Evidence map›Paper›PMID 24470285›Full record

ReviewProteomics. Clinical applications2014

Carboxypeptidases in disease: insights from peptidomic studies.

Matthew R Sapio, Lloyd D Fricker

Open access · greenAbstract readReview
In one paragraph

Review in Proteomics. Clinical applications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.6field-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

35 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. International journal of molecular sciences · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Origins, Technological Advancement, and Applications of Peptidomics.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  12. Article
  13. Article
  14. The identification of two M20B family peptidases required for full virulence inFrontiers in cellular and infection microbiology · 2023
    Article
  15. Review
  16. In Silico Structural Analysis of Serine CarboxypeptidaseInternational journal of molecular sciences · 2022
    Article
  17. Structure ofLife science alliance · 2022
    Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Matthew R SapioDepartment of Neuroscience, Albert Einstein College of Medicine, Bronx, NY, USA.
Lloyd D Fricker
Albert Einstein College of Medicine · US

Funding

REGULATION OF ENKEPHALIN CONVERTASE--CARBOXYPEPTIDASE ER01DA004494 · NIDA · YESHIVA UNIVERSITY · PI FRICKER, LLOYD D · 1987 to 2015
$5.9M
NIDA NIH HHS DA-004494NIDA NIH HHS R01 DA004494
6 · The paper itself

Abstract

Carboxypeptidases (CPs) perform many diverse physiological functions by removing C-terminal amino acids from proteins and peptides. Some CPs function in the degradation of proteins in the digestive tract while other enzymes play biosynthetic roles in the formation of neuropeptides and peptide hormones. Another set of CPs modify tubulin by removing amino acids from the C-terminus and from polyglutamyl side chains, thereby altering the properties of microtubules. This review focuses on three CPs: carboxypeptidase E, carboxypeptidase A6, and cytosolic carboxypeptidase 1. Naturally occurring mutations in all three of these enzymes are associated with disease phenotypes, ranging from obesity to epilepsy to neurodegeneration. Peptidomics is a useful tool to investigate the relationship between these mutations and alterations in peptide levels. This technique has also been used to define the function and characteristics of CPs. Results from peptidomics studies have helped to elucidate the function of CPs and clarify the biological underpinnings of pathologies by identifying peptides altered in disease states. This review describes the use of peptidomic techniques to gain insights into the normal function of CPs and the molecular defects caused by mutations in the enzymes.

Indexed as

DiseaseAnimalsCarboxypeptidasesHumansPeptidesProteomicsCarboxypeptidasesPeptidesCarboxypeptidaseMetallopeptidase

Identifiers

PMID24470285
PMCPMC4062080
OpenAlexW2126743932

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.