Evidence map›Paper›PMID 25056123›Full record

ArticleJournal of molecular modeling2014

Evidence supporting the existence of a NUPR1-like family of helix-loop-helix chromatin proteins related to, yet distinct from, AT hook-containing HMG proteins.

Raul Urrutia, Gabriel Velez, Marisa Lin, Gwen Lomberk, Jose Luis Neira, Juan Iovanna

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular modeling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Oncogenic Role of NUPR1 in Ovarian Cancer.OncoTargets and therapy · 2020
    Article
  6. Article
  7. Intrinsically disordered chromatin protein NUPR1 binds to the C-terminal region of Polycomb RING1B.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. Elucidation ofJCI insight · 2017
    Article
  9. Article
  10. Article
  11. Article
  12. 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

6 authors at 3 institutions in 3 countries.

Raul UrrutiaLaboratory of Epigenetics and Chromatin Dynamics, Departments of Biochemistry and Molecular Biology, Biophysics, and Medicine, Epigenomics Translational Program, Center for Individualized Medicine., Mayo Clinic, 200 First Street SW, Guggenheim 10, Rochester, MN, 55905, USA, urrutia.raul@mayo.edu.
Gabriel Velez
Marisa Lin
Gwen Lomberk
Jose Luis Neira
Juan Iovanna
Mayo Clinic · USAix-Marseille Université · FRUniversitat de Miguel Hernández d'Elx · ES

Funding

Tissue CoreP50CA102701 · NCI · MAYO CLINIC ROCHESTER · PI MUKHOPADHYAY, DEBABRATA · 2004 to 2018
$32.7M
PILOT AND FEASIBILTY PROGRAMP30DK084567 · NIDDK · MAYO CLINIC ROCHESTER · PI GREGORY J. GORES · 2009 to 2026
$22.2M
ZINC FINGER GENES AND PANCREATIC CELL GROWTHR01DK052913 · NIDDK · MEDICAL COLLEGE OF WISCONSIN · PI LOMBERK, GWEN, URRUTIA, RAUL A. · 1998 to 2023
$7.0M
The Role of Zinc Finger Genes in Pancreatic Cell GrowthR56DK052913 · NIDDK · MAYO CLINIC ROCHESTER · PI URRUTIA, RAUL A. · 2008 to 2008
$291k
NCI NIH HHS P50 CA102701NIDDK NIH HHS DK52913NIDDK NIH HHS P30 DK084567NIDDK NIH HHS P30DK084567NIDDK NIH HHS R01 DK052913NIDDK NIH HHS R56 DK052913
6 · The paper itself

Abstract

NUPR1, a small chromatin protein, plays a critical role in cancer development, progression, and resistance to therapy. Here, using a combination of structural bioinformatics and molecular modeling methods, we report several novel findings that enhance our understanding of the biochemical function of this protein. We find that NUPR1 has been conserved throughout evolution, and over time it has undergone duplications and transpositions to form other transcriptional regulators. Using threading, homology-based molecular modeling, molecular mechanics calculations, and molecular dynamics simulations, we generated structural models for four of these proteins: NUPR1a, NUPR1b, NUPR2, and the NUPR-like domain of GTF2-I. Comparative analyses of these models combined with extensive linear motif identification reveal that these four proteins, though similar in their propensities for folding, differ in size, surface changes, and sites amenable for posttranslational modification. Lastly, taking NUPR1a as the paradigm for this family, we built models of a NUPR-DNA complex. Additional structural comparisons revealed that NUPR1 defines a new family of small-groove-binding proteins that share structural features with, yet are distinct from, helix-loop-helix AT-hook-containing HMG proteins. These models and inferences should lead to a better understanding of the function of this group of chromatin proteins, which play a critical role in the development of human malignant diseases.

Indexed as

AT-Hook MotifsHelix-Turn-Helix MotifsAmino Acid SequenceBasic Helix-Loop-Helix ProteinsConserved SequenceDNAHigh Mobility Group ProteinsHumansModels, MolecularMolecular Sequence DataMutant ProteinsNeoplasm ProteinsNucleic Acid ConformationProtein BindingProtein Processing, Post-TranslationalProtein Structure, TertiaryBasic Helix-Loop-Helix ProteinsDNAHigh Mobility Group ProteinsMutant ProteinsNeoplasm ProteinsNUPR1 protein, human

Identifiers

PMID25056123
PMCPMC4139591
OpenAlexW2018860421

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.