Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein. - Wikidata - awgldk - TriplyDB

Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein.

Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein.

http://www.wikidata.org/entity/Q29977747

about

Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases Protein kinases and phosphatases in the control of cell fate The ubiquitin ligase Nedd4-1 is dispensable for the regulation of PTEN stability and localization Critical role of PICT-1, a tumor suppressor candidate, in phosphatidylinositol 3,4,5-trisphosphate signals and tumorigenic transformation Focus on PTEN Regulation Deubiquitylase OTUD3 regulates PTEN stability and suppresses tumorigenesis Expression profiling of rat mammary epithelial cells reveals candidate signaling pathways in dietary protection from mammary tumors Nucleolar stress induces ubiquitination-independent proteasomal degradation of PICT1 protein GLTSCR2/PICT1 links mitochondrial stress and Myc signaling.Regulation of the MDM2-P53 pathway and tumor growth by PICT1 via nucleolar RPL11.Nucleolar protein GLTSCR2 stabilizes p53 in response to ribosomal stresses Involvement of GLTSCR2 in the DNA Damage Response.The nucleolar protein GLTSCR2 is required for efficient viral replication PICT-1 is a key nucleolar sensor in DNA damage response signaling that regulates apoptosis through the RPL11-MDM2-p53 pathway GLTSCR2/PICT-1, a putative tumor suppressor gene product, induces the nucleolar targeting of the Kaposi's sarcoma-associated herpesvirus KS-Bcl-2 protein.PICT-1 triggers a pro-death autophagy through inhibiting rRNA transcription and AKT/mTOR/p70S6K signaling pathway.Exosome-mediated delivery of the intrinsic C-terminus domain of PTEN protects it from proteasomal degradation and ablates tumorigenesis Genes and proteins differentially expressed during in vitro malignant transformation of bovine pancreatic duct cells.Expression profiling identifies genes involved in neoplastic transformation of serous ovarian cancer.Salivary transcriptomic biomarkers for detection of resectable pancreatic cancer.Functional interaction of phosphatase and tensin homologue (PTEN) with the E3 ligase NEDD4-1 during neuronal response to zinc.Nucleolar localization of GLTSCR2/PICT-1 is mediated by multiple unique nucleolar localization sequences.Targeting the translational apparatus to improve leukemia therapy: roles of the PI3K/PTEN/Akt/mTOR pathway.Functional analysis of the protein phosphatase activity of PTEN Interdiction of sphingolipid metabolism to improve standard cancer therapies.Saliva: diagnostics and therapeutic perspectives Protein interactions of phosphatase and tensin homologue (PTEN) and its cancer-associated G20E mutant compared by using stable isotope labeling by amino acids in cell culture-based parallel affinity purification.UVA induces lesions resembling seborrheic keratoses in mice with keratinocyte-specific PTEN downregulation NHERFs, NEP, MAGUKs, and more: interactions that regulate PTEN.Class reunion: PTEN joins the nuclear crew.Posttranslational protein modifications: current implications for cancer detection, prevention, and therapeutics.Differential expression of PTEN-targeting microRNAs miR-19a and miR-21 in Cowden syndrome PTEN: a default gate-keeping tumor suppressor with a versatile tail.PICT1 regulates TP53 via RPL11 and is involved in gastric cancer progression.PTEN and the PI3-kinase pathway in cancer Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs.Therapeutic resistance resulting from mutations in Raf/MEK/ERK and PI3K/PTEN/Akt/mTOR signaling pathways.PTEN-Associated Complexes: An Overview.Merlin: the wizard requires protein stability to function as a tumor suppressor.Scission of the p53-MDM2 Loop by Ribosomal Proteins.

P2860

5b0edc31e8998b4c9ef1db56e2b4b89566105bf4 940f86a7cc060e03db7f84dc59320a0feadc7fce c12fdbd20324ef98532bf8dda723dc8792f900c1

P248

Q24305156-6E894742-20B8-4F8C-8F13-347E3F2C3F4B Q24604987-035C9F88-BDB1-4372-8D8B-47053E4C09F8 Q24650856-573D2DBE-4D90-43E2-82A0-F8F6B89005A2 Q24673801-FBC336B8-C177-48EC-B011-F3E0C970EF83 Q26797287-2F0EC9ED-2B50-431E-9078-0E1C8AD56862 Q28117749-D4D011A8-91B1-4F32-B376-60AB1FF52528 Q28577689-66AB7C72-718A-4E0D-AF64-BBB640D3D4F4 Q29871437-BC6A55B3-D5FA-4BCC-B2A4-06065AA71B63 Q29871472-38525A61-C3DC-42BD-8E05-987B835F6774 Q29976922-A8916669-A6D6-4DD0-8111-45B94A685FDF Q30032662-FA6AE500-F76A-448A-87C6-104389850B3A Q30032667-F298CAD1-52C1-4DCC-A44D-B440FCF46D00 Q30090230-2026C178-39D4-48D2-8A51-9754AE351FE0 Q30090233-1CF96A56-B314-4471-B846-43AD394F32A1 Q30090237-7E217408-B388-4A8B-AB04-068D1EB7F923 Q30090238-533EA58E-4821-4999-B90B-57848C71F758 Q30392471-7C2AD1E3-5A7E-4443-8588-D8C42B1E440B Q33278299-87A9C5F9-9EB8-446C-9AB1-FA74422D8E24 Q33511864-7F77A78B-2400-4CCF-B450-3AA378A32DC8 Q33699291-8EB18B2F-E79F-4A38-9F0D-7353783EEEC5 Q33744696-EEA0CEA5-6299-4CA8-B322-4A1AB44FECD2 Q34146439-8980B60D-B02A-492B-B1EA-A227CCCB40A1 Q34173253-5536E549-ACC7-4C72-B126-657F172B9B7F Q34194118-667FEF82-0520-483E-AB04-D31DA5804504 Q34373466-BB8898B9-75F9-4FDB-8B67-CB9102495C34 Q34669417-1C2AF4C7-376A-4FC6-A973-0C2AE0021911 Q34979078-A9354CB3-08ED-4CB4-A594-D96229C7EC1D Q35048193-4C8171B4-3887-419A-A549-5CF016592303 Q35256204-01909E92-D7F0-48C0-969E-DD11E26DEE4D Q36313163-FD8483E7-3C35-45A8-81FB-EDB3E5D8B581 Q36537788-F261847B-425B-44A0-AB91-C8DCD6191209 Q36718983-B78861A1-8DEA-4F7B-B115-76A2214822E3 Q37216319-28B7459A-E493-4742-8358-F2523C1CA868 Q37235547-3FED6E25-B1FC-45A4-800C-6B164CBC9113 Q37259680-CFACF8B2-F898-4E04-9193-8F944EA860D9 Q37649607-5DC23858-1289-4827-8354-02220A4BEC2E Q37837732-58FC056B-2D7E-4F21-88FD-C4B98D749CD0 Q37955889-D67A5DA0-530B-4B5A-9271-D8EED0F3EA56 Q38023101-183D5E3F-D9F4-458F-8655-9A5D13E78BBB Q38059701-E7492772-5A7B-40E4-9105-8591A5C3CA14

