Evidence map›Paper›PMID 33233712›Full record

ArticleMarine drugs2020

Endolysins from Antarctic

Marco Orlando, Sandra Pucciarelli, Marina Lotti

Abstract read
In one paragraph

Article in Marine drugs, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

13 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. DNA damage-associated vesicle production inJournal of bacteriology · 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

3 authors.

Marco OrlandoDepartment of Biotechnology and Biosciences, State University of Milano Bicocca, 20126 Milano, Italy.ORCID 0000-0002-5914-3052
Sandra PucciarelliSchool of Biosciences and Veterinary Medicine, University of Camerino, 62032 Camerino, Italy.
Marina LottiDepartment of Biotechnology and Biosciences, State University of Milano Bicocca, 20126 Milano, Italy.ORCID 0000-0001-5419-7572

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Organisms specialized to thrive in cold environments (so-called psychrophiles) produce enzymes with the remarkable ability to catalyze chemical reactions at low temperature. Cold activity relies on adaptive changes in the proteins' sequence and structural organization that result in high conformational flexibility. As a consequence of flexibility, several such enzymes are inherently heat sensitive. Cold-active enzymes are of interest for application in a number of bioprocesses, where cold activity coupled with easy thermal inactivation can be of advantage. We describe the biochemical and functional properties of two glycosyl hydrolases (named LYS177 and LYS188) of family 19 (GH19), identified in the genome of an Antarctic marine

Indexed as

Cold TemperatureAntarctic RegionsBacterial ProteinsEndopeptidasesEnzyme StabilityEvolution, MolecularHalf-LifeMuramidasePseudomonasSubstrate SpecificityBacterial ProteinsendolysinEndopeptidasesMuramidasecold-active enzymecold adaptationendolysinglycoside hydrolase 19

Identifiers

PMID33233712
PMCPMC7699920

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.