SHP2 Tyrosine Phosphatase Converts Parafibromin/Cdc73 from a Tumor Suppressor to an Oncogenic Driver

Deregulation of SHP2 is associated with malignant diseases as well as developmental disorders. Although SHP2 is required for full activation of RAS signaling, other potential roles in cell physiology have not been elucidated. Here we show that SHP2 dephosphorylates parafibromin/Cdc73, a core compone...

Full description

Saved in:
Bibliographic Details
Published inMolecular cell Vol. 43; no. 1; pp. 45 - 56
Main Authors Takahashi, Atsushi, Tsutsumi, Ryouhei, Kikuchi, Ippei, Obuse, Chikashi, Saito, Yasuhiro, Seidi, Azadeh, Karisch, Robert, Fernandez, Minerva, Cho, Taewoo, Ohnishi, Naomi, Rozenblatt-Rosen, Orit, Meyerson, Matthew, Neel, Benjamin G., Hatakeyama, Masanori
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 08.07.2011
Subjects
abnormal development
Animals
beta Catenin - metabolism
Cell Nucleus - metabolism
cell physiology
Cercopithecus aethiops
COS Cells
Cyclin D1 - genetics
Cyclin D1 - metabolism
cyclins
dephosphorylation
DNA-directed RNA polymerase
Gene Expression Regulation
genes
HEK293 Cells
histones
Humans
malformations
Mass Spectrometry
methyltransferases
Mice
Mice, Inbred C57BL
neoplasms
Phosphorylation
Protein Tyrosine Phosphatase, Non-Receptor Type 11 - analysis
Protein Tyrosine Phosphatase, Non-Receptor Type 11 - genetics
Protein Tyrosine Phosphatase, Non-Receptor Type 11 - physiology
Proto-Oncogene Proteins c-myc - genetics
Proto-Oncogene Proteins c-myc - metabolism
RNA
Signal Transduction
signals
Tumor Suppressor Proteins - genetics
Tumor Suppressor Proteins - metabolism
Tumor Suppressor Proteins - physiology
tyrosine
Tyrosine - metabolism
Wnt Proteins - metabolism
Online AccessGet full text

Cover

Abstract Deregulation of SHP2 is associated with malignant diseases as well as developmental disorders. Although SHP2 is required for full activation of RAS signaling, other potential roles in cell physiology have not been elucidated. Here we show that SHP2 dephosphorylates parafibromin/Cdc73, a core component of the RNA polymerase II-associated factor (PAF) complex. Parafibromin is known to act as a tumor suppressor that inhibits cyclin D1 and c-myc by recruiting SUV39H1 histone methyltransferase. However, parafibromin can also act in the opposing direction by binding β-catenin, thereby activating promitogenic/oncogenic Wnt signaling. We found that, on tyrosine dephosphorylation by SHP2, parafibromin acquires the ability to stably bind β-catenin. The parafibromin/β-catenin interaction overrides parafibromin/SUV39H1-mediated transrepression and induces expression of Wnt target genes, including cyclin D1 and c-myc. Hence, SHP2 governs the opposing functions of parafibromin, deregulation of which may cause the development of tumors or developmental malformations. [Display omitted] ► SHP2 tyrosine-dephosphorylates parafibromin/Cdc73, a putative tumor suppressor ► On dephosphorylation, parafibromin acquires the ability to bind β-catenin ► SHP2 stimulates Wnt signaling by promoting parafibromin/β-catenin interaction ► Binding to β-catenin overrides the tumor-suppressive functions of parafibromin
AbstractList Deregulation of SHP2 is associated with malignant diseases as well as developmental disorders. Although SHP2 is required for full activation of RAS signaling, other potential roles in cell physiology have not been elucidated. Here we show that SHP2 dephosphorylates parafibromin/Cdc73, a core component of the RNA polymerase II-associated factor (PAF) complex. Parafibromin is known to act as a tumor suppressor that inhibits cyclin D1 and c-myc by recruiting SUV39H1 histone methyltransferase. However, parafibromin can also act in the opposing direction by binding β-catenin, thereby activating promitogenic/oncogenic Wnt signaling. We found that, on tyrosine dephosphorylation by SHP2, parafibromin acquires the ability to stably bind β-catenin. The parafibromin/β-catenin interaction overrides parafibromin/SUV39H1-mediated transrepression and induces expression of Wnt target genes, including cyclin D1 and c-myc. Hence, SHP2 governs the opposing functions of parafibromin, deregulation of which may cause the development of tumors or developmental malformations. [Display omitted] ► SHP2 tyrosine-dephosphorylates parafibromin/Cdc73, a putative tumor suppressor ► On dephosphorylation, parafibromin acquires the ability to bind β-catenin ► SHP2 stimulates Wnt signaling by promoting parafibromin/β-catenin interaction ► Binding to β-catenin overrides the tumor-suppressive functions of parafibromin
Deregulation of SHP2 is associated with malignant diseases as well as developmental disorders. Although SHP2 is required for full activation of RAS signaling, other potential roles in cell physiology have not been elucidated. Here we show that SHP2 dephosphorylates parafibromin/Cdc73, a core component of the RNA polymerase II-associated factor (PAF) complex. Parafibromin is known to act as a tumor suppressor that inhibits cyclin D1 and c-myc by recruiting SUV39H1 histone methyltransferase. However, parafibromin can also act in the opposing direction by binding β-catenin, thereby activating promitogenic/oncogenic Wnt signaling. We found that, on tyrosine dephosphorylation by SHP2, parafibromin acquires the ability to stably bind β-catenin. The parafibromin/β-catenin interaction overrides parafibromin/SUV39H1-mediated transrepression and induces expression of Wnt target genes, including cyclin D1 and c-myc. Hence, SHP2 governs the opposing functions of parafibromin, deregulation of which may cause the development of tumors or developmental malformations.
Deregulation of SHP2 is associated with malignant diseases as well as developmental disorders. Although SHP2 is required for full activation of RAS signaling, other potential roles in cell physiology have not been elucidated. Here we show that SHP2 dephosphorylates parafibromin/Cdc73, a core component of the RNA polymerase II-associated factor (PAF) complex. Parafibromin is known to act as a tumor suppressor that inhibits cyclin D1 and c-myc by recruiting SUV39H1 histone methyltransferase. However, parafibromin can also act in the opposing direction by binding β-catenin, thereby activating pro-mitogenic/oncogenic Wnt signaling. We found that, upon tyrosine dephosphorylation by SHP2, parafibromin acquires the ability to stably bind β-catenin. The parafibromin/β-catenin interaction overrides parafibromin/SUV39H1-mediated transrepression and induces expression of Wnt target genes, including cyclin D1 and c-myc . Hence, SHP2 governs the opposing functions of parafibromin, deregulation of which may cause the development of tumors or developmental malformations.
Deregulation of SHP2 is associated with malignant diseases as well as developmental disorders. Although SHP2 is required for full activation of RAS signaling, other potential roles in cell physiology have not been elucidated. Here we show that SHP2 dephosphorylates parafibromin/Cdc73, a core component of the RNA polymerase II-associated factor (PAF) complex. Parafibromin is known to act as a tumor suppressor that inhibits cyclin D1 and c-myc by recruiting SUV39H1 histone methyltransferase. However, parafibromin can also act in the opposing direction by binding beta -catenin, thereby activating promitogenic/oncogenic Wnt signaling. We found that, on tyrosine dephosphorylation by SHP2, parafibromin acquires the ability to stably bind beta -catenin. The parafibromin/ beta -catenin interaction overrides parafibromin/SUV39H1-mediated transrepression and induces expression of Wnt target genes, including cyclin D1 and c-myc. Hence, SHP2 governs the opposing functions of parafibromin, deregulation of which may cause the development of tumors or developmental malformations.
Author Tsutsumi, Ryouhei
Seidi, Azadeh
Fernandez, Minerva
Cho, Taewoo
Obuse, Chikashi
Karisch, Robert
Kikuchi, Ippei
Hatakeyama, Masanori
Rozenblatt-Rosen, Orit
Meyerson, Matthew
Neel, Benjamin G.
