Evidence map›Paper›PMID 33385272›Full record

ArticleMolecular biotechnology2021

Dramatic Changes in Oligomerization Property Caused by Single Residue Deletion in Staphylococcus aureus Enolase.

Vijay Hemmadi, Malabika Biswas

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.3field-weighted citation impact, top 45% 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

0 citing papers in PubMed, 4 citations in OpenAlex.

No citing paper in PubMed yet.

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.

Vijay HemmadiDepartment of Biological Sciences, Birla Institute of Technology and Science, Pilani, K. K. Birla Goa Campus, NH17B, Zuarinagar, Goa, 403726, India.ORCID http://orcid.org/0000-0002-8169-6817
Malabika BiswasDepartment of Biological Sciences, Birla Institute of Technology and Science, Pilani, K. K. Birla Goa Campus, NH17B, Zuarinagar, Goa, 403726, India. mbiswas@goa.bits-pilani.ac.in.ORCID http://orcid.org/0000-0002-2497-9765
Birla Institute of Technology and Science, Pilani - Goa Campus · IN

Funding

DST-SERB EMR/2015/002229
6 · The paper itself

Abstract

Studies were conducted to understand the role of C-terminal lysine residues in the catalytic activity, structural stability and oligomeric properties of Staphylococcus aureus enolase. Interestingly, the S. aureus enolase, in solution, shows its presence as a stable dimer as well as the catalytically active fragile octamer. Compared to the hexa-histidine tagged S. aureus enolase (rSaeno), the deletion mutant showed the negligible difference in K

Indexed as

Protein MultimerizationBiocatalysisCloning, MolecularDynamic Light ScatteringEnzyme StabilityHydrogen-Ion ConcentrationIonsKineticsLysineMutant ProteinsMutationPhosphopyruvate HydrataseProtein Structure, SecondarySpectrometry, FluorescenceStaphylococcus aureusSubstrate SpecificityIonsLysineMutant ProteinsPhosphopyruvate HydrataseTryptophanCatalysisC-terminal lysineEnolaseKineticsMetalsMutantOctamer

Identifiers

PMID33385272
OpenAlexW3117242186

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.