Evidence map›Paper›PMID 24349474›Full record

ArticlePloS one2013

LipL41, a hemin binding protein from Leptospira santarosai serovar Shermani.

Ming-Hsing Lin, Yuan-Chih Chang, Chwan-Deng Hsiao, Shih-Hsun Huang, Min-Shi Wang, Yi-Ching Ko, Chih-Wei Yang, Yuh-Ju Sun

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 28 citations in OpenAlex.

  1. Leptospirosis.Nature reviews. Disease primers · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Pathogen-specific leptospiral proteins in urine of patients with febrile illness aids in differential diagnosis of leptospirosis from dengue.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2018
    Article
  11. The leptospiral outer membrane.Current topics in microbiology and immunology · 2015
    Review
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

8 authors at 4 institutions in 1 country.

Ming-Hsing LinInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, Taiwan.
Yuan-Chih ChangInstitute of Cellular and Organismic Biology, Academia Sinica, Taipei, Taiwan.
Chwan-Deng HsiaoInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Shih-Hsun HuangInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, Taiwan.
Min-Shi WangInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, Taiwan.
Yi-Ching KoDepartment of Nephrology, Kidney Research Center, Chang Gung Memorial Hospital, Chang Gung University College of Medicine, Taoyuan, Taiwan.
Chih-Wei YangDepartment of Nephrology, Kidney Research Center, Chang Gung Memorial Hospital, Chang Gung University College of Medicine, Taoyuan, Taiwan.
Yuh-Ju SunInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, Taiwan.
National Tsing Hua University · TWChang Gung University · TWInstitute of Cellular and Organismic Biology, Academia Sinica · TWInstitute of Molecular Biology, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Leptospirosis is one of the most widespread zoonotic diseases in the world. It is caused by the pathogen Leptospira that results in multiple-organ failure, in particular of the kidney. Outer membrane lipoprotein is the suspected virulence factor of Leptospira. In Leptospira spp LipL41 is one major lipoprotein and is highly conserved. Previous study suggests that LipL41 bears hemin-binding ability and might play a possible role in iron regulation and storage. However, the characterization of hemin-binding ability of LipL41 is still unclear. Here the hemin-binding ability of LipL41 was examined, yielding a K d = 0.59 ± 0.14 μM. Two possible heme regulatory motifs (HRMs), C[P/S], were found in LipL41 at (140)Cys-Ser and (220)Cys-Pro. The mutation study indicates that Cys140 and Cys220 might be cooperatively involved in hemin binding. A supramolecular assembly of LipL41 was determined by transmission electron microscopy. The LipL41 oligomer consists of 36 molecules and folds as a double-layered particle. At the C-terminus of LipL41, there are two tetratricopeptide repeats (TPRs), which might be involved in the protein-protein interaction of the supramolecular assembly.

Indexed as

Bacterial ProteinsCarrier ProteinsHeme-Binding ProteinsHemeproteinsHeminLeptospiraLipoproteinsProtein MultimerizationBacterial ProteinsCarrier ProteinsHeme-Binding ProteinsHemeproteinsHeminLipoproteins

Identifiers

PMID24349474
PMCPMC3861479
OpenAlexW2161140633

What OpenQuestion holds

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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.