Evidence map›Paper›PMID 25414705›Full record

ReviewFrontiers in immunology2014

Deciphering the fine details of c1 assembly and activation mechanisms: "mission impossible"?

Christine Gaboriaud, Wai Li Ling, Nicole M Thielens, Isabelle Bally, Véronique Rossi

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

32 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Mechanisms by which Factor H protectsFrontiers in immunology · 2024
    Article
  7. Functional assays to evaluate antibody-mediated responses againstFrontiers in cellular and infection microbiology · 2023
    Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Complement C1r serine protease contributes to kidney fibrosis.American journal of physiology. Renal physiology · 2019
    Article
  17. Article
  18. Frontiers in immunology · 2019
    Article
  19. Two Different MissenseFrontiers in immunology · 2019
    Article
  20. 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

5 authors at 4 institutions in 1 country.

Christine GaboriaudInstitut de Biologie Structurale, Université Grenoble Alpes , Grenoble , France ; CNRS, Institut de Biologie Structurale , Grenoble , France ; CEA, Institut de Biologie Structurale , Grenoble , France.
Wai Li LingInstitut de Biologie Structurale, Université Grenoble Alpes , Grenoble , France ; CNRS, Institut de Biologie Structurale , Grenoble , France ; CEA, Institut de Biologie Structurale , Grenoble , France.
Nicole M ThielensInstitut de Biologie Structurale, Université Grenoble Alpes , Grenoble , France ; CNRS, Institut de Biologie Structurale , Grenoble , France ; CEA, Institut de Biologie Structurale , Grenoble , France.
Isabelle BallyInstitut de Biologie Structurale, Université Grenoble Alpes , Grenoble , France ; CNRS, Institut de Biologie Structurale , Grenoble , France ; CEA, Institut de Biologie Structurale , Grenoble , France.
Véronique RossiInstitut de Biologie Structurale, Université Grenoble Alpes , Grenoble , France ; CNRS, Institut de Biologie Structurale , Grenoble , France ; CEA, Institut de Biologie Structurale , Grenoble , France.
Institut de Biologie Structurale · FRCEA Grenoble · FRCentre National de la Recherche Scientifique · FRUniversité Grenoble Alpes · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The classical complement pathway is initiated by the large (~800 kDa) and flexible multimeric C1 complex. Its catalytic function is triggered by the proteases hetero-tetramer C1r2s2, which is associated to the C1q sensing unit, a complex assembly of 18 chains built as a hexamer of heterotrimers. Initial pioneering studies gained insights into the main architectural principles of the C1 complex. A dissection strategy then provided the high-resolution structures of its main functional and/or structural building blocks, as well as structural details on some key protein-protein interactions. These past and current discoveries will be briefly summed up in order to address the question of what is still ill-defined. On a functional point of view, the main molecular determinants of C1 activation and its tight control will be delineated. The current perspective remains to decipher how C1 really works and is controlled in vivo, both in normal and pathological settings.

Indexed as

C1 complexC1qC1rC1sclassical complement pathwaycomplement-dependent cytotoxicityserine protease activationX-ray structures

Identifiers

PMID25414705
PMCPMC4222235
OpenAlexW2037604262

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.