Evidence map›Paper›PMID 30337134›Full record

ReviewTrends in biochemical sciences2019

Monotopic Membrane Proteins Join the Fold.

Karen N Allen, Sonya Entova, Leah C Ray, Barbara Imperiali

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

32 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Scrutinizing aApplied and environmental microbiology · 2024
    Article
  6. Article
  7. Cryo-EM analysis ofScience advances · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Retinal pigment epithelium 65 kDa protein (RPE65): An update.Progress in retinal and eye research · 2022
    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

4 authors at 2 institutions in 1 country.

Karen N AllenDepartment of Chemistry, Boston University, Boston, MA 02215, USA; Program in Biomolecular Pharmacology, Boston University School of Medicine, Boston, MA 02118, USA. Electronic address: drkallen@bu.edu.
Sonya EntovaDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Leah C RayProgram in Biomolecular Pharmacology, Boston University School of Medicine, Boston, MA 02118, USA.
Barbara ImperialiDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. Electronic address: imper@mit.edu.
Boston University · USMassachusetts Institute of Technology · US

Funding

PRE-DOCTORAL TRAINING IN THE BIOLOGICAL SCIENCEST32GM007287 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BELL, STEPHEN P., KEATING, AMY E · 1985 to 2019
$40.8M
SPECIFICITY IN CO- AND POST-TRANSLATIONAL MODIFICATIONR01GM039334 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALLEN, KAREN N., IMPERIALI, BARBARA · 1993 to 2025
$8.0M
TRAINING IN BIOMOLECULAR PHARMACOLOGYT32GM008541 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI FARB, DAVID H · 1997 to 2022
$5.2M
NIGMS NIH HHS R01 GM039334NIGMS NIH HHS T32 GM007287NIGMS NIH HHS T32 GM008541
6 · The paper itself

Abstract

Monotopic membrane proteins, classified by topology, are proteins that embed into a single face of the membrane. These proteins are generally underrepresented in the Protein Data Bank (PDB), but the past decade of research has revealed new examples that allow the description of generalizable features. This Opinion article summarizes shared characteristics including oligomerization states, modes of membrane association, mechanisms of interaction with hydrophobic or amphiphilic substrates, and homology to soluble folds. We also discuss how associations of monotopic enzymes in pathways can be used to promote substrate specificity and product composition. These examples highlight the challenges in structure determination specific to this class of proteins, but also the promise of new understanding from future study of these proteins that reside at the interface.

Indexed as

AnimalsDatabases, ProteinHumansHydrophobic and Hydrophilic InteractionsMembrane ProteinsMembrane Proteinsmembrane interfacemembrane–protein interactionmembranomemonotopic enzymes

Identifiers

PMID30337134
PMCPMC6309722
OpenAlexW2896957283

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.