Evidence map›Paper›PMID 34942166›Full record

ArticleJournal of molecular biology2022

Structural Mechanics of the Alpha-2-Macroglobulin Transformation.

Yasuhiro Arimura, Hironori Funabiki

Abstract read
In one paragraph

Article in Journal of molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Human α2-Macroglobulin: Architecture, Mechanisms, and Functional Implications.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Proteases in intestinal health and disease.Nature reviews. Gastroenterology & hepatology · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Plasma proteome fingerprint in kidney diseases.Frontiers in molecular biosciences · 2024
    Article
  10. Review
  11. Article
  12. Article
  13. Recent cryogenic electron microscopy structures of human A2M may not be representative of the native protein.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Article
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

2 authors.

Yasuhiro ArimuraLaboratory of Chromosome and Cell Biology, The Rockefeller University, New York, NY 10065, United States. Electronic address: yarimura@rockefeller.edu.
Hironori FunabikiLaboratory of Chromosome and Cell Biology, The Rockefeller University, New York, NY 10065, United States. Electronic address: funabih@rockefeller.edu.

Funding

Regulation of mitotic chromosomes - Revision - 2R35GM132111 · NIGMS · ROCKEFELLER UNIVERSITY · PI Hironori Funabiki · 2019 to 2026
$6.9M
NIGMS NIH HHS R35 GM132111
6 · The paper itself

Abstract

Alpha-2-Macroglobulin (A2M) is the critical pan-protease inhibitor of the innate immune system. When proteases cleave the A2M bait region, global structural transformation of the A2M tetramer is triggered to entrap the protease. The structural basis behind the cleavage-induced transformation and the protease entrapment remains unclear. Here, we report cryo-EM structures of native- and intermediate-forms of the Xenopus laevis egg A2M homolog (A2Moo or ovomacroglobulin) tetramer at 3.7-4.1 Å and 6.4 Å resolution, respectively. In the native A2Moo tetramer, two pairs of dimers arrange into a cross-like configuration with four 60 Å-wide bait-exposing grooves. Each bait in the native form threads into an aperture formed by three macroglobulin domains (MG2, MG3, MG6). The bait is released from the narrowed aperture in the induced protomer of the intermediate form. We propose that the intact bait region works as a "latch-lock" to block futile A2M transformation until its protease-mediated cleavage.

Indexed as

alpha-MacroglobulinsProteolysisTranscription FactorsXenopus ProteinsCryoelectron MicroscopyPeptide HydrolasesProtein ConformationProtein MultimerizationA2M protein, Xenopusalpha-MacroglobulinsovomacroglobulinPeptide HydrolasesTranscription FactorsXenopus Proteinsalpha-2-macroglobulincryo-EMinnate immunityprotein inhibitorXenopus egg extract

Identifiers

PMID34942166
PMCPMC8897276

What OpenQuestion holds

Textmetadata
LicenceTDM
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.