Takahashi, Atsushi
Saito, Yasuhiro
Ohnishi, Naomi
AuthorAffiliation 2 Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan
6 Research Center for Infection-associated Cancer, Institute for Genetic Medicine, Hokkaido University, Sapporo 060-0815, Japan
8 Broad Institute of Harvard and MIT, Cambridge, Massachusetts 02142, USA
3 Division of Molecular Life Science, Graduate School of Life Science, Hokkaido University, Sapporo 001-0021, Japan
1 Division of Microbiology, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan
5 Princess Margaret Hospital & Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2M9, Canada
7 Department of Medical Oncology & Center for Cancer Genome Discovery, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA
4 Campbell Family Research Institute, Ontario Cancer Institute, Toronto, Ontario M5G 1L7, Canada
AuthorAffiliation_xml – name: 4 Campbell Family Research Institute, Ontario Cancer Institute, Toronto, Ontario M5G 1L7, Canada
– name: 1 Division of Microbiology, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan
– name: 6 Research Center for Infection-associated Cancer, Institute for Genetic Medicine, Hokkaido University, Sapporo 060-0815, Japan
– name: 3 Division of Molecular Life Science, Graduate School of Life Science, Hokkaido University, Sapporo 001-0021, Japan
– name: 2 Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan
– name: 8 Broad Institute of Harvard and MIT, Cambridge, Massachusetts 02142, USA
– name: 5 Princess Margaret Hospital & Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2M9, Canada
– name: 7 Department of Medical Oncology & Center for Cancer Genome Discovery, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA
Author_xml – sequence: 1
  givenname: Atsushi
  surname: Takahashi
  fullname: Takahashi, Atsushi
  organization: Division of Microbiology, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan
– sequence: 2
  givenname: Ryouhei
  surname: Tsutsumi
  fullname: Tsutsumi, Ryouhei
  organization: Division of Microbiology, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan
– sequence: 3
  givenname: Ippei
  surname: Kikuchi
  fullname: Kikuchi, Ippei
  organization: Division of Microbiology, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan
– sequence: 4
  givenname: Chikashi
  surname: Obuse
  fullname: Obuse, Chikashi
  organization: Division of Molecular Life Science, Graduate School of Life Science, 001-0021, Hokkaido University, Sapporo, Japan
– sequence: 5
  givenname: Yasuhiro
  surname: Saito
  fullname: Saito, Yasuhiro
  organization: Division of Microbiology, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan
– sequence: 6
  givenname: Azadeh
  surname: Seidi
  fullname: Seidi, Azadeh
  organization: Division of Microbiology, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan
– sequence: 7
  givenname: Robert
  surname: Karisch
  fullname: Karisch, Robert
  organization: Campbell Family Cancer Research Institute, Ontario Cancer Institute and Princess Margaret Hospital, University Health Network, Toronto, ON M5G 1L7, Canada
– sequence: 8
  givenname: Minerva
  surname: Fernandez
  fullname: Fernandez, Minerva
  organization: Campbell Family Cancer Research Institute, Ontario Cancer Institute and Princess Margaret Hospital, University Health Network, Toronto, ON M5G 1L7, Canada
– sequence: 9
  givenname: Taewoo
  surname: Cho
  fullname: Cho, Taewoo
  organization: Campbell Family Cancer Research Institute, Ontario Cancer Institute and Princess Margaret Hospital, University Health Network, Toronto, ON M5G 1L7, Canada
– sequence: 10
  givenname: Naomi
  surname: Ohnishi
  fullname: Ohnishi, Naomi
  organization: Research Center for Infection-Associated Cancer, Institute for Genetic Medicine, 060-0185, Hokkaido University, Sapporo, Japan
– sequence: 11
  givenname: Orit
  surname: Rozenblatt-Rosen
  fullname: Rozenblatt-Rosen, Orit
  organization: Department of Medical Oncology and Center for Cancer Genome Discovery, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA
– sequence: 12
  givenname: Matthew
  surname: Meyerson
  fullname: Meyerson, Matthew
  organization: Department of Medical Oncology and Center for Cancer Genome Discovery, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA
– sequence: 13
  givenname: Benjamin G.
  surname: Neel
  fullname: Neel, Benjamin G.
  organization: Campbell Family Cancer Research Institute, Ontario Cancer Institute and Princess Margaret Hospital, University Health Network, Toronto, ON M5G 1L7, Canada
– sequence: 14
  givenname: Masanori
  surname: Hatakeyama
  fullname: Hatakeyama, Masanori
  email: mhata@m.u-tokyo.ac.jp
  organization: Division of Microbiology, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/21726809$$D View this record in MEDLINE/PubMed
BookMark eNqFkUuP2yAUhVE1VefR_oOqZddVPGCDgU2lKn1MpZEmUjJrhPF1QmSDC3ak-fclSjptN-2Ki_ju0eGca3ThgweE3lJSUELr230xhN5CX5SE0oLwglD2Al1RosSC0ZpdnOdS1PwSXae0J5ngUr1ClyUVZS2JukLt-m5V4s1TDMl5wKtdSOPOTCYBXgZ_gDglvDLRdK6JYXD-dtlaUeEuX7DBm3kIEa_ncYyQUh6ngI3HD96GLXhn8efossZr9LIzfYI35_MGPX79slneLe4fvn1ffrpfWC7ZtOgIYVIZ3ijGGqhETeuWdhJ4Nt0IolgNbVNaKUVjFLGlqgwjFjpLQArDVXWDPp50x7kZoLXgp2h6PUY3mPikg3H67xfvdnobDprnRGVFssCHs0AMP2ZIkx5cyhn3xkOYk1ZEUEGVVP8lpeBESl7VmWQn0uaMU4Tu2Q8l-tik3utTk_rYpCZc557y2rs___K89Ku6DLw_AZ0J2myjS_pxnRVqkns-Ur_jgJz5wUHUyTrwFloXwU66De7fHn4CXwy9CQ
CitedBy_id crossref_primary_10_1101_gad_198051_112
crossref_primary_10_18632_oncotarget_25204
crossref_primary_10_3892_ijo_2013_2191
crossref_primary_10_1016_j_ejmg_2015_08_005
crossref_primary_10_1016_j_jcmgh_2015_11_001
crossref_primary_10_1210_en_2016_1286
crossref_primary_10_1002_jbmr_3650
crossref_primary_10_1242_jcs_260593
crossref_primary_10_1016_j_bbagrm_2012_08_011
crossref_primary_10_1016_j_jmb_2021_166979
crossref_primary_10_1016_j_isci_2018_01_003
crossref_primary_10_1038_onc_2015_184
crossref_primary_10_1186_s13046_019_1417_3
crossref_primary_10_1371_journal_pone_0092904
crossref_primary_10_1007_s00535_016_1299_5
crossref_primary_10_1210_clinem_dgad455
crossref_primary_10_1038_s41598_017_15715_9
crossref_primary_10_1042_BCJ20210254
crossref_primary_10_1016_j_jcmgh_2019_03_003
crossref_primary_10_3389_fimmu_2024_1340726
crossref_primary_10_1016_j_bbrc_2023_07_051
crossref_primary_10_1016_j_devcel_2013_08_013
crossref_primary_10_1097_MPH_0000000000000443
crossref_primary_10_4155_fmc_2021_0324
crossref_primary_10_1007_s12022_020_09656_9
crossref_primary_10_1172_jci_insight_92061
crossref_primary_10_1073_pnas_1700978114
crossref_primary_10_15252_embj_2021109720
crossref_primary_10_1158_0008_5472_CAN_13_2321
crossref_primary_10_1038_cddis_2013_98
crossref_primary_10_3390_jcm11071773
crossref_primary_10_1074_jbc_M111_258673
crossref_primary_10_1210_clinem_dgad368
crossref_primary_10_1007_s13277_015_4103_x
crossref_primary_10_1016_j_tibs_2017_08_003
crossref_primary_10_3892_mmr_2020_11529
crossref_primary_10_1007_s13402_022_00698_1
crossref_primary_10_1038_ncomms15741
crossref_primary_10_1016_j_chom_2014_02_008
crossref_primary_10_1097_JCMA_0000000000000957
crossref_primary_10_1038_ncomms12751
crossref_primary_10_2183_pjab_93_013
crossref_primary_10_1002_jcb_23424
crossref_primary_10_1074_jbc_RA120_013820
crossref_primary_10_1007_s11154_013_9282_4
crossref_primary_10_1016_j_ijbiomac_2022_04_095
crossref_primary_10_1038_ncomms12887
crossref_primary_10_1093_nar_gkx1131
crossref_primary_10_3892_ijo_2024_5610
crossref_primary_10_1002_ajmg_a_37295
crossref_primary_10_1534_g3_116_034231
crossref_primary_10_1038_ncomms6409
crossref_primary_10_1038_nrendo_2012_102
crossref_primary_10_7314_APJCP_2013_14_7_4249
crossref_primary_10_1002_hep_28919
crossref_primary_10_1002_mc_22785
crossref_primary_10_3390_molecules27227774
crossref_primary_10_1021_acs_jproteome_9b00130
crossref_primary_10_1126_science_aad2338
crossref_primary_10_18632_oncotarget_20446
crossref_primary_10_1210_jendso_bvab087
crossref_primary_10_3412_jsb_70_319
crossref_primary_10_1038_s41423_019_0339_5
crossref_primary_10_1016_j_jprot_2019_02_008
crossref_primary_10_1016_j_tcb_2015_05_002
crossref_primary_10_1016_j_bbrc_2015_12_117
crossref_primary_10_1002_ijc_34769
crossref_primary_10_4248_BR201301004
crossref_primary_10_1371_journal_pone_0061055
crossref_primary_10_1038_s41379_019_0252_6
crossref_primary_10_3389_fcell_2022_1006400
crossref_primary_10_1016_j_biocel_2017_09_013
crossref_primary_10_1210_endrev_bnad009
crossref_primary_10_18632_oncotarget_15377
crossref_primary_10_1073_pnas_1705816114
crossref_primary_10_1093_carcin_bgu025
crossref_primary_10_3390_cancers11070926
Cites_doi 10.1242/dev.033910
10.1073/pnas.0604130103
10.1074/jbc.M805138200
10.1038/nature05765
10.1038/ng772
10.1016/S0968-0004(03)00091-4
10.1038/sj.onc.1210445
10.1128/MCB.00654-07
10.1016/j.cell.2006.01.053
10.1038/sj.onc.1210582
10.1016/j.devcel.2006.01.002
10.1038/ncb1141
10.1111/j.1349-7006.2004.tb03229.x
10.1128/MCB.25.2.612-620.2005
10.1182/blood-2004-10-4057
10.1016/j.cell.2009.02.037
10.1016/j.bbagrm.2010.01.001
10.1038/ng.425
10.1111/j.1365-2796.2009.02107.x
10.1093/nar/gkp991
10.1083/jcb.130.2.461
10.1016/j.ceb.2005.08.009
10.1073/pnas.0710725105
10.1038/cr.2007.69
10.1126/science.1067147
10.1016/j.ydbio.2009.11.030
10.1016/j.gde.2009.04.001
10.1002/jcb.22020
10.1038/ng1048
10.1002/eji.200738118
10.1002/humu.20748
10.1016/j.devcel.2009.06.016
10.1016/j.gde.2006.12.011
10.1038/sj.onc.1208274
10.1038/ncpendmet0292
10.1074/jbc.M207536200
10.1182/blood.V96.6.2310
10.1038/nm1341
10.1016/j.cell.2009.12.050
10.1111/j.1365-2613.2009.00667.x
10.1053/j.gastro.2006.08.011
10.1093/genetics/159.3.1073
10.1101/gad.1295405
10.1016/j.bbrc.2006.08.169
10.1038/nrc1433
10.1038/sj.onc.1211019
10.1038/nm1084
10.1182/blood-2006-07-028829
10.1074/jbc.M210670200
ContentType Journal Article
Copyright 2011 Elsevier Inc.
