Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies - Wikidata - awgldk - TriplyDB

Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies

Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies

http://www.wikidata.org/entity/Q30832005

about

Stabilization and activation of p53 by the coactivator protein TAFII31 Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modification The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase Histone sumoylation is associated with transcriptional repression Gene expression patterns associated with blood-feeding in the malaria mosquito Anopheles gambiae An acetylation/deacetylation-SUMOylation switch through a phylogenetically conserved psiKXEP motif in the tumor suppressor HIC1 regulates transcriptional repression activity Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif Ras1 interacts with multiple new signaling and cytoskeletal loci in Drosophila eggshell patterning and morphogenesis SUMO and Chromatin Remodeling.Notch signaling through tramtrack bypasses the mitosis promoting activity of the JNK pathway in the mitotic-to-endocycle transition of Drosophila follicle cells.Genetic and proteomic evidence for roles of Drosophila SUMO in cell cycle control, Ras signaling, and early pattern formation.Dual-functioning transcription factors in the developmental gene network of Drosophila melanogaster Wrestling with Chromosomes: The Roles of SUMO During Meiosis A new Saccharomyces cerevisiae strain with a mutant Smt3-deconjugating Ulp1 protein is affected in DNA replication and requires Srs2 and homologous recombination for its viability.SUMO: of branched proteins and nuclear bodies.Many P-element insertions affect wing shape in Drosophila melanogaster SUMO conjugation attenuates the activity of the gypsy chromatin insulator.Versatile protein tag, SUMO: its enzymology and biological function.Scavenger receptors mediate the role of SUMO and Ftz-f1 in Drosophila steroidogenesis.Nuclear structure and chromosome segregation in Drosophila male meiosis depend on the ubiquitin ligase dTopors.Production of sumoylated proteins using a baculovirus expression system The SUMO pathway promotes basic helix-loop-helix proneural factor activity via a direct effect on the Zn finger protein senseless SUMO: a multifaceted modifier of chromatin structure and function.Long-Term Memory in Drosophila Is Influenced by Histone Deacetylase HDAC4 Interacting with SUMO-Conjugating Enzyme Ubc9.Identifications of SUMO-1 cDNA and its expression patterns in Pacific white shrimp Litopeanaeus vannamei.A platform for interrogating cancer-associated p53 alleles.Control in time and space: Tramtrack69 cooperates with Notch and Ecdysone to repress ectopic fate and shape changes during Drosophila egg chamber maturation.SUMOylation in Drosophila Development.Drosophila transcription factor Tramtrack69 binds MEP1 to recruit the chromatin remodeler NuRD.Drosophila Bicoid is a substrate of sumoylation and its activator function is subject to inhibition by this post-translational modification.Nuclear IE2 structures are related to viral DNA replication sites during baculovirus infection.Modification of Drosophila p53 by SUMO modulates its transactivation and pro-apoptotic functions.Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins.In vivo analysis of a fluorescent SUMO fusion in transgenic Drosophila.Tramtrack69 interacts with the dMi-2 subunit of the Drosophila NuRD chromatin remodelling complex Coordinated repression and activation of two transcriptional programs stabilizes cell fate during myogenesis.Pointed and Tramtrack69 establish an EGFR-dependent transcriptional switch to regulate mitosis.Sumoylation of the progesterone receptor and of the steroid receptor coactivator SRC-1.The function of EHD2 in endocytosis and defense signaling is affected by SUMO.The Drosophila UBC9 homologue lesswright mediates the disjunction of homologues in meiosis I.

P2860

Q24291008-31C99D60-B9C8-48ED-9DAE-6E26AE169A23 Q24291154-DC2120F9-6821-41F6-A365-3D8D8C696206 Q24534918-61774069-CFBE-4A12-9215-891D4DF8A733 Q24656259-37B17D96-6D75-463F-B68E-4F65D76F62EE Q24792805-240CD991-A115-43D3-B73D-4078B97BE70E Q28117824-8409025D-23B2-4A3B-A24A-C4294ACCC1E3 Q28144708-2438C314-1E25-4E22-8383-31C73255BCD9 Q28362128-89B3FCCA-AF61-45DD-8745-A3BBDC77DCAE Q30274768-FD192D24-131A-4433-BC3E-B4D115D91E98 Q33236738-295608A4-B050-45E4-AC69-2F7BBBDE1087 Q33468445-A4E82A31-1BEF-4F88-9992-6BDF44B7FA8E Q33623007-01B9B556-CAA4-4D5B-9D84-B2430669E17C Q33920029-EE44DAC5-77BD-45C2-A49E-33793FB3497E Q34345773-3A395178-C71B-4E6D-A3D8-FE3333B0FE86 Q34435551-35A7B149-52A1-4F47-9F64-1777932FDB9F Q34572511-145EA7DF-48EE-4742-ACFA-DF047A772D9A Q34590443-C7701368-5A81-4189-AB00-FB9D3F583145 Q34638636-06CF38FC-E7A1-43DA-9D74-636254158C39 Q34699820-52581E6C-6664-4981-9565-17D1245567CB Q35541976-7DEA9E24-F43B-4D38-9AE2-22A3918DA336 Q35691250-8D30F1FF-7EB1-4A03-A0A5-78EE10A85894 Q36155106-8D012BF3-3B2F-4DDA-A89E-B245BA9D94DD Q36564384-70968C77-EE6F-42A7-8A23-3B87EF901028 Q37076788-CD5D50BF-BE67-4DDE-937C-F8C2531EA0EF Q37105905-B8BD1F54-C2D5-40AC-8A48-A0DC31C5EF1F Q37273127-5B908D83-F74F-4CBE-A664-60F3D96A27AE Q37429777-2398A0EA-794D-4818-90D2-AE330BC50726 Q38223674-9C19D99B-6DD0-4F0B-9C06-73FD6B220752 Q38341411-F5D9B562-B3C5-4EAF-8EFF-19C426ADE29C Q39348508-66B43A7B-A622-4664-A4DE-C550F797B38F Q39683565-2A812335-B60D-4D48-8FA9-C0F8FD824FE3 Q40423291-CF0E411A-63FD-4322-85A6-E965D589F617 Q40579335-89516E02-D39B-4707-9B29-A4C9BC7BB59D Q42607353-CC6B4E2F-1E6B-439B-8CC5-D422E903B10E Q42724599-CF9164FA-2E14-4781-B22F-3A97BF2E9FE4 Q42845436-A7CB78AE-55A7-41CF-89B9-08827B07B7B2 Q44226373-94DF43B0-ED1D-4190-8B76-11493497AD58 Q44279178-7FB19037-F31C-418A-83A8-6C77F4716217 Q46931366-7E1D74AC-F833-4388-BADD-88848C89AB1B Q47072121-664B17CA-F993-4D30-9F76-6E5CE5F39DDD

