Evidence map›Paper›PMID 18840288›Full record

ArticleMolecular cancer2008

A conserved acidic patch in the Myb domain is required for activation of an endogenous target gene and for chromatin binding.

Emily Ray Ko, Dennis Ko, Carolyn Chen, Joseph S Lipsick

Open access · goldAbstract read
In one paragraph

Article in Molecular cancer, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Animal-specific C-terminal domain links myeloblastosis oncoprotein (Myb) to an ancient repressor complex.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  14. Valproate and amitriptyline exert common and divergent influences on global and gene promoter-specific chromatin modifications in rat primary astrocytes.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2010
    Article
  15. Article
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

4 authors at 1 institution in 1 country.

Emily Ray KoDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305-5324, USA. emilyeray@gmail.com
Dennis Ko
Carolyn Chen
Joseph S Lipsick
Stanford University · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007365 · NIGMS · STANFORD UNIVERSITY · PI CHUA, KATRIN F · 1985 to 2021
$33.8M
Biology of the Myb-MuvB Oncoprotein-Tumor Suppressor Protein ComplexR01CA128836 · NCI · STANFORD UNIVERSITY · PI LIPSICK, JOSEPH STEVEN · 2007 to 2016
$2.6M
NCI NIH HHS R01 CA128836NIGMS NIH HHS T32 GM007365NIGMS NIH HHS T32GM007365
6 · The paper itself

Abstract

The c-Myb protein is a transcriptional regulator initially identified by homology to the v-Myb oncoprotein, and has since been implicated in human cancer. The most highly conserved portion of the c-Myb protein is the DNA-binding domain which consists of three imperfect repeats. Many other proteins contain one or more Myb-related domains, including a number of proteins that do not bind directly to DNA. We performed a phylogenetic analysis of diverse classes of Myb-related domains and discovered a highly conserved patch of acidic residues common to all Myb-related domains. These acidic residues are positioned in the first of three alpha-helices within each of the three repeats that comprise the c-Myb DNA-binding domain. Interestingly, these conserved acidic residues are present on a surface of the protein which is distinct from that which binds to DNA. Alanine mutagenesis revealed that the acidic patch of the third c-Myb repeat is essential for transcriptional activity, but neither for nuclear localization nor DNA-binding. Instead, these acidic residues are required for efficient chromatin binding and interaction with the histone H4 N-terminal tail.

Indexed as

Transcriptional ActivationAmino Acid SequenceAnimalsBinding SitesCell NucleusChromatinConserved SequenceDNAHumansMolecular Sequence DataOncogene Proteins v-mybPhylogenyProtein Structure, TertiarySequence AlignmentChromatinDNAOncogene Proteins v-myb

Identifiers

PMID18840288
PMCPMC2572630
OpenAlexW2057444975

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.