Copyright © 2011 Elsevier Inc. All rights reserved.
Copyright_xml – notice: 2011 Elsevier Inc.
– notice: Copyright © 2011 Elsevier Inc. All rights reserved.
DBID 6I.
AAFTH
FBQ
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7X8
7TO
H94
5PM
DOI 10.1016/j.molcel.2011.05.014
DatabaseName ScienceDirect Open Access Titles
Elsevier:ScienceDirect:Open Access
AGRIS
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
MEDLINE - Academic
Oncogenes and Growth Factors Abstracts
AIDS and Cancer Research Abstracts
PubMed Central (Full Participant titles)
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
MEDLINE - Academic
Oncogenes and Growth Factors Abstracts
AIDS and Cancer Research Abstracts
DatabaseTitleList


MEDLINE
Oncogenes and Growth Factors Abstracts
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 3
  dbid: FBQ
  name: AGRIS
  url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN
  sourceTypes: Publisher
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 1097-4164
EndPage 56
ExternalDocumentID 10_1016_j_molcel_2011_05_014
21726809
US201600012172
S1097276511003819
Genre Research Support, Non-U.S. Gov't
Journal Article
Research Support, N.I.H., Extramural
GrantInformation_xml – fundername: Canadian Institutes of Health Research
– fundername: NCI NIH HHS
  grantid: R01 CA049152
– fundername: NCI NIH HHS
  grantid: R37CA39152
GroupedDBID ---
--K
-DZ
-~X
0R~
123
1~5
2WC
4.4
457
4G.
5RE
62-
6I.
7-5
AACTN
AAEDT
AAEDW
AAFTH
AAIAV
AAIKJ
AAKRW
AAKUH
AALRI
AAUCE
AAVLU
AAXJY
AAXUO
ABJNI
ABMAC
ABMWF
ABVKL
ACGFO
ACGFS
ACNCT
ADBBV
ADEZE
ADJPV
AEFWE
AENEX
AEXQZ
AFFNX
AFTJW
AGHFR
AGKMS
AITUG
ALKID
ALMA_UNASSIGNED_HOLDINGS
AMRAJ
ASPBG
AVWKF
AZFZN
BAWUL
CS3
DIK
DU5
E3Z
EBS
EJD
F5P
FCP
FDB
FEDTE
FIRID
HH5
HVGLF
HZ~
IH2
IHE
IXB
J1W
JIG
KQ8
L7B
M3Z
M41
N9A
NCXOZ
O-L
O9-
OK1
P2P
RCE
RIG
ROL
RPZ
SDG
SES
SSZ
TR2
WQ6
ZA5
.55
.GJ
29M
3O-
53G
5VS
AAQFI
AAQXK
ABPTK
ADMUD
AEQTP
FBQ
FGOYB
OZT
R2-
UHS
X7M
ZGI
ZXP
0SF
AAHBH
AAMRU
ADVLN
AKAPO
AKRWK
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
ACRPL
ADNMO
CITATION
7X8
7TO
H94
5PM
ID FETCH-LOGICAL-c584t-f00489a5b944be37616d1f8e5589b70946edb2c887ba90c293a40cefc0e87a593
IEDL.DBID ABVKL
ISSN 1097-2765
IngestDate Tue Sep 17 21:16:06 EDT 2024
Fri Oct 25 04:09:51 EDT 2024
Fri Oct 25 02:01:24 EDT 2024
Fri Dec 06 03:24:07 EST 2024
Sat Sep 28 07:48:53 EDT 2024
Wed Dec 27 19:17:17 EST 2023
Fri Feb 23 02:19:48 EST 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 1
Language English
License http://www.elsevier.com/open-access/userlicense/1.0
Copyright © 2011 Elsevier Inc. All rights reserved.
https://www.elsevier.com/tdm/userlicense/1.0
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c584t-f00489a5b944be37616d1f8e5589b70946edb2c887ba90c293a40cefc0e87a593
Notes http://dx.doi.org/10.1016/j.molcel.2011.05.014
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ObjectType-Article-2
ObjectType-Feature-1
OpenAccessLink https://www.sciencedirect.com/science/article/pii/S1097276511003819
PMID 21726809
PQID 875088536
PQPubID 23479
PageCount 12
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_5101830
proquest_miscellaneous_907171989
proquest_miscellaneous_875088536
crossref_primary_10_1016_j_molcel_2011_05_014
pubmed_primary_21726809
fao_agris_US201600012172
elsevier_sciencedirect_doi_10_1016_j_molcel_2011_05_014
PublicationCentury 2000
PublicationDate 2011-07-08
PublicationDateYYYYMMDD 2011-07-08
PublicationDate_xml – month: 07
  year: 2011
  text: 2011-07-08
  day: 08
PublicationDecade 2010
PublicationPlace United States
PublicationPlace_xml – name: United States
PublicationTitle Molecular cell
PublicationTitleAlternate Mol Cell
PublicationYear 2011
Publisher Elsevier Inc
Publisher_xml – name: Elsevier Inc
References Chaudhary, Deb, Moniaux, Ponnusamy, Batra (bib9) 2007; 26
Tidyman, Rauen (bib41) 2009; 19
Jakob, Schroeder, Lukosz, Büchner, Spyridopoulos, Altschmied, Haendeler (bib21) 2008; 283
Tartaglia, Mehler, Goldberg, Zampino, Brunner, Kremer, van der Burgt, Crosby, Ion, Jeffery (bib40) 2001; 29
Yang, Han, Youn, Cho (bib49) 2010; 38
Luo, Brooks, Ye, Hamoudi, Poulogiannis, Patek, Winton, Arends (bib27) 2009; 90
Kim, Guermah, Roeder (bib23) 2010; 140
MacDonald, Tamai, He (bib28) 2009; 17
Jaehning (bib20) 2010; 1799
Lin, Zhang, Panicker, Simonds (bib26) 2008; 105
Iwata, Mizusawa, Taketani, Itakura, Yoshimoto (bib19) 2007; 26
Zhang, Kong, Tan, Pappas, Wang, Chen, Farber, Zhang, Koo, Weinreich (bib50) 2006; 350
Rozenblatt-Rosen, Hughes, Nannepaga, Shanmugam, Copeland, Guszczynski, Resau, Meyerson (bib36) 2005; 25
Cooper, Shannon, Loken, Weaver, Stephens, Sievers (bib11) 2000; 96
Johnson Hamlet, Perkins (bib15) 2001; 159
Cordeddu, Di Schiavi, Pennacchio, Ma'ayan, Sarkozy, Fodale, Cecchetti, Cardinale, Martin, Schackwitz (bib12) 2009; 41
Hatakeyama (bib16) 2004; 4
Sansom, Meniel, Wilkins, Cole, Oien, Marsh, Jamieson, Guerra, Ashton, Barbacid, Clarke (bib38) 2006; 103
Gregorieff, Clevers (bib14) 2005; 19
Woodard, Lin, Zhang, Agarwal, Marx, Simonds (bib45) 2005; 24
Bentires-Alj, Gil, Chan, Wang, Wang, Imanaka, Harris, Richardson, Neel, Gu (bib5) 2006; 12
Caca, Kolligs, Ji, Hayes, Qian, Yahanda, Rimm, Costa, Fearon (bib6) 1999; 10
Dreijerink, Hoppener, Timmers, Lips (bib13) 2006; 2
Higuchi, Tsutsumi, Higashi, Hatakeyama (bib18) 2004; 95
Phelps, Chidester, Dehghanizadeh, Phelps, Sandoval, Rai, Broadbent, Sarkar, Burt, Jones (bib35) 2009; 137
Carpten, Robbins, Villablanca, Forsberg, Presciuttini, Bailey-Wilson, Simonds, Gillanders, Kennedy, Chen (bib7) 2002; 32
Newey, Bowl, Thakker (bib34) 2009; 266
van Amerongen, Nusse (bib43) 2009; 136
Janssen, Alberici, Fsihi, Gaspar, Breukel, Franken, Rosty, Abal, El Marjou, Smits (bib22) 2006; 131
Mohi, Neel (bib30) 2007; 17
Higashi, Tsutsumi, Muto, Sugiyama, Azuma, Asaka, Hatakeyama (bib17) 2002; 295
Nemeth, Bodine (bib33) 2007; 17
Chen, Alman (bib10) 2009; 106
Staal, Sen (bib39) 2008; 38
Wang, Bowl, Bender, Peng, Farber, Chen, Ali, Zhang, Alberts, Thakker (bib44) 2008; 28
Araki, Mohi, Ismat, Bronson, Williams, Kutok, Yang, Pao, Gilliland, Epstein, Neel (bib4) 2004; 10