P2860

Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies

http://www.wikidata.org/entity/Q30832005

description

2000 nî lūn-bûn

@nan

2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

Covalent modification of the t ...... otein Smt3 in Drosophila flies

@ast

Covalent modification of the t ...... otein Smt3 in Drosophila flies

@en

type

label

Covalent modification of the t ...... otein Smt3 in Drosophila flies

@ast

Covalent modification of the t ...... otein Smt3 in Drosophila flies

@en

prefLabel

Covalent modification of the t ...... otein Smt3 in Drosophila flies

@ast

Covalent modification of the t ...... otein Smt3 in Drosophila flies

@en

P1433

Q30832005-AB808C42-4252-41C7-A420-18190C3747D7

P1476

Q30832005-94ADBAAA-8937-49F5-8430-00A27AB726DF

P2093

Q30832005-0A27E077-0991-4012-8C65-4B4537303214

Q30832005-131B8813-858D-4FC3-AFC2-812B519CB90A

Q30832005-7AA27613-C4A6-4ADD-935D-E60924FC0BC9

Q30832005-85883640-AF21-4858-AE91-2ACC30A932FE

Q30832005-A3B9B9AB-0CAA-4112-94EE-81FD9B564F3B

Q30832005-C395F3DC-EED4-4CF8-B135-27B85858F049

P2860

Q30832005-011D2551-56FB-432F-A45B-9B27E1941811

Q30832005-04E61F1E-5E87-4172-A7C8-D6A6A3F47D97

Q30832005-08C785AC-1CD2-4AA6-AB93-8BE72598B52F

Q30832005-1341F3CD-2633-4271-944A-30B561F879BF

Q30832005-192AFFC7-33D4-4B5E-99A3-91DCA9956882

Q30832005-192F8FF6-A9F5-4C01-9591-18CED2417395

Q30832005-2320B55B-4E12-48F0-B22E-C5BB0E9C438E

Q30832005-2677EB83-AA58-4300-9DE9-1197B16BBCA2

Q30832005-2DB9E80F-F9B9-46C5-AE33-F0B6D0148DD9

Q30832005-31DD026C-2567-4F61-81D3-024A8713FC15

P304

Q30832005-73BF7186-1C7F-49EC-90A1-25E80AABA638

P31

Q30832005-8BA228D8-05D7-490F-9035-7072D44CB8BC

P356

Q30832005-5A2F44F0-28B6-4771-AA79-7571FCC2C5D5

P407

Q30832005-BD899BD0-8B19-459D-89F9-45CEB5509405

P433

Q30832005-6A2B4A5A-E1B3-4A24-A6BD-6EDCD6945A41

P478

Q30832005-44E23B07-486A-420E-BD5C-E3C7F87105CB

P577

Q30832005-2DE9F3F9-7346-4A4D-BF68-4C9D73E0EF0B

P698

Q30832005-348240D6-B0AD-4CAE-A234-BDD15B47E072

P921

Q30832005-11338610-B610-49D4-8D3B-C4A50DF9BEE4

P932

Q30832005-52E69B90-786C-4645-B368-1874C03DAD3C

P356

MCB.20.3.1072-1082.2000

P1433

Molecular and Cellular Biology

P1476

Covalent modification of the t ...... otein Smt3 in Drosophila flies

@en

P2093

A Dejean

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

A Travers

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

F Lehembre

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

F Schweisguth

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

P Badenhorst

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

S Müller

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

P2860

A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex

Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1

SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family

A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2

Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway

Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus.

Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins

Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association

Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p.

The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer.

P304

1072-1082

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

P31

scholarly article

P356

10.1128/MCB.20.3.1072-1082.2000

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

P407

P433

3

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

P478

20

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

P577

2000-02-01T00:00:00Z

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

P698

10629064

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

P921

P932

85224

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