Evidence map›Paper›PMID 22323284›Full record

ReviewProtein science : a publication of the Protein Society2012

The mysterious RAMP proteins and their roles in small RNA-based immunity.

Ruiying Wang, Hong Li

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Cas6 processes tight and relaxed repeat RNA via multiple mechanisms: A hypothesis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017
    Review
  10. Archaeal extrachromosomal genetic elements.Microbiology and molecular biology reviews : MMBR · 2015
    Review
  11. Structural Principles of CRISPR RNA Processing.Structure (London, England : 1993) · 2015
    Article
  12. Article
  13. CRISPR interference: a structural perspective.The Biochemical journal · 2013
    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

2 authors.

Ruiying WangDepartment of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida 32306, USA.
Hong Li

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A new class of prokaryotic RNA binding proteins called Repeat Associated Mysterious Proteins (RAMPs), has recently been identified. These proteins play key roles in a novel type immunity in which the DNA of the host organism (e.g. a prokaryote) has sequence segments corresponding to the sequences of potential viral invaders. The sequences embedded in the host DNA confer immunity by directing selective destruction of the nucleic acid of the virus using an RNA-based strategy. In this viral defense mechanism, RAMP proteins have multiple functional roles including endoribonucleotic cleavage and ribonucleoprotein particle assembly. RAMPs contain the classical RNA recognition motif (RRM), often in tandem, and a conserved glycine-rich segment (G-loop) near the carboxyl terminus. However, unlike RRMs that bind single-stranded RNA using their β-sheet surface, RAMPs make use of both sides of the RRM fold and interact with both single-stranded and structured RNA. The unique spatial arrangement of the two RRM folds, facilitated by a hallmark G-loop, is crucial to formation of a composite surface for recognition of specific RNA. Evidence for RNA-dependent oligomerization is also observed in some RAMP proteins that may serve as an important strategy to increase specificity.

Indexed as

Host-Pathogen InteractionsBacteriaBacterial ProteinsNucleotide MotifsProtein FoldingRNA, BacterialRNA-Binding ProteinsRNA CleavageRNA StabilitySpecies SpecificityVirusesBacterial ProteinsRNA, BacterialRNA-Binding Proteins

Identifiers

PMID22323284
PMCPMC3375746

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.