Evidence map›Paper›PMID 20957445›Full record

ArticleCellular & molecular biology letters2011

The prediction of novel multiple lipid-binding regions in protein translocation motor proteins: a possible general feature.

Rob C A Keller

Open access · hybridAbstract read
In one paragraph

Article in Cellular & molecular biology letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 25% 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

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Biomedical reports · 2018
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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

1 author.

Rob C A KellerSection Chemistry, Charlemagne College, Wilhelminastraat 13-15, Nijmegen, 3913 NH, The Netherlands. r.keller@kgcnijmegen.nl

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein translocation is an important cellular process. SecA is an essential protein component in the Sec system, as it contains the molecular motor that facilitates protein translocation. In this study, a bioinformatics approach was applied in the search for possible lipid-binding helix regions in protein translocation motor proteins. Novel lipid-binding regions in Escherichia coli SecA were identified. Remarkably, multiple lipid-binding sites were also identified in other motor proteins such as BiP, which is involved in ER protein translocation. The prokaryotic signal recognition particle receptor FtsY, though not a motor protein, is in many ways related to SecA, and was therefore included in this study. The results demonstrate a possible general feature for motor proteins involved in protein translocation.

Indexed as

Protein TransportAdenosine TriphosphatasesAmino Acid SequenceBacterial ProteinsComputational BiologyEndoplasmic Reticulum Chaperone BiPEscherichia coliHeat-Shock ProteinsLipidsMembrane Transport ProteinsMolecular Motor ProteinsMolecular Sequence DataProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryReceptors, Cytoplasmic and NuclearAdenosine TriphosphatasesBacterial ProteinsEndoplasmic Reticulum Chaperone BiPFtsY protein, BacteriaHeat-Shock ProteinsLipidsMembrane Transport ProteinsMolecular Motor ProteinsReceptors, Cytoplasmic and NuclearSecA ProteinsSEC Translocation Channels

Identifiers

PMID20957445
PMCPMC6275888
OpenAlexW2028677391

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.