Lilien, Balsamo (bib25) 2005; 17
Townsley, Cliffe, Bienz (bib42) 2004; 6
Yang, Klaman, Chen, Araki, Harada, Thomas, George, Neel (bib48) 2006; 10
Miyamoto, Miyamoto, Takahashi, Yomogita, Higashi, Kondo, Hatakeyama (bib29) 2008; 27
Alfieri, Cheek, Chakraborty, Yutzey (bib2) 2010; 338
Saadat, Higashi, Obuse, Umeda, Murata-Kamiya, Saito, Lu, Ohnishi, Azuma, Suzuki (bib37) 2007; 447
Xu, Yu, Zheng, Zhao, Dong, He, Liang, Lu, Fang, Gan (bib47) 2005; 106
Neel, Gu, Pao (bib32) 2003; 28
Chan, Feng (bib8) 2007; 109
Wu, Hong, Wang, Ling, Dragoi, Chung, Campbell, Han, Feng, Chin (bib46) 2002; 277
Kinch, Clark, Der, Burridge (bib24) 1995; 130
Aoki, Niihori, Narumi, Kure, Matsubara (bib3) 2008; 29
Mosimann, Hausmann, Basler (bib31) 2006; 125
Agazie, Hayman (bib1) 2003; 278
17053061 - Blood. 2007 Feb 1;109(3):862-7
16989776 - Biochem Biophys Res Commun. 2006 Nov 10;350(1):17-24
17227708 - Curr Opin Genet Dev. 2007 Feb;17(1):23-30
12270932 - J Biol Chem. 2002 Dec 6;277(49):47572-80
10979983 - Blood. 2000 Sep 15;96(6):2310-3
17024155 - Nat Clin Pract Endocrinol Metab. 2006 Oct;2(10):562-70
15273746 - Nat Med. 2004 Aug;10(8):849-57
16099633 - Curr Opin Cell Biol. 2005 Oct;17(5):459-65
11704759 - Nat Genet. 2001 Dec;29(4):465-8
19906718 - Nucleic Acids Res. 2010 Jan;38(2):382-90
11729154 - Genetics. 2001 Nov;159(3):1073-87
12582165 - J Biol Chem. 2003 Apr 18;278(16):13952-8
11743164 - Science. 2002 Jan 25;295(5555):683-6
18581335 - Eur J Immunol. 2008 Jul;38(7):1788-94
18212049 - Mol Cell Biol. 2008 May;28(9):2930-40
16959882 - Proc Natl Acad Sci U S A. 2006 Sep 19;103(38):14122-7
19961844 - Dev Biol. 2010 Feb 15;338(2):127-35
17768401 - Cell Res. 2007 Sep;17(9):746-58
19467855 - Curr Opin Genet Dev. 2009 Jun;19(3):230-6
15208637 - Nat Cell Biol. 2004 Jul;6(7):626-33
19127541 - J Cell Biochem. 2009 Feb 15;106(3):353-62
17030180 - Gastroenterology. 2006 Oct;131(4):1096-109
19450512 - Cell. 2009 May 15;137(4):623-34
19684605 - Nat Genet. 2009 Sep;41(9):1022-6
18223690 - Oncogene. 2008 Jun 5;27(25):3508-15
10392898 - Cell Growth Differ. 1999 Jun;10(6):369-76
17507984 - Nature. 2007 May 17;447(7142):330-3
19765110 - Int J Exp Pathol. 2009 Oct;90(5):558-74
17404568 - Oncogene. 2007 Sep 13;26(42):6176-83
18470943 - Hum Mutat. 2008 Aug;29(8):992-1006
20060942 - Biochim Biophys Acta. 2010 May-Jun;1799(5-6):379-88
7542250 - J Cell Biol. 1995 Jul;130(2):461-71
20178742 - Cell. 2010 Feb 19;140(4):491-503
19619488 - Dev Cell. 2009 Jul;17(1):9-26
15833914 - Genes Dev. 2005 Apr 15;19(8):877-90
18829466 - J Biol Chem. 2008 Nov 28;283(48):33155-61
19522828 - J Intern Med. 2009 Jul;266(1):84-98
19736321 - Development. 2009 Oct;136(19):3205-14
15632063 - Mol Cell Biol. 2005 Jan;25(2):612-20
16630820 - Cell. 2006 Apr 21;125(2):327-41
12826400 - Trends Biochem Sci. 2003 Jun;28(6):284-93
12434154 - Nat Genet. 2002 Dec;32(4):676-80
16369543 - Nat Med. 2006 Jan;12(1):114-21
15580289 - Oncogene. 2005 Feb 10;24(7):1272-6
17599057 - Oncogene. 2007 Nov 29;26(54):7499-507
16030196 - Blood. 2005 Nov 1;106(9):3142-9
15343275 - Nat Rev Cancer. 2004 Sep;4(9):688-94
18987311 - Proc Natl Acad Sci U S A. 2008 Nov 11;105(45):17420-5
Zhang (10.1016/j.molcel.2011.05.014_bib50) 2006; 350
Dreijerink (10.1016/j.molcel.2011.05.014_bib13) 2006; 2
Xu (10.1016/j.molcel.2011.05.014_bib47) 2005; 106
Bentires-Alj (10.1016/j.molcel.2011.05.014_bib5) 2006; 12
Cooper (10.1016/j.molcel.2011.05.014_bib11) 2000; 96
Phelps (10.1016/j.molcel.2011.05.014_bib35) 2009; 137
Miyamoto (10.1016/j.molcel.2011.05.014_bib29) 2008; 27
Luo (10.1016/j.molcel.2011.05.014_bib27) 2009; 90
Cordeddu (10.1016/j.molcel.2011.05.014_bib12) 2009; 41
Caca (10.1016/j.molcel.2011.05.014_bib6) 1999; 10
Lilien (10.1016/j.molcel.2011.05.014_bib25) 2005; 17
Carpten (10.1016/j.molcel.2011.05.014_bib7) 2002; 32
Iwata (10.1016/j.molcel.2011.05.014_bib19) 2007; 26
Yang (10.1016/j.molcel.2011.05.014_bib49) 2010; 38
van Amerongen (10.1016/j.molcel.2011.05.014_bib43) 2009; 136
Townsley (10.1016/j.molcel.2011.05.014_bib42) 2004; 6
Chaudhary (10.1016/j.molcel.2011.05.014_bib9) 2007; 26
Jakob (10.1016/j.molcel.2011.05.014_bib21) 2008; 283
Tidyman (10.1016/j.molcel.2011.05.014_bib41) 2009; 19
Janssen (10.1016/j.molcel.2011.05.014_bib22) 2006; 131
Staal (10.1016/j.molcel.2011.05.014_bib39) 2008; 38
Aoki (10.1016/j.molcel.2011.05.014_bib3) 2008; 29
Gregorieff (10.1016/j.molcel.2011.05.014_bib14) 2005; 19
Newey (10.1016/j.molcel.2011.05.014_bib34) 2009; 266
Sansom (10.1016/j.molcel.2011.05.014_bib38) 2006; 103
Neel (10.1016/j.molcel.2011.05.014_bib32) 2003; 28
Higuchi (10.1016/j.molcel.2011.05.014_bib18) 2004; 95
Chen (10.1016/j.molcel.2011.05.014_bib10) 2009; 106
Lin (10.1016/j.molcel.2011.05.014_bib26) 2008; 105
Kim (10.1016/j.molcel.2011.05.014_bib23) 2010; 140
Araki (10.1016/j.molcel.2011.05.014_bib4) 2004; 10
Nemeth (10.1016/j.molcel.2011.05.014_bib33) 2007; 17
Kinch (10.1016/j.molcel.2011.05.014_bib24) 1995; 130
Hatakeyama (10.1016/j.molcel.2011.05.014_bib16) 2004; 4
MacDonald (10.1016/j.molcel.2011.05.014_bib28) 2009; 17
Wu (10.1016/j.molcel.2011.05.014_bib46) 2002; 277
Yang (10.1016/j.molcel.2011.05.014_bib48) 2006; 10
Mohi (10.1016/j.molcel.2011.05.014_bib30) 2007; 17
Higashi (10.1016/j.molcel.2011.05.014_bib17) 2002; 295
Jaehning (10.1016/j.molcel.2011.05.014_bib20) 2010; 1799
Mosimann (10.1016/j.molcel.2011.05.014_bib31) 2006; 125
Rozenblatt-Rosen (10.1016/j.molcel.2011.05.014_bib36) 2005; 25
Tartaglia (10.1016/j.molcel.2011.05.014_bib40) 2001; 29
Saadat (10.1016/j.molcel.2011.05.014_bib37) 2007; 447
Chan (10.1016/j.molcel.2011.05.014_bib8) 2007; 109
Wang (10.1016/j.molcel.2011.05.014_bib44) 2008; 28
Alfieri (10.1016/j.molcel.2011.05.014_bib2) 2010; 338
Johnson Hamlet (10.1016/j.molcel.2011.05.014_bib15) 2001; 159
Woodard (10.1016/j.molcel.2011.05.014_bib45) 2005; 24
Agazie (10.1016/j.molcel.2011.05.014_bib1) 2003; 278
References_xml – volume: 12
  start-page: 114
  year: 2006
  end-page: 121
  ident: bib5
  article-title: A role for the scaffolding adapter GAB2 in breast cancer
  publication-title: Nat. Med.
