Evidence map›Paper›PMID 24370256›Full record

ReviewProtein and peptide letters2014

Macromolecular mechanisms of protein translocation.

M Muthukumar

Abstract readReview
In one paragraph

Review in Protein and peptide letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. 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

1 author.

M MuthukumarDepartment of Polymer Science and Engineering, University of Massachusetts, Amherst, MA 01003, USA. muthu@polysci.umass.edu.

Funding

Modeling Macromolecular Transport through Protein Channels and NanoporesR01HG002776 · NHGRI · UNIVERSITY OF MASSACHUSETTS AMHERST · PI MUTHUKUMAR, MURUGAPPAN · 2003 to 2022
$5.3M
NHGRI NIH HHS R01 HG002776NHGRI NIH HHS R01HG002776-09
6 · The paper itself

Abstract

When macromolecules such as proteins are forced to translocate through a narrow pore, their conformational entropy is reduced, resulting in a free energy barrier. This free energy barrier is additionally modulated by protein-pore interactions. Furthermore, the driving force of the translocation such as the electrochemical potential gradient and electroosmotic flow navigates the transport of the protein through the free energy landscape. Depending on the specifics of the protein-pore system and the driving force, the details of the translocation process and their statistical properties such as the average translocation time can vary significantly. Nevertheless, there are a few fundamental physical concepts that underly the ubiquitous phenomenon of polymer translocation, which are reviewed here.

Indexed as

AnimalsEntropyHumansNanoporesProtein ConformationProteinsProtein TransportProteins

Identifiers

PMID24370256
PMCPMC5956915

What OpenQuestion holds

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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.