Evidence map›Paper›PMID 32647822›Full record

ArticleJournal of structural biology: X2020

Structural basis for differentiation between two classes of thiolase: Degradative vs biosynthetic thiolase.

Sukritee Bhaskar, David L Steer, Ruchi Anand, Santosh Panjikar

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of structural biology: X, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

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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 3 institutions in 2 countries.

Sukritee BhaskarIITB-Monash Research Academy, Mumbai 400076, Maharashtra, India.
David L SteerMonash Proteomics and Metabolomics Facility, Monash University, Victoria 3800, Australia.
Ruchi AnandDepartment of Chemistry, Indian Institute of Technology Bombay, Mumbai 400076, Maharashtra, India.
Santosh PanjikarDepartment of Biochemistry and Molecular Biology, Monash University, Victoria 3800, Australia.
Indian Institute of Technology Bombay · INAustralian Nuclear Science and Technology Organisation · AUMonash University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thiolases are a well characterized family of enzymes with two distinct categories: degradative, β-ketoadipyl-CoA thiolases and biosynthetic, acetoacetyl-CoA thiolases. Both classes share an identical catalytic triad but catalyze reactions in opposite directions. Moreover, it is established that in contrast to the biosynthetic thiolases the degradative thiolases can accept substrates with broad chain lengths. Hitherto, no residue or structural pattern has been recognized that might help to discern the two thiolases, here we exploit, a tetrameric degradative thiolase from

Indexed as

AA-mutants, H356A-C386A MutantA-mutant-HAL-CoA, A-mutant-hexanal CoA complexA-mutant-Hex-CoA, A-mutant-Hexanoyl CoA complexA-mutants, H356A MutantAS-mutant-OAL-CoA, AS-mutant-octanal CoA complexAS-mutant-Oct-CoA, AS-mutant-Octanoyl CoA complexAS-mutants, H356A-C90S MutantCovalent lockingCovering loopHAL, hexanalHexanoyl CoAHex-CoA, Hexanoyl CoAMtb-thiolase, Mycobacterium tuberculosis thiolaseOAL, octanalOctanoyl CoAOct-CoA, Octanoyl CoAPcaF, β-ketoadipyl-CoA thiolaseTunnelZr-thiolase, Zoogleria ramigera thiolase

Identifiers

PMID32647822
PMCPMC7337054
OpenAlexW2999976776

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.