  contributor:
    fullname: Gu
– volume: 17
  start-page: 459
  year: 2005
  end-page: 465
  ident: bib25
  article-title: The regulation of cadherin-mediated adhesion by tyrosine phosphorylation/dephosphorylation of β-catenin
  publication-title: Curr. Opin. Cell Biol.
  contributor:
    fullname: Balsamo
– volume: 19
  start-page: 877
  year: 2005
  end-page: 890
  ident: bib14
  article-title: Wnt signaling in the intestinal epithelium: from endoderm to cancer
  publication-title: Genes Dev.
  contributor:
    fullname: Clevers
– volume: 350
  start-page: 17
  year: 2006
  end-page: 24
  ident: bib50
  article-title: Parafibromin inhibits cancer cell growth and causes G1 phase arrest
  publication-title: Biochem. Biophys. Res. Commun.
  contributor:
    fullname: Weinreich
– volume: 17
  start-page: 23
  year: 2007
  end-page: 30
  ident: bib30
  article-title: The role of Shp2 (
  publication-title: Curr. Opin. Genet. Dev.
  contributor:
    fullname: Neel
– volume: 338
  start-page: 127
  year: 2010
  end-page: 135
  ident: bib2
  article-title: Wnt signaling in heart valve development and osteogenic gene induction
  publication-title: Dev. Biol.
  contributor:
    fullname: Yutzey
– volume: 29
  start-page: 465
  year: 2001
  end-page: 468
  ident: bib40
  article-title: Mutations in
  publication-title: Nat. Genet.
  contributor:
    fullname: Jeffery
– volume: 95
  start-page: 442
  year: 2004
  end-page: 447
  ident: bib18
  article-title: Conditional gene silencing utilizing the
  publication-title: Cancer Sci.
  contributor:
    fullname: Hatakeyama
– volume: 159
  start-page: 1073
  year: 2001
  end-page: 1087
  ident: bib15
  article-title: Analysis of corkscrew signaling in the
  publication-title: Genetics
  contributor:
    fullname: Perkins
– volume: 4
  start-page: 688
  year: 2004
  end-page: 694
  ident: bib16
  article-title: Oncogenic mechanisms of the
  publication-title: Nat. Rev. Cancer
  contributor:
    fullname: Hatakeyama
– volume: 28
  start-page: 284
  year: 2003
  end-page: 293
  ident: bib32
  article-title: The ‘Shp’ing news: SH2 domain-containing tyrosine phosphatases in cell signaling
  publication-title: Trends Biochem. Sci.
  contributor:
    fullname: Pao
– volume: 17
  start-page: 9
  year: 2009
  end-page: 26
  ident: bib28
  article-title: Wnt/β-catenin signaling: components, mechanisms, and diseases
  publication-title: Dev. Cell
  contributor:
    fullname: He
– volume: 295
  start-page: 683
  year: 2002
  end-page: 686
  ident: bib17
  article-title: SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein
  publication-title: Science
  contributor:
    fullname: Hatakeyama
– volume: 17
  start-page: 746
  year: 2007
  end-page: 758
  ident: bib33
  article-title: Regulation of hematopoiesis and the hematopoietic stem cell niche by Wnt signaling pathways
  publication-title: Cell Res.
  contributor:
    fullname: Bodine
– volume: 277
  start-page: 47572
  year: 2002
  end-page: 47580
  ident: bib46
  article-title: SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Chin
– volume: 447
  start-page: 330
  year: 2007
  end-page: 333
  ident: bib37
  article-title: CagA targets PAR1/MARK kinase to disrupt epithelial cell polarity
  publication-title: Nature
  contributor:
    fullname: Suzuki
– volume: 278
  start-page: 13952
  year: 2003
  end-page: 13958
  ident: bib1
  article-title: Development of an efficient “substrate-trapping” mutant of Src homology phosphotyrosine phosphatase 2 and identification of the epidermal growth factor receptor, Gab1, and three other proteins as target substrates
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Hayman
– volume: 130
  start-page: 461
  year: 1995
  end-page: 471
  ident: bib24
  article-title: Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia
  publication-title: J. Cell Biol.
  contributor:
    fullname: Burridge
– volume: 283
  start-page: 33155
  year: 2008
  end-page: 33161
  ident: bib21
  article-title: Nuclear protein tyrosine phosphatase Shp-2 is one important negative regulator of nuclear export of telomerase reverse transcriptase
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Haendeler
– volume: 6
  start-page: 626
  year: 2004
  end-page: 633
  ident: bib42
  article-title: Pygopus and Legless target Armadillo/β-catenin to the nucleus to enable its transcriptional co-activator function
  publication-title: Nat. Cell Biol.
  contributor:
    fullname: Bienz
– volume: 266
  start-page: 84
  year: 2009
  end-page: 98
  ident: bib34
  article-title: Parafibromin—functional insights
  publication-title: J. Intern. Med.
  contributor:
    fullname: Thakker
– volume: 109
  start-page: 862
  year: 2007
  end-page: 867
  ident: bib8
  article-title: is the first identified proto-oncogene that encodes a tyrosine phosphatase
  publication-title: Blood
  contributor:
    fullname: Feng
– volume: 96
  start-page: 2310
  year: 2000
  end-page: 2313
  ident: bib11
  article-title: Evidence that juvenile myelomonocytic leukemia can arise from a pluripotential stem cell
  publication-title: Blood
  contributor:
    fullname: Sievers
– volume: 27
  start-page: 3508
  year: 2008
  end-page: 3515
  ident: bib29
  article-title: Isolation of a distinct class of gain-of-function SHP-2 mutants with oncogenic RAS-like transforming activity from solid tumors
  publication-title: Oncogene
  contributor:
    fullname: Hatakeyama
– volume: 38
  start-page: 382
  year: 2010
  end-page: 390
  ident: bib49
  article-title: The tumor suppressor, parafibromin, mediates histone H3 K9 methylation for cyclin D1 repression
  publication-title: Nucleic Acids Res.
  contributor:
    fullname: Cho
– volume: 10
  start-page: 317
  year: 2006
  end-page: 327
  ident: bib48
  article-title: An Shp2/SFK/Ras/Erk signaling pathway controls trophoblast stem cell survival
  publication-title: Dev. Cell
  contributor:
    fullname: Neel
– volume: 2
  start-page: 562
  year: 2006
  end-page: 570
  ident: bib13
  article-title: Mechanisms of disease: multiple endocrine neoplasia type 1-relation to chromatin modifications and transcription regulation
  publication-title: Nat. Clin. Pract. Endocrinol. Metab.
  contributor:
    fullname: Lips
– volume: 26
  start-page: 6176
  year: 2007
  end-page: 6183
  ident: bib19
  article-title: Parafibromin tumor suppressor enhances cell growth in the cells expressing SV40 large T antigen
  publication-title: Oncogene
  contributor:
    fullname: Yoshimoto
– volume: 103
  start-page: 14122
  year: 2006
  end-page: 14127
  ident: bib38
  article-title: Loss of Apc allows phenotypic manifestation of the transforming properties of an endogenous K-
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Clarke
– volume: 137
  start-page: 623
  year: 2009
  end-page: 634
  ident: bib35
  article-title: A two-step model for colon adenoma initiation and progression caused by APC loss
  publication-title: Cell
  contributor:
    fullname: Jones
– volume: 1799
  start-page: 379
  year: 2010
  end-page: 388
  ident: bib20
  article-title: The Paf1 complex: platform or player in RNA polymerase II transcription?
  publication-title: Biochim. Biophys. Acta
  contributor:
    fullname: Jaehning
– volume: 32
  start-page: 676
  year: 2002
  end-page: 680
  ident: bib7
  article-title: , encoding parafibromin, is mutated in hyperparathyroidism-jaw tumor syndrome
  publication-title: Nat. Genet.
