Evidence map›Paper›PMID 39572145›Full record

ArticleMethods in enzymology2024

Sample optimizations to enable the structure determination of biotin-dependent carboxylases.

Jia Wei, Christine S Huang, Yang Shen, Kianoush Sadre-Bazzaz, Liang Tong

Abstract read
In one paragraph

Article in Methods in enzymology, 2024. 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
–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

0 citing papers in PubMed.

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

5 authors.

Jia WeiDepartment of Biological Sciences, Columbia University, New York, NY, United States.
Christine S HuangDepartment of Biological Sciences, Columbia University, New York, NY, United States.
Yang ShenDepartment of Biological Sciences, Columbia University, New York, NY, United States.
Kianoush Sadre-BazzazDepartment of Biological Sciences, Columbia University, New York, NY, United States.
Liang TongDepartment of Biological Sciences, Columbia University, New York, NY, United States. Electronic address: ltong@columbia.edu.

Funding

Structural and functional studies of mRNA processing, stability and quality controlR35GM118093 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI LIANG TONG · 2016 to 2026
$8.5M
Structural biology of enzymes in fatty acid metabolismR01DK067238 · NIDDK · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TONG, LIANG · 2004 to 2012
$2.6M
NIDDK NIH HHS R01 DK067238NIGMS NIH HHS R35 GM118093
6 · The paper itself

Abstract

Biotin-dependent carboxylases have central roles in the metabolisms of fatty acids, amino acids and other compounds. Their functional importance is underscored by their strong conservation from bacteria to humans. These enzymes are large, multi-domain or multi-subunit complexes, and can have molecular weights of 500 to 750 kDa. Despite their large sizes, the first structures of most of these enzymes were determined using X-ray crystallography. This chapter presents various technical challenges that were overcome during their structure determination, which involves extensive optimization of the protein samples and their crystals. The cryo electron microscopy resolution revolution has made it easier to study these large complexes at the atomic level.

Indexed as

BiotinCryoelectron MicroscopyCarbon-Nitrogen LigasesCrystallizationCrystallography, X-RayHumansModels, MolecularProtein ConformationBiotinbiotin carboxylaseCarbon-Nitrogen LigasesAcetyl-CoA carboxylaseCryo electron microscopyMethylcrotonyl-CoA carboxylasePropionyl-CoA carboxylaseProtein crystallographyPyruvate carboxylaseStructural biology

Identifiers

PMID39572145
PMCPMC11734766

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Registered trials

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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.