Evidence map›Paper›PMID 35714601›Full record

ArticleStructure (London, England : 1993)2022

Structures of an active type III-A CRISPR effector complex.

Eric M Smith, Sé Ferrell, Valerie L Tokars, Alfonso Mondragón

Open access · greenAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

9 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Structure of theCurrent research in structural biology · 2023
    Article
  8. Article
  9. 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.

Eric M SmithDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
Sé FerrellDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
Valerie L TokarsDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Alfonso MondragónDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA. Electronic address: a-mondragon@northwestern.edu.
Northwestern University · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LEONIDAS C. PLATANIAS · 1993 to 2026
$153.9M
Northwestern University Clinical and Translational Science Institute (NUCATS)UL1TR001422 · NCATS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI D'AQUILA, RICHARD · 2015 to 2023
$56.8M
The Stanford-SLAC CryoEM Center supplementU24GM129541 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH, HEDMAN, BRITT · 2018 to 2023
$54.8M
NCCAT: National Center for CryoEM Access and Training- Supplement for Windows 10 and FFIU24GM129539 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2018 to 2023
$53.9M
Structural and biophysical studies of proteins, nucleic acids, and their complexesR35GM118108 · NIGMS · NORTHWESTERN UNIVERSITY · PI Alfonso Mondragon · 2017 to 2026
$5.4M
NCATS NIH HHS UL1 TR001422NCI NIH HHS P30 CA060553NIGMS NIH HHS R35 GM118108NIGMS NIH HHS U24 GM129539NIGMS NIH HHS U24 GM129541
6 · The paper itself

Abstract

Clustered regularly interspaced short palindromic repeats (CRISPR) and their CRISPR-associated proteins (Cas) provide many prokaryotes with an adaptive immune system against invading genetic material. Type III CRISPR systems are unique in that they can degrade both RNA and DNA. In response to invading nucleic acids, they produce cyclic oligoadenylates that act as secondary messengers, activating cellular nucleases that aid in the immune response. Here, we present seven single-particle cryo-EM structures of the type III-A Staphylococcus epidermidis CRISPR effector complex. The structures reveal the intact S. epidermidis effector complex in an apo, ATP-bound, cognate target RNA-bound, and non-cognate target RNA-bound states and illustrate how the effector complex binds and presents crRNA. The complexes bound to target RNA capture the type III-A effector complex in a post-RNA cleavage state. The ATP-bound structures give details about how ATP binds to Cas10 to facilitate cyclic oligoadenylate production.

Indexed as

CRISPR-Associated ProteinsAdenosine TriphosphateCRISPR-Cas SystemsRNAStaphylococcus epidermidisAdenosine TriphosphateCRISPR-Associated ProteinsRNAcomplex with ATPcomplex with target RNACRISPRcrRNAcryo-EMstructuretype III-A

Identifiers

PMID35714601
PMCPMC9357104
OpenAlexW4283021088

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.