  contributor:
    fullname: Chen
– volume: 10
  start-page: 849
  year: 2004
  end-page: 857
  ident: bib4
  article-title: Mouse model of Noonan syndrome reveals cell type- and gene dosage-dependent effects of
  publication-title: Nat. Med.
  contributor:
    fullname: Neel
– volume: 28
  start-page: 2930
  year: 2008
  end-page: 2940
  ident: bib44
  article-title: Parafibromin, a component of the human PAF complex, regulates growth factors and is required for embryonic development and survival in adult mice
  publication-title: Mol. Cell. Biol.
  contributor:
    fullname: Thakker
– volume: 24
  start-page: 1272
  year: 2005
  end-page: 1276
  ident: bib45
  article-title: Parafibromin, product of the hyperparathyroidism-jaw tumor syndrome gene
  publication-title: Oncogene
  contributor:
    fullname: Simonds
– volume: 125
  start-page: 327
  year: 2006
  end-page: 341
  ident: bib31
  article-title: Parafibromin/Hyrax activates Wnt/Wg target gene transcription by direct association with β-catenin/Armadillo
  publication-title: Cell
  contributor:
    fullname: Basler
– volume: 19
  start-page: 230
  year: 2009
  end-page: 236
  ident: bib41
  article-title: The RASopathies: developmental syndromes of Ras/MAPK pathway dysregulation
  publication-title: Curr. Opin. Genet. Dev.
  contributor:
    fullname: Rauen
– volume: 140
  start-page: 491
  year: 2010
  end-page: 503
  ident: bib23
  article-title: The human PAF1 complex acts in chromatin transcription elongation both independently and cooperatively with SII/TFIIS
  publication-title: Cell
  contributor:
    fullname: Roeder
– volume: 106
  start-page: 353
  year: 2009
  end-page: 362
  ident: bib10
  article-title: Wnt pathway, an essential role in bone regeneration
  publication-title: J. Cell. Biochem.
  contributor:
    fullname: Alman
– volume: 136
  start-page: 3205
  year: 2009
  end-page: 3214
  ident: bib43
  article-title: Towards an integrated view of Wnt signaling in development
  publication-title: Development
  contributor:
    fullname: Nusse
– volume: 29
  start-page: 992
  year: 2008
  end-page: 1006
  ident: bib3
  article-title: The RAS/MAPK syndromes: novel roles of the RAS pathway in human genetic disorders
  publication-title: Hum. Mutat.
  contributor:
    fullname: Matsubara
– volume: 90
  start-page: 558
  year: 2009
  end-page: 574
  ident: bib27
  article-title: Mutated K-ras(Asp12) promotes tumourigenesis in Apc(Min) mice more in the large than the small intestines, with synergistic effects between K-ras and Wnt pathways
  publication-title: Int. J. Exp. Pathol.
  contributor:
    fullname: Arends
– volume: 131
  start-page: 1096
  year: 2006
  end-page: 1109
  ident: bib22
  article-title: and oncogenic
  publication-title: Gastroenterology
  contributor:
    fullname: Smits
– volume: 38
  start-page: 1788
  year: 2008
  end-page: 1794
  ident: bib39
  article-title: The canonical Wnt signaling pathway plays an important role in lymphopoiesis and hematopoiesis
  publication-title: Eur. J. Immunol.
  contributor:
    fullname: Sen
– volume: 105
  start-page: 17420
  year: 2008
  end-page: 17425
  ident: bib26
  article-title: The parafibromin tumor suppressor protein inhibits cell proliferation by repression of the
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Simonds
– volume: 10
  start-page: 369
  year: 1999
  end-page: 376
  ident: bib6
  article-title: Beta- and gamma-catenin mutations, but not E-cadherin inactivation, underlie T-cell factor/lymphoid enhancer factor transcriptional deregulation in gastric and pancreatic cancer
  publication-title: Cell Growth Differ.
  contributor:
    fullname: Fearon
– volume: 25
  start-page: 612
  year: 2005
  end-page: 620
  ident: bib36
  article-title: The parafibromin tumor suppressor protein is part of a human Paf1 complex
  publication-title: Mol. Cell. Biol.
  contributor:
    fullname: Meyerson
– volume: 41
  start-page: 1022
  year: 2009
  end-page: 1026
  ident: bib12
  article-title: Mutation of
  publication-title: Nat. Genet.
  contributor:
    fullname: Schackwitz
– volume: 26
  start-page: 7499
  year: 2007
  end-page: 7507
  ident: bib9
  article-title: Human RNA polymerase II-associated factor complex: dysregulation in cancer
  publication-title: Oncogene
  contributor:
    fullname: Batra
– volume: 106
  start-page: 3142
  year: 2005
  end-page: 3149
  ident: bib47
  article-title: Overexpression of Shp2 tyrosine phosphatase is implicated in leukemogenesis in adult human leukemia
  publication-title: Blood
  contributor:
    fullname: Gan
– volume: 136
  start-page: 3205
  year: 2009
  ident: 10.1016/j.molcel.2011.05.014_bib43
  article-title: Towards an integrated view of Wnt signaling in development
  publication-title: Development
  doi: 10.1242/dev.033910
  contributor:
    fullname: van Amerongen
– volume: 103
  start-page: 14122
  year: 2006
  ident: 10.1016/j.molcel.2011.05.014_bib38
  article-title: Loss of Apc allows phenotypic manifestation of the transforming properties of an endogenous K-ras oncogene in vivo
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0604130103
  contributor:
    fullname: Sansom
– volume: 283
  start-page: 33155
  year: 2008
  ident: 10.1016/j.molcel.2011.05.014_bib21
  article-title: Nuclear protein tyrosine phosphatase Shp-2 is one important negative regulator of nuclear export of telomerase reverse transcriptase
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M805138200
  contributor:
    fullname: Jakob
– volume: 447
  start-page: 330
  year: 2007
  ident: 10.1016/j.molcel.2011.05.014_bib37
  article-title: Helicobacter pylori CagA targets PAR1/MARK kinase to disrupt epithelial cell polarity
  publication-title: Nature
  doi: 10.1038/nature05765
  contributor:
    fullname: Saadat
– volume: 29
  start-page: 465
  year: 2001
  ident: 10.1016/j.molcel.2011.05.014_bib40
  article-title: Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome
  publication-title: Nat. Genet.
  doi: 10.1038/ng772
  contributor:
    fullname: Tartaglia
– volume: 28
  start-page: 284
  year: 2003
  ident: 10.1016/j.molcel.2011.05.014_bib32
  article-title: The ‘Shp’ing news: SH2 domain-containing tyrosine phosphatases in cell signaling
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/S0968-0004(03)00091-4
  contributor:
    fullname: Neel
– volume: 26
  start-page: 6176
  year: 2007
  ident: 10.1016/j.molcel.2011.05.014_bib19
  article-title: Parafibromin tumor suppressor enhances cell growth in the cells expressing SV40 large T antigen
  publication-title: Oncogene
  doi: 10.1038/sj.onc.1210445
  contributor:
    fullname: Iwata
– volume: 28
  start-page: 2930
  year: 2008
  ident: 10.1016/j.molcel.2011.05.014_bib44
  article-title: Parafibromin, a component of the human PAF complex, regulates growth factors and is required for embryonic development and survival in adult mice
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.00654-07
  contributor:
    fullname: Wang
– volume: 125
  start-page: 327
  year: 2006
  ident: 10.1016/j.molcel.2011.05.014_bib31
  article-title: Parafibromin/Hyrax activates Wnt/Wg target gene transcription by direct association with β-catenin/Armadillo
  publication-title: Cell
  doi: 10.1016/j.cell.2006.01.053
  contributor:
    fullname: Mosimann
– volume: 26
  start-page: 7499
  year: 2007
  ident: 10.1016/j.molcel.2011.05.014_bib9
  article-title: Human RNA polymerase II-associated factor complex: dysregulation in cancer
  publication-title: Oncogene
  doi: 10.1038/sj.onc.1210582
  contributor:
    fullname: Chaudhary
– volume: 10
  start-page: 317
  year: 2006
  ident: 10.1016/j.molcel.2011.05.014_bib48
  article-title: An Shp2/SFK/Ras/Erk signaling pathway controls trophoblast stem cell survival
  publication-title: Dev. Cell
  doi: 10.1016/j.devcel.2006.01.002
  contributor:
    fullname: Yang
– volume: 6
  start-page: 626
  year: 2004
  ident: 10.1016/j.molcel.2011.05.014_bib42
  article-title: Pygopus and Legless target Armadillo/β-catenin to the nucleus to enable its transcriptional co-activator function
  publication-title: Nat. Cell Biol.
  doi: 10.1038/ncb1141
  contributor:
    fullname: Townsley
– volume: 95
  start-page: 442
  year: 2004
  ident: 10.1016/j.molcel.2011.05.014_bib18
  article-title: Conditional gene silencing utilizing the lac repressor reveals a role of SHP-2 in cagA-positive Helicobacter pylori pathogenicity
  publication-title: Cancer Sci.
