Evidence map›Paper›PMID 18184105›Full record

ReviewAnnual review of pharmacology and toxicology2008

Proteases for processing proneuropeptides into peptide neurotransmitters and hormones.

Vivian Hook, Lydiane Funkelstein, Douglas Lu, Steven Bark, Jill Wegrzyn, Shin-Rong Hwang

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of pharmacology and toxicology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed, 1 pooled it
10.5field-weighted citation impact, top 1% 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

131 citing papers in PubMed, 1 synthesis or guideline pooled it, 262 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
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  8. Review
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  12. Review
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  15. Article
  16. Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Neuropeptidomics of the American LobsterJournal of proteome research · 2024
    Article
  18. Article
  19. Review
  20. Article

71 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Vivian HookSkaggs School of Pharmacy and Pharmaceutical Sciences, and Department of Neuroscience, Pharmacology, and Medicine, School of Medicine, University of California-San Diego, La Jolla, CA 92093-0744, USA. vhook@ucsd.edu
Lydiane Funkelstein
Douglas Lu
Steven Bark
Jill Wegrzyn
Shin-Rong Hwang
University of California, San Diego · US

Funding

Trafficking of catecholamine storage vesicle proteinsP01HL058120 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ZIEGLER, MICHAEL G. · 1999 to 2009
$18.5M
Serpin Protease Inhibitors &Opioid NeuropeptidesR01NS024553 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HOOK, VIVIAN Y. H. · 1987 to 2006
$2.5M
BIOSYNTHESIS OF ENKEPHALIN OPIOID PEPTIDESR01DA004271 · NIDA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HOOK, VIVIAN Y. H · 1987 to 2009
$2.5M
POMC Processing Beta-Endorphin-Related Opioid PeptidesR01MH077305 · NIMH · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HOOK, VIVIAN Y. H · 2006 to 2010
$1.6M
NHLBI NIH HHS P01 HL058120NIDA NIH HHS R01 DA004271NIMH NIH HHS R01 MH077305NINDS NIH HHS R01 NS024553
6 · The paper itself

Abstract

Peptide neurotransmitters and peptide hormones, collectively known as neuropeptides, are required for cell-cell communication in neurotransmission and for regulation of endocrine functions. Neuropeptides are synthesized from protein precursors (termed proneuropeptides or prohormones) that require proteolytic processing primarily within secretory vesicles that store and secrete the mature neuropeptides to control target cellular and organ systems. This review describes interdisciplinary strategies that have elucidated two primary protease pathways for prohormone processing consisting of the cysteine protease pathway mediated by secretory vesicle cathepsin L and the well-known subtilisin-like proprotein convertase pathway that together support neuropeptide biosynthesis. Importantly, this review discusses important areas of current and future biomedical neuropeptide research with respect to biological regulation, inhibitors, structural features of proneuropeptide and protease interactions, and peptidomics combined with proteomics for systems biological approaches. Future studies that gain in-depth understanding of protease mechanisms for generating active neuropeptides will be instrumental for translational research to develop pharmacological strategies for regulation of neuropeptide functions. Pharmacological applications for neuropeptide research may provide valuable therapeutics in health and disease.

Indexed as

AnimalsCathepsin LCathepsinsCysteine EndopeptidasesHumansMiceNeuropeptidesNeurotransmitter AgentsPeptide HormonesPeptide HydrolasesProprotein ConvertasesProtease InhibitorsProtein PrecursorsCathepsin LCathepsinsCTSL protein, humanCtsl protein, mouseCysteine EndopeptidasesNeuropeptidesNeurotransmitter AgentsPeptide HormonesPeptide HydrolasesProprotein ConvertasesProtease InhibitorsProtein Precursors

Identifiers

PMID18184105
PMCPMC2731677
OpenAlexW2134660680

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.