Evidence map›Paper›PMID 30960835›Full record

ReviewPolymers2018

Role of PhaC Type I and Type II Enzymes during PHA Biosynthesis.

Valeria Mezzolla, Oscar Fernando D'Urso, Palmiro Poltronieri

Open access · goldAbstract readReview
In one paragraph

Review in Polymers, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

16 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. 3 Biotech · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. PHA Production and PHA Synthases of the Halophilic BacteriumBioengineering (Basel, Switzerland) · 2020
    Article
  15. Article
  16. 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

3 authors at 2 institutions in 1 country.

Valeria MezzollaDepartment of Biological and Environmental Science and Technologies, University of Salento, Ecotekne, 73100 Lecce, Italy. valeria.mezzolla@gmail.com.ORCID 0000-0002-2844-6990
Oscar Fernando D'UrsoDepartment of Biological and Environmental Science and Technologies, University of Salento, Ecotekne, 73100 Lecce, Italy. bioesplora@gmail.com.
Palmiro PoltronieriCNR, Agrofood Department, Institute of Sciences of Food Productions (ISPA-CNR), 73100 Lecce, Italy. palmiro.poltronieri@ispa.cnr.it.ORCID 0000-0002-5404-9411
University of Salento · ITInstitute of Sciences of Food Production · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PHA synthases (PhaC) are grouped into four classes based on the kinetics and mechanisms of reaction. The grouping of PhaC enzymes into four classes is dependent on substrate specificity, according to the preference in forming short-chain-length (scl) or medium-chain-length (mcl) polymers: Class I, Class III and Class IV produce scl-PHAs depending on propionate, butyrate, valerate and hexanoate precursors, while Class II PhaC synthesize mcl-PHAs based on the alkane (C6 to C14) precursors. PHA synthases of Class I, in particular PhaC

Indexed as

C3–C14 alkanesclassificationdimerizationexit cavityPhaC synthasepolymer compositionsubstrate binding

Identifiers

PMID30960835
PMCPMC6403647
OpenAlexW2885033661

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.