Evidence map›Paper›PMID 16567619›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression.

Adam Rosendorff, Shuhei Sakakibara, Sixin Lu, Elliott Kieff, Yan Xuan, Alessandra DiBacco, Yujiang Shi, Yang Shi, Grace Gill

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
6.0field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

63 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Comparative genomics of mortal and immortal cnidarians unveils novel keys behind rejuvenation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. The role of interferons type I, II and III in myositis: A review.Brain pathology (Zurich, Switzerland) · 2021
    Review
  12. Article
  13. Mechanism for autoinhibition and activation of the MORC3 ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Adam RosendorffDepartment of Medicine, Channing Laboratory, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
Shuhei Sakakibara
Sixin Lu
Elliott Kieff
Yan Xuan
Alessandra DiBacco
Yujiang Shi
Yang Shi
Grace Gill
Harvard University · USBrigham and Women's Hospital · US

Funding

Epstein-Barr Virus Nuclear Proteins in B Cell Growth TransformationR01CA047006 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI ZHAO, BO · 2002 to 2021
$12.1M
VIRUS AND CELL GENE EXPRESSION IN KAPOSI SARCOMA ASSOCIATED HERPESVIRUS TUMORSP01CA087661 · NCI · PRINCETON UNIVERSITY · PI SHENK, THOMAS E · 2000 to 2004
$10.9M
MOLECULAR BIOLOGY OF EPSTEIN-BARR VIRUS INFECTIONR35CA047006 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI KIEFF, ELLIOTT D · 1987 to 2000
$1.6M
NCI NIH HHS CA 47006NCI NIH HHS CA 87661NCI NIH HHS P01 CA087661NCI NIH HHS R01 CA047006NCI NIH HHS R35 CA047006
6 · The paper itself

Abstract

Small ubiquitin-like modifier (SUMO) modification of transcription factors is generally associated with repression. Reverse genetic analysis of SUMO-1, and -2 conserved residues emphasized the importance of dual charge reversals in abrogating the critical role of SUMO-2 K33, K35, and K42 in repression. GST-SUMO-2-affinity chromatography followed by liquid chromatography (LC)-MS analysis identified proteins that appeared to bind preferentially to WT SUMO-2 versus SUMO-2 K33E and K35E. LSD1, NXP-2, KIAA0809 (ARIP4), SAE2, RanGAP1, PELP1, and SETDB1 bound to SUMO-2 and not to SUMO-2 K33E, K42E, or K35E and K42E. Although LSD1 is a histone lysine demethylase, and histone H3K4 was demethylated at a SUMO-2-repressed promoter, neither overexpression of a dominant-negative LSD1 nor LSD1 depletion with RNA interference affected SUMO-2-mediated repression, indicating that LSD1 is not essential for repression, in this context. When tethered to a promoter by fusion to Gal4, NXP-2 repressed transcription, consistent with a role for NXP-2 in SUMO-mediated repression. SUMO-2-associated proteins identified in this study may contribute to SUMO-dependent regulation of transcription or other processes.

Indexed as

Amino Acid SequenceBase SequenceBlotting, WesternChromatin ImmunoprecipitationDNADNA PrimersElectrophoresis, Polyacrylamide GelGenes, ReporterMethylationMolecular Sequence DataNuclear Matrix-Associated ProteinsPromoter Regions, GeneticProtein BindingSequence Homology, Amino AcidSmall Ubiquitin-Related Modifier ProteinsTranscription FactorsDNADNA PrimersNuclear Matrix-Associated ProteinsSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanTranscription Factors

Identifiers

PMID16567619
PMCPMC1459351
OpenAlexW2106770461

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.