Evidence map›Paper›PMID 19274739›Full record

ArticleProteins2009

Formation of the RFX gene regulatory complex induces folding of the interaction domain of RFXAP.

LaTese Briggs, Kholiswa Laird, Jeremy M Boss, Colin W Garvie

Abstract read
In one paragraph

Article in Proteins, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
26.5field-weighted citation impact, top 1% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Auto-fatty acylation of transcription factor RFX3 regulates ciliogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  3. Article
  4. Article
  5. Review
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 3 institutions in 1 country.

LaTese BriggsBroad Institute of Harvard and MIT, Cambridge, Massachusetts 02141, USA.
Kholiswa Laird
Jeremy M Boss
Colin W Garvie
University of Maryland, Baltimore County · USBroad Institute · USEmory University · US

Funding

EXPAND PARTICIPATION BY MINORITIES IN BIOMEDICAL SCIENCER25GM055036 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SUMMERS, MICHAEL FINLEY · 1996 to 2021
$16.9M
Regulation of MHC Class II GenesR01GM047310 · NIGMS · EMORY UNIVERSITY · PI BOSS, JEREMY M. · 1993 to 2015
$4.6M
MHC Class II Transactivator Function and RegulationR01AI034000 · NIAID · EMORY UNIVERSITY · PI BOSS, JEREMY M. · 1993 to 2009
$2.6M
NIAID NIH HHS R01 AI034000NIGMS NIH HHS R01 GM047310NIGMS NIH HHS R25 GM055036NIGMS NIH HHS R25-GM55036
6 · The paper itself

Abstract

Major histocompatibility complex class II (MHCII) molecules have a central role in the mammalian adaptive immune response against infection. The level of the immune response is directly related to the concentration of MHCII molecules in the cell, which have a central role in initiating the immune response. MHCII molecules are therefore a potential target for the development of immunosuppressant drugs for the treatment of organ transplant rejection and autoimmune disease. The expression of MHCII molecules is regulated by a cell specific multiprotein complex. The RFX complex is the key DNA binding component of this complex. The RFX complex is composed of three proteins-RFX5, RFXAP, and RFXB-all of which are required for activation of expression of the MHCII genes. Little is currently known about the precise regions of the RFX proteins that are required for complex formation, or their structure. We have therefore identified the key regions of RFX5, RFXAP, and RFXB, which are required to form the RFX complex and have characterized the individual domains and the complexes they form using NMR and circular dichroism spectroscopy and isothermal titration calorimetry. Our results support a model for the assembly of the RFX complex in which the interaction between RFX5 and RFXAP promote folding of a poorly structured region ofRFXAP, which is required for high affinity binding of RFXB to the RFX5.RFXAP complex.

Indexed as

Gene Expression RegulationCalorimetryCircular DichroismDNA-Binding ProteinsGenetic VectorsHumansMagnetic Resonance SpectroscopyMutagenesis, Site-DirectedPolymerase Chain ReactionProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryRegulatory Factor X Transcription FactorsTranscription FactorsDNA-Binding ProteinsRegulatory Factor X Transcription FactorsRFX5 protein, humanRFXAP protein, humanTranscription Factors

Identifiers

PMID19274739
PMCPMC2700855
OpenAlexW2134795664

What OpenQuestion holds

Textmetadata
LicenceTDM
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.