ArticleRNA biology2012
Transformation: the next level of regulation.
Article in RNA biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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.
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.
Who cites it
8 citing papers in PubMed.
- Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024Article
- Structural and Functional Aspects of Ebola Virus Proteins.Pathogens (Basel, Switzerland) · 2021Review
- Measures of single- versus multiple-round translation argue against a mechanism to ensure coupling of transcription and translation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Unfolding the Mysteries of Protein Metamorphosis.ACS chemical biology · 2018Review
- Flipping states: a few key residues decide the winning conformation of the only universally conserved transcription factor.Nucleic acids research · 2017Article
- Thermotoga maritima NusG: domain interaction mediates autoinhibition and thermostability.Nucleic acids research · 2017Article
- Interdomain Contacts Control Native State Switching of RfaH on a Dual-Funneled Landscape.PLoS computational biology · 2015Article
- A polymetamorphic protein.Protein science : a publication of the Protein Society · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The textbook view that a primary sequence determines the unique fold of a given protein has been challenged by identification of proteins with variant structures, such as prions. Our recent studies revealed that the transcription factor RfaH simultaneously changes its topology and function. RfaH is a two-domain protein whose N-terminal domain binds to transcribing RNA polymerase, stimulating its processivity. The α-helical C-terminal domain masks the RNA polymerase-binding site of the N-terminal domain, preventing unwarranted recruitment to genes lacking a specific DNA sequence. Upon binding to its DNA target, RfaH domains dissociate, and the C-terminal domain refolds into a β-barrel. This dramatic transformation allows binding to the ribosomal protein S10 and subsequent recruitment of a ribosome, coupling transcription and translation. We define RfaH as first example of "transformer proteins", in which two alternative structural states have distinct cellular functions and hypothesize that transformer proteins may be widespread in nature.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.