Evidence map›Paper›PMID 35124797›Full record

ReviewBritish journal of pharmacology2022

Peptidylglycine α-amidating monooxygenase as a therapeutic target or biomarker for human diseases.

David J Merkler, Aidan J Hawley, Betty A Eipper, Richard E Mains

Open access · bronzeAbstract readReview
In one paragraph

Review in British journal of pharmacology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Review
  3. A ribosomally synthesized and posttranslationally modified peptide with ADP-ribosylation.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

4 authors at 2 institutions in 1 country.

David J MerklerDepartment of Chemistry, University of South Florida, Tampa, Florida, USA.
Aidan J HawleyDepartment of Chemistry, University of South Florida, Tampa, Florida, USA.
Betty A EipperDepartment of Molecular Biology & Biophysics, University of Connecticut Health Center, Farmington, Connecticut, USA.
Richard E MainsDepartment of Neuroscience, University of Connecticut Health Center, Farmington, Connecticut, USA.ORCID 0000-0003-1154-1331
UConn Health · USUniversity of South Florida · US

Funding

CELL BIOLOGY OF BIOACTIVE PEPTIDE SECRETIONR01DK032948 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH ANNE, MAINS, RICHARD E · 1986 to 2019
$7.3M
BIOCHEMISTRY AND PHYSIOLOGY OF PEPTIDE AMIDATIONR01DK032949 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH ANNE, KING, STEPHEN M · 1986 to 2017
$6.4M
Peptide Amidation in CiliogenesisR01GM125606 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI KING, STEPHEN M · 2019 to 2021
$1.3M
Tools and Methods for the Elucidation of Fatty Acid Amide Cell Signaling PathwaysR21GM140390 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI LEAHY, JAMES · 2021 to 2022
$391k
Enzymatic Cleavage of the C-N Bond in GlycineR15GM073659 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI MERKLER, DAVID J · 2005 to 2005
$218k
Anti-PAM Inhibitors for the Treatment of CancerR15GM067257 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI MERKLER, DAVID J · 2002 to 2002
$145k
NIDDK NIH HHS R01 DK032948NIDDK NIH HHS R01 DK032949NIGMS NIH HHS R01 GM125606NIGMS NIH HHS R15 GM067257NIGMS NIH HHS R15 GM073659NIGMS NIH HHS R21 GM140390
6 · The paper itself

Abstract

Peptides play a key role in controlling many physiological and neurobiological pathways. Many bioactive peptides require a C-terminal α-amide for full activity. The bifunctional enzyme catalysing α-amidation, peptidylglycine α-amidating monooxygenase (PAM), is the sole enzyme responsible for amidated peptide biosynthesis, from Chlamydomonas reinhardtii to Homo sapiens. Many neuronal and endocrine functions are dependent upon amidated peptides; additional amidated peptides are growth promoters in tumours. The amidation reaction occurs in two steps, glycine α-hydroxylation followed by dealkylation to generate the α-amide product. Currently, most potentially useful inhibitors target the first reaction, which is rate-limiting. PAM is a membrane-bound enzyme that visits the cell surface during peptide secretion. PAM is then used again in the biosynthetic pathway, meaning that cell-impermeable inhibitors or inactivators could have therapeutic value for the treatment of cancer or psychiatric abnormalities. To date, inhibitor design has not fully exploited the structures and mechanistic details of PAM.

Indexed as

Mixed Function OxygenasesAmidesAnimalsBiomarkersHumansMolecular Targeted TherapyMultienzyme ComplexesPeptidesAmidesBiomarkersMixed Function OxygenasesMultienzyme ComplexesPeptidespeptidylglycine monooxygenaseascorbatecopperoxygenpeptidepeptidylglycine α-amidating monooxygenase

Identifiers

PMID35124797
PMCPMC9177522
OpenAlexW4210679780

What Socratic 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 Socratic graph.