  doi: 10.1111/j.1349-7006.2004.tb03229.x
  contributor:
    fullname: Higuchi
– volume: 25
  start-page: 612
  year: 2005
  ident: 10.1016/j.molcel.2011.05.014_bib36
  article-title: The parafibromin tumor suppressor protein is part of a human Paf1 complex
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.25.2.612-620.2005
  contributor:
    fullname: Rozenblatt-Rosen
– volume: 10
  start-page: 369
  year: 1999
  ident: 10.1016/j.molcel.2011.05.014_bib6
  article-title: Beta- and gamma-catenin mutations, but not E-cadherin inactivation, underlie T-cell factor/lymphoid enhancer factor transcriptional deregulation in gastric and pancreatic cancer
  publication-title: Cell Growth Differ.
  contributor:
    fullname: Caca
– volume: 106
  start-page: 3142
  year: 2005
  ident: 10.1016/j.molcel.2011.05.014_bib47
  article-title: Overexpression of Shp2 tyrosine phosphatase is implicated in leukemogenesis in adult human leukemia
  publication-title: Blood
  doi: 10.1182/blood-2004-10-4057
  contributor:
    fullname: Xu
– volume: 137
  start-page: 623
  year: 2009
  ident: 10.1016/j.molcel.2011.05.014_bib35
  article-title: A two-step model for colon adenoma initiation and progression caused by APC loss
  publication-title: Cell
  doi: 10.1016/j.cell.2009.02.037
  contributor:
    fullname: Phelps
– volume: 1799
  start-page: 379
  year: 2010
  ident: 10.1016/j.molcel.2011.05.014_bib20
  article-title: The Paf1 complex: platform or player in RNA polymerase II transcription?
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/j.bbagrm.2010.01.001
  contributor:
    fullname: Jaehning
– volume: 41
  start-page: 1022
  year: 2009
  ident: 10.1016/j.molcel.2011.05.014_bib12
  article-title: Mutation of SHOC2 promotes aberrant protein N-myristoylation and causes Noonan-like syndrome with loose anagen hair
  publication-title: Nat. Genet.
  doi: 10.1038/ng.425
  contributor:
    fullname: Cordeddu
– volume: 266
  start-page: 84
  year: 2009
  ident: 10.1016/j.molcel.2011.05.014_bib34
  article-title: Parafibromin—functional insights
  publication-title: J. Intern. Med.
  doi: 10.1111/j.1365-2796.2009.02107.x
  contributor:
    fullname: Newey
– volume: 38
  start-page: 382
  year: 2010
  ident: 10.1016/j.molcel.2011.05.014_bib49
  article-title: The tumor suppressor, parafibromin, mediates histone H3 K9 methylation for cyclin D1 repression
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkp991
  contributor:
    fullname: Yang
– volume: 130
  start-page: 461
  year: 1995
  ident: 10.1016/j.molcel.2011.05.014_bib24
  article-title: Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.130.2.461
  contributor:
    fullname: Kinch
– volume: 17
  start-page: 459
  year: 2005
  ident: 10.1016/j.molcel.2011.05.014_bib25
  article-title: The regulation of cadherin-mediated adhesion by tyrosine phosphorylation/dephosphorylation of β-catenin
  publication-title: Curr. Opin. Cell Biol.
  doi: 10.1016/j.ceb.2005.08.009
  contributor:
    fullname: Lilien
– volume: 105
  start-page: 17420
  year: 2008
  ident: 10.1016/j.molcel.2011.05.014_bib26
  article-title: The parafibromin tumor suppressor protein inhibits cell proliferation by repression of the c-myc proto-oncogene
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0710725105
  contributor:
    fullname: Lin
– volume: 17
  start-page: 746
  year: 2007
  ident: 10.1016/j.molcel.2011.05.014_bib33
  article-title: Regulation of hematopoiesis and the hematopoietic stem cell niche by Wnt signaling pathways
  publication-title: Cell Res.
  doi: 10.1038/cr.2007.69
  contributor:
    fullname: Nemeth
– volume: 295
  start-page: 683
  year: 2002
  ident: 10.1016/j.molcel.2011.05.014_bib17
  article-title: SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein
  publication-title: Science
  doi: 10.1126/science.1067147
  contributor:
    fullname: Higashi
– volume: 338
  start-page: 127
  year: 2010
  ident: 10.1016/j.molcel.2011.05.014_bib2
  article-title: Wnt signaling in heart valve development and osteogenic gene induction
  publication-title: Dev. Biol.
  doi: 10.1016/j.ydbio.2009.11.030
  contributor:
    fullname: Alfieri
– volume: 19
  start-page: 230
  year: 2009
  ident: 10.1016/j.molcel.2011.05.014_bib41
  article-title: The RASopathies: developmental syndromes of Ras/MAPK pathway dysregulation
  publication-title: Curr. Opin. Genet. Dev.
  doi: 10.1016/j.gde.2009.04.001
  contributor:
    fullname: Tidyman
– volume: 106
  start-page: 353
  year: 2009
  ident: 10.1016/j.molcel.2011.05.014_bib10
  article-title: Wnt pathway, an essential role in bone regeneration
  publication-title: J. Cell. Biochem.
  doi: 10.1002/jcb.22020
  contributor:
    fullname: Chen
– volume: 32
  start-page: 676
  year: 2002
  ident: 10.1016/j.molcel.2011.05.014_bib7
  article-title: HRPT2, encoding parafibromin, is mutated in hyperparathyroidism-jaw tumor syndrome
  publication-title: Nat. Genet.
  doi: 10.1038/ng1048
  contributor:
    fullname: Carpten
– volume: 38
  start-page: 1788
  year: 2008
  ident: 10.1016/j.molcel.2011.05.014_bib39
  article-title: The canonical Wnt signaling pathway plays an important role in lymphopoiesis and hematopoiesis
  publication-title: Eur. J. Immunol.
  doi: 10.1002/eji.200738118
  contributor:
    fullname: Staal
– volume: 29
  start-page: 992
  year: 2008
  ident: 10.1016/j.molcel.2011.05.014_bib3
  article-title: The RAS/MAPK syndromes: novel roles of the RAS pathway in human genetic disorders
  publication-title: Hum. Mutat.
  doi: 10.1002/humu.20748
  contributor:
    fullname: Aoki
– volume: 17
  start-page: 9
  year: 2009
  ident: 10.1016/j.molcel.2011.05.014_bib28
  article-title: Wnt/β-catenin signaling: components, mechanisms, and diseases
  publication-title: Dev. Cell
  doi: 10.1016/j.devcel.2009.06.016
  contributor:
    fullname: MacDonald
– volume: 17
  start-page: 23
  year: 2007
  ident: 10.1016/j.molcel.2011.05.014_bib30
  article-title: The role of Shp2 (PTPN11) in cancer
  publication-title: Curr. Opin. Genet. Dev.
  doi: 10.1016/j.gde.2006.12.011
  contributor:
    fullname: Mohi
– volume: 24
  start-page: 1272
  year: 2005
  ident: 10.1016/j.molcel.2011.05.014_bib45
  article-title: Parafibromin, product of the hyperparathyroidism-jaw tumor syndrome gene HRPT2, regulates cyclin D1/PRAD1 expression
  publication-title: Oncogene
  doi: 10.1038/sj.onc.1208274
  contributor:
    fullname: Woodard
– volume: 2
  start-page: 562
  year: 2006
  ident: 10.1016/j.molcel.2011.05.014_bib13
  article-title: Mechanisms of disease: multiple endocrine neoplasia type 1-relation to chromatin modifications and transcription regulation
  publication-title: Nat. Clin. Pract. Endocrinol. Metab.
  doi: 10.1038/ncpendmet0292
  contributor:
    fullname: Dreijerink
– volume: 277
  start-page: 47572
  year: 2002
  ident: 10.1016/j.molcel.2011.05.014_bib46
  article-title: SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M207536200
  contributor:
    fullname: Wu
– volume: 96
  start-page: 2310
  year: 2000
  ident: 10.1016/j.molcel.2011.05.014_bib11
  article-title: Evidence that juvenile myelomonocytic leukemia can arise from a pluripotential stem cell
  publication-title: Blood
  doi: 10.1182/blood.V96.6.2310
  contributor:
    fullname: Cooper
– volume: 12
  start-page: 114
  year: 2006
  ident: 10.1016/j.molcel.2011.05.014_bib5
  article-title: A role for the scaffolding adapter GAB2 in breast cancer
  publication-title: Nat. Med.
  doi: 10.1038/nm1341
  contributor:
    fullname: Bentires-Alj
– volume: 140
  start-page: 491
  year: 2010
  ident: 10.1016/j.molcel.2011.05.014_bib23
  article-title: The human PAF1 complex acts in chromatin transcription elongation both independently and cooperatively with SII/TFIIS
  publication-title: Cell
  doi: 10.1016/j.cell.2009.12.050
  contributor:
    fullname: Kim
– volume: 90
  start-page: 558
  year: 2009
  ident: 10.1016/j.molcel.2011.05.014_bib27
  article-title: Mutated K-ras(Asp12) promotes tumourigenesis in Apc(Min) mice more in the large than the small intestines, with synergistic effects between K-ras and Wnt pathways
  publication-title: Int. J. Exp. Pathol.
