Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 504

The DOI matches its Crossref record.

D‐E‐A‐D protein family of putative RNA helicases

Schmid, S. R., Linder, P.·1992·Molecular Microbiology

Abstract

Summary: RNA metabolism plays a central role in cell growth. It is essential to regulate RNA synthesis, processing, stability and degradation. Conformational changes in RNA are key elements in regulating cellular processes. Recently, an increasing number of putative RNA helicases from different organisms ranging from Escherichia coli to humans and viruses have been identified. They are Involved in diverse cellular functions such as RNA splicing, ribosome assembly, initiation of translation, spermatogenesis, embryogenesis, and cell growth and division. Based on sequence homologies these proteins were grouped in a family, the D‐E‐A‐D box protein family (D‐E‐A‐D = Asp‐Glu‐Ala‐Asp). Some of the better characterized members have been shown to possess ATP‐binding and hydrolysing activities as well as ATP‐dependent RNA helicase activities. Most of the genes encoding such proteins have been isolated from yeast, on which we will focus in this review. From sequence data, three of the members form a subfamily, the D‐E‐A‐H subfamily.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1111/j.1365-2958.1992.tb01470.x

Cites

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cited by

See all 504

Metadata

Authors
Schmid, S. R., & Linder, P.
Venue
Molecular Microbiology
Publisher
Wiley
Published
1992-02
Volume
6
Issue
3
Pages
283-291
ISSN
  • 0950-382X (ISSN-L)
  • 1365-2958
OpenAlex
W2017874433
Cited by
504
References
0
FWCI
12.98
Type
journal article
Language
en
Open access
closed

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: D‐E‐A‐D protein family of putative RNA helicases. https://app.cochat.ai/papers/10.1111/j.1365-2958.1992.tb01470.x
The paper
Schmid, S. R., & Linder, P. (1992). D‐E‐A‐D protein family of putative RNA helicases. Molecular Microbiology. https://doi.org/10.1111/j.1365-2958.1992.tb01470.x

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.