Evidence map›Paper›PMID 27373148›Full record

ArticleCell reports2016

2.8-Å Cryo-EM Structure of the Large Ribosomal Subunit from the Eukaryotic Parasite Leishmania.

Moran Shalev-Benami, Yan Zhang, Donna Matzov, Yehuda Halfon, Arie Zackay, Haim Rozenberg, Ella Zimmerman, Anat Bashan, Charles L Jaffe, Ada Yonath and 1 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

42 citing papers in PubMed, 73 citations in OpenAlex.

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  18. The 23S Ribosomal RNA FromFrontiers in microbiology · 2020
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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

11 authors at 2 institutions in 2 countries.

Moran Shalev-BenamiDepartment of Structural Biology, Faculty of Chemistry, Weizmann Institute of Science, Rehovot 7610001, Israel.
Yan ZhangLife Sciences Institute and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Donna MatzovDepartment of Structural Biology, Faculty of Chemistry, Weizmann Institute of Science, Rehovot 7610001, Israel.
Yehuda HalfonDepartment of Structural Biology, Faculty of Chemistry, Weizmann Institute of Science, Rehovot 7610001, Israel.
Arie ZackayDepartment of Microbiology and Molecular Genetics, IMRIC, Hebrew University-Hadassah Medical School, Jerusalem 9112102, Israel.
Haim RozenbergDepartment of Structural Biology, Faculty of Chemistry, Weizmann Institute of Science, Rehovot 7610001, Israel.
Ella ZimmermanDepartment of Structural Biology, Faculty of Chemistry, Weizmann Institute of Science, Rehovot 7610001, Israel.
Anat BashanDepartment of Structural Biology, Faculty of Chemistry, Weizmann Institute of Science, Rehovot 7610001, Israel.
Charles L JaffeDepartment of Microbiology and Molecular Genetics, IMRIC, Hebrew University-Hadassah Medical School, Jerusalem 9112102, Israel.
Ada YonathDepartment of Structural Biology, Faculty of Chemistry, Weizmann Institute of Science, Rehovot 7610001, Israel. Electronic address: ada.yonath@weizmann.ac.il.
Georgios SkiniotisLife Sciences Institute and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: skinioti@umich.edu.
Weizmann Institute of Science · ILUniversity of Michigan–Ann Arbor · US

Funding

Architectural Basis of Leptin Transmembrane SignalingR01DK090165 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SKINIOTIS, GEORGIOS · 2011 to 2017
$2.3M
NIDDK NIH HHS R01 DK090165
6 · The paper itself

Abstract

Leishmania is a single-cell eukaryotic parasite of the Trypanosomatidae family, whose members cause an array of tropical diseases. The often fatal outcome of infections, lack of effective vaccines, limited selection of therapeutic drugs, and emerging resistant strains, underline the need to develop strategies to combat these pathogens. The Trypanosomatid ribosome has recently been highlighted as a promising therapeutic target due to structural features that are distinct from other eukaryotes. Here, we present the 2.8-Å resolution structure of the Leishmania donovani large ribosomal subunit (LSU) derived from a cryo-EM map, further enabling the structural observation of eukaryotic rRNA modifications that play a significant role in ribosome assembly and function. The structure illustrates the unique fragmented nature of leishmanial LSU rRNA and highlights the irregular distribution of rRNA modifications in Leishmania, a characteristic with implications for anti-parasitic drug development.

Indexed as

Leishmania donovaniCryoelectron MicroscopyModels, MolecularNucleic Acid ConformationProtein Structure, QuaternaryProtozoan ProteinsRibosomal ProteinsRibosome Subunits, LargeRNA, ProtozoanRNA, RibosomalProtozoan ProteinsRibosomal ProteinsRNA, ProtozoanRNA, Ribosomal

Identifiers

PMID27373148
PMCPMC5835689
OpenAlexW2474384657

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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.