  doi: 10.1111/j.1365-2613.2009.00667.x
  contributor:
    fullname: Luo
– volume: 131
  start-page: 1096
  year: 2006
  ident: 10.1016/j.molcel.2011.05.014_bib22
  article-title: APC and oncogenic KRAS are synergistic in enhancing Wnt signaling in intestinal tumor formation and progression
  publication-title: Gastroenterology
  doi: 10.1053/j.gastro.2006.08.011
  contributor:
    fullname: Janssen
– volume: 159
  start-page: 1073
  year: 2001
  ident: 10.1016/j.molcel.2011.05.014_bib15
  article-title: Analysis of corkscrew signaling in the Drosophila epidermal growth factor receptor pathway during myogenesis
  publication-title: Genetics
  doi: 10.1093/genetics/159.3.1073
  contributor:
    fullname: Johnson Hamlet
– volume: 19
  start-page: 877
  year: 2005
  ident: 10.1016/j.molcel.2011.05.014_bib14
  article-title: Wnt signaling in the intestinal epithelium: from endoderm to cancer
  publication-title: Genes Dev.
  doi: 10.1101/gad.1295405
  contributor:
    fullname: Gregorieff
– volume: 350
  start-page: 17
  year: 2006
  ident: 10.1016/j.molcel.2011.05.014_bib50
  article-title: Parafibromin inhibits cancer cell growth and causes G1 phase arrest
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2006.08.169
  contributor:
    fullname: Zhang
– volume: 4
  start-page: 688
  year: 2004
  ident: 10.1016/j.molcel.2011.05.014_bib16
  article-title: Oncogenic mechanisms of the Helicobacter pylori CagA protein
  publication-title: Nat. Rev. Cancer
  doi: 10.1038/nrc1433
  contributor:
    fullname: Hatakeyama
– volume: 27
  start-page: 3508
  year: 2008
  ident: 10.1016/j.molcel.2011.05.014_bib29
  article-title: Isolation of a distinct class of gain-of-function SHP-2 mutants with oncogenic RAS-like transforming activity from solid tumors
  publication-title: Oncogene
  doi: 10.1038/sj.onc.1211019
  contributor:
    fullname: Miyamoto
– volume: 10
  start-page: 849
  year: 2004
  ident: 10.1016/j.molcel.2011.05.014_bib4
  article-title: Mouse model of Noonan syndrome reveals cell type- and gene dosage-dependent effects of Ptpn11 mutation
  publication-title: Nat. Med.
  doi: 10.1038/nm1084
  contributor:
    fullname: Araki
– volume: 109
  start-page: 862
  year: 2007
  ident: 10.1016/j.molcel.2011.05.014_bib8
  article-title: PTPN11 is the first identified proto-oncogene that encodes a tyrosine phosphatase
  publication-title: Blood
  doi: 10.1182/blood-2006-07-028829
  contributor:
    fullname: Chan
– volume: 278
  start-page: 13952
  year: 2003
  ident: 10.1016/j.molcel.2011.05.014_bib1
  article-title: Development of an efficient “substrate-trapping” mutant of Src homology phosphotyrosine phosphatase 2 and identification of the epidermal growth factor receptor, Gab1, and three other proteins as target substrates
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M210670200
  contributor:
    fullname: Agazie
SSID ssj0014589
Score 2.4136925
Snippet Deregulation of SHP2 is associated with malignant diseases as well as developmental disorders. Although SHP2 is required for full activation of RAS signaling,...
SourceID pubmedcentral
proquest
crossref
pubmed
fao
elsevier
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 45
SubjectTerms abnormal development
Animals
beta Catenin - metabolism
Cell Nucleus - metabolism
cell physiology
Cercopithecus aethiops
COS Cells
Cyclin D1 - genetics
Cyclin D1 - metabolism
cyclins
dephosphorylation
DNA-directed RNA polymerase
Gene Expression Regulation
genes
HEK293 Cells
histones
Humans
malformations
Mass Spectrometry
methyltransferases
Mice
Mice, Inbred C57BL
neoplasms
Phosphorylation
Protein Tyrosine Phosphatase, Non-Receptor Type 11 - analysis
Protein Tyrosine Phosphatase, Non-Receptor Type 11 - genetics
Protein Tyrosine Phosphatase, Non-Receptor Type 11 - physiology
Proto-Oncogene Proteins c-myc - genetics
Proto-Oncogene Proteins c-myc - metabolism
RNA
Signal Transduction
signals
Tumor Suppressor Proteins - genetics
Tumor Suppressor Proteins - metabolism
Tumor Suppressor Proteins - physiology
tyrosine
Tyrosine - metabolism
Wnt Proteins - metabolism
Title SHP2 Tyrosine Phosphatase Converts Parafibromin/Cdc73 from a Tumor Suppressor to an Oncogenic Driver
URI https://dx.doi.org/10.1016/j.molcel.2011.05.014
https://www.ncbi.nlm.nih.gov/pubmed/21726809
https://search.proquest.com/docview/875088536
https://search.proquest.com/docview/907171989
https://pubmed.ncbi.nlm.nih.gov/PMC5101830
Volume 43
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9swDBaaFgN2Gda9mnUrdNjViGNJfhxbb0XabW2AJEOwiyDJ8pKhsQLHOfTfl_QjWIYWA3azLckPkfpEWtRHQj4N8xiJ6LhnhTbgoFjfU8iEqUEBYp0nmaqzKHy_CUczfj0X8wOSdnthMKyyxf4G02u0bq8M2t4crJfLwQTXToMoFEh6hn5Hjxwhlzmo9tH5xY-v33aLCVzUmfCwvocNuh10dZjXyt0Ze9dyeSKFJ39qhurlyj1mh_4dTvnH_HT5krxoDUt63rz7MTmwxSvyrEk1ef-aZJPROKDTe3gk2JV0vHCb9UJVMIfRFAPPy2pDx6pUObjPbgXecpqZiFHcfUIVnW5XrqSYARS9czisHFUFvS2MAwVcGvq5xPiON2R2-WWajrw2w4JnwPCovBwHcKKETjjXFrBmGGYgPSugx3QEnl9oMx0YACKtEt-AaaC4b2xufBtHSiTsLTksXGFPCM2sNmJoRcQM4yLIFbS3AWNBxhSYCbxPvK5X5boh0pBdhNlv2UhBohSkLyRIoU-iruvlnkJIwPp_tDwBSUn1C1BSziYBcujV1HVR0Ce0E5-EYYRrI6qwbruR4LYB3goWPl0lQdcXQ8z65F0j8N2H4L3D2IeSaE8VdhWQxHu_pFguajLvmjKN-e__-3NPyfPmP3fk-fEHcliVW_sRDKVKn7UD4Yz0ruYXcHaTzm9_PgB6QBLu
link.rule.ids 230,314,780,784,885,3506,27569,27924,27925,45663,45874
linkProvider Elsevier
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9swDBb6wLBdir2bPXXY1YhjSZZ97LIV2Zp2AZIMvQmSLDcZGitwnEP_fUk_gmVYMWA3w5JsS6Qofhb1kZBPgzxBIjoeOGEsABQXBhqZMA0oQGLyNNN1FoXLq3g059-vxfUBGXZnYTCssrX9jU2vrXV7p9-OZn-9XPanuHcayVgg6RnijkNyDN5ADMp-fPb558V4t5nARZ0JD-sH2KA7QVeHea38rXW3LZcnUnjyh1aow1z7v_mhf4ZT_rY-nT8lJ61jSc-ab39GDlzxnDxqUk3evSDZdDSJ6OwOXgl-JZ0s_Ga90BWsYXSIgedltaETXeoc4LNfAVoeZlYyiqdPqKaz7cqXFDOAIjqHy8pTXdAfhfWggEtLv5QY3_GSzM-_zoajoM2wEFhwPKogxwmcamFSzo0DWzOIM5CeEzBiRgLyi11mIguGyOg0tOAaaB5al9vQJVKLlL0iR4Uv3CmhmTNWDJyQzDIuolxDexcxFmVMg5vAeyToRlWtGyIN1UWY_VKNFBRKQYVCgRR6RHZDr_YUQoGt_0fLU5CU0jdgJdV8GiGHXk1dJ6MeoZ34FEwj3BvRhfPbjQLYBvZWsPjhKilCXwwx65HXjcB3HcFnx0kIJXJPFXYVkMR7v6RYLmoy75oyjYVv_ru7H8nj0exyrMbfri7ekifNP28ZhMk7clSVW_cenKbKfGgnxT1ZcRMa
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=SHP2+Tyrosine+Phosphatase+Converts+Parafibromin%2FCdc73+from+a+Tumor+Suppressor+to+an+Oncogenic+Driver&rft.jtitle=Molecular+cell&rft.au=Takahashi%2C+Atsushi&rft.au=Tsutsumi%2C+Ryouhei&rft.au=Kikuchi%2C+Ippei&rft.au=Obuse%2C+Chikashi&rft.date=2011-07-08&rft.issn=1097-2765&rft.volume=43&rft.issue=1&rft.spage=45&rft.epage=56&rft_id=info:doi/10.1016%2Fj.molcel.2011.05.014&rft.externalDBID=n%2Fa&rft.externalDocID=10_1016_j_molcel_2011_05_014
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1097-2765&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1097-2765&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1097-2765&client=summon