": "307",
      "DOI": "10.1016/S0076-6879(97)76066-X",
      "article-title": "Processing of X-ray diffraction data collected in oscillation mode",
      "volume": "276",
      "author": "Otwinowski",
      "year": "1997",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib30",
      "doi-asserted-by": "crossref",
      "first-page": "449",
      "DOI": "10.1006/jmbi.1998.1770",
      "article-title": "Side-chain effects on peptidyl-prolyl cis/trans isomerisation",
      "volume": "279",
      "author": "Reimer",
      "year": "1998",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib31",
      "doi-asserted-by": "crossref",
      "first-page": "7215",
      "DOI": "10.1021/bi00397a003",
      "article-title": "Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A",
      "volume": "26",
      "author": "Stone",
      "year": "1987",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib32",
      "doi-asserted-by": "crossref",
      "first-page": "899",
      "DOI": "10.1111/j.1432-1033.1994.00899.x",
      "article-title": "The phosphotyrosyl phosphatase activator of protein phosphatase 2A. A novel purification method, immunological and enzymic characterization",
      "volume": "226",
      "author": "Van Hoof",
      "year": "1994",
      "journal-title": "Eur. J. Biochem."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib33",
      "doi-asserted-by": "crossref",
      "first-page": "93",
      "DOI": "10.1042/BJ20040887",
      "article-title": "Specific interactions of PP2A and PP2A-like phosphatases with the yeast PTPA homologues, Ypa1 and Ypa2",
      "volume": "386",
      "author": "Van Hoof",
      "year": "2005",
      "journal-title": "Biochem. J."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib34",
      "doi-asserted-by": "crossref",
      "first-page": "180",
      "DOI": "10.1016/S0955-0674(99)00074-5",
      "article-title": "Protein phosphatase 2A: a panoply of enzymes",
      "volume": "12",
      "author": "Virshup",
      "year": "2000",
      "journal-title": "Curr. Opin. Cell Biol."
    },
    {
      "key": "10.1016/j.molcel.2006.07.027_bib35",
      "doi-asserted-by": "crossref",
      "first-page": "20688",
      "DOI": "10.1074/jbc.M100174200",
      "article-title": "Formation of a stable heterodimer between Smad2 and Smad4",
      "volume": "276",
      "author": "Wu",
      "year": "2001",
      "journal-title": "J. Biol. Chem."
    }
  ],
  "container-title": "Molecular Cell",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://api.elsevier.com/content/article/PII:S1097276506005284?httpAccept=text/xml",
      "content-type": "text/xml",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://api.elsevier.com/content/article/PII:S1097276506005284?httpAccept=text/plain",
      "content-type": "text/plain",
      "content-version": "vor",
      "intended-application": "text-mining"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2024,
        5,
        11
      ]
    ],
    "date-time": "2024-05-11T07:05:33Z",
    "timestamp": 1715411133000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://linkinghub.elsevier.com/retrieve/pii/S1097276506005284"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        2006,
        8
      ]
    ]
  },
  "references-count": 35,
  "journal-issue": {
    "issue": "4",
    "published-print": {
      "date-parts": [
        [
          2006,
          8
        ]
      ]
    }
  },
  "alternative-id": [
    "S1097276506005284"
  ],
  "URL": "http://dx.doi.org/10.1016/j.molcel.2006.07.027",
  "relation": {},
  "ISSN": [
    "1097-2765"
  ],
  "subject": [],
  "container-title-short": "Molecular Cell",
  "published": {
    "date-parts": [
      [
        2006,
        8
      ]
    ]
  },
  "assertion": [
    {
      "value": "Elsevier",
      "name": "publisher",
      "label": "This article is maintained by"
    },
    {
      "value": "Structure and Mechanism of the Phosphotyrosyl Phosphatase Activator",
      "name": "articletitle",
      "label": "Article Title"
    },
    {
      "value": "Molecular Cell",
      "name": "journaltitle",
      "label": "Journal Title"
    },
    {
      "value": "https://doi.org/10.1016/j.molcel.2006.07.027",
      "name": "articlelink",
      "label": "CrossRef DOI link to publisher maintained version"
    },
    {
      "value": "article",
      "name": "content_type",
      "label": "Content Type"
    },
    {
      "value": "Copyright \u00a9 2006 Elsevier Inc. All rights reserved.",
      "name": "copyright",
      "label": "Copyright"
    }
  ]
}