P2860

Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein.

http://www.wikidata.org/entity/Q29977747

description

2004 nî lūn-bûn

@nan

2004 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein.

@ast

Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein.

@en

type

label

Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein.

@ast

Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein.

@en

prefLabel

Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein.

@ast

Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein.

@en

P1433

Q29977747-3BE7299B-0DF6-406D-9778-7838FBFD5DD0

P1476

Q29977747-298F0913-934E-4453-8658-7479B686D5B0

P2093

Q29977747-07E5AF9B-9D7C-4423-AFB8-CB4B22F381E7

Q29977747-1840C613-36A1-4DF1-84AB-03E36A725F4D

Q29977747-8640518E-BA90-4227-A43D-8456ADFB5F1F

P2860

Q29977747-054E6BD5-EC11-4C12-8E99-55CD07347538

Q29977747-08D7C151-39DD-45B8-831A-AD8F011FC87F

Q29977747-0902C8EE-A499-4511-95F7-87A6FD3715BC

Q29977747-090447A9-F6B9-40B6-9BC7-BF2ABB231A40

Q29977747-0FEC23FE-CD84-4B40-8442-778924588931

Q29977747-1BD3A2E9-5C6E-4543-BCFC-A4DA52BDA77D

Q29977747-243202CC-F208-46EE-B8DC-280F50D9DB88

Q29977747-40223D04-35E8-4C30-9057-E97724BA0D3D

Q29977747-6C6965E8-1DFA-435F-85D3-7C4E5DF5A3B1

Q29977747-6D7DBFE0-E979-4282-8D63-CA212E2012A7

P304

Q29977747-34A74732-266C-4473-A248-ED98327BA827

P31

Q29977747-C61DA23E-F075-4A59-AF9A-4D2F02A24343

P3181

Q29977747-A3FFA476-E2C9-4BDE-BFB1-D51A270CF9D5

P356

Q29977747-AE0E7215-84A2-44AF-ADEB-0F2161632537

P407

Q29977747-2CEA09FC-4058-4F0C-8820-304016C94359

P433

Q29977747-993459EF-78D3-41E5-96F4-E1711EBDE788

P478

Q29977747-C6CAC10F-4478-4DBB-AFED-FD519922501C

P50

Q29977747-25954335-C926-4A66-A615-F75490FC8144

P577

Q29977747-BC87B004-0C66-4472-A008-148B554A5FCF

P698

Q29977747-7300C7C1-2C01-41A1-A298-6D4FC05F4A0D

P921

Q29977747-03BED459-13C2-4CD2-B5D6-7AA190CBC8A7

Q29977747-3343279B-CA34-4634-A517-75E12E638549

Q29977747-AE50AD14-8760-4C4B-B458-61EB1AC14261

P3181

P356

P1433

Journal of Biological Chemistry

P1476

Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein

@en

P2093

Fumiaki Okahara

http://www.w3.org/2001/XMLSchema#string

Hideki Ikawa

http://www.w3.org/2001/XMLSchema#string

Yasunori Kanaho

http://www.w3.org/2001/XMLSchema#string

P2860

The tumor-suppressor activity of PTEN is regulated by its carboxyl-terminal region

Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase

Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2

Phosphorylation of the PTEN tail regulates protein stability and function

The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation

The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

PTEN and myotubularin: novel phosphoinositide phosphatases.

A transcript map of the chromosome 19q-arm glioma tumor suppressor region

PTEN tumor suppressor regulates p53 protein levels and activity through phosphatase-dependent and -independent mechanisms

Direct identification of PTEN phosphorylation sites

P304

45300-45303

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

2640941

http://www.w3.org/2001/XMLSchema#string

P356

10.1074/JBC.C400377200

http://www.w3.org/2001/XMLSchema#string

P407

P433

44

http://www.w3.org/2001/XMLSchema#string

P478

279

http://www.w3.org/2001/XMLSchema#string

P50

Tomohiko Maehama

P577

2004-09-07T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

15355975

http://www.w3.org/2001/XMLSchema#string

P921

protein stabilization

NOP53 ribosome biogenesis factor

phosphorylation