Evidence map›Paper›PMID 34210544›Full record

ArticleTrends in biochemical sciences2021

Protein Amyloid Cofactors: Charged Side-Chain Arrays Meet Their Match?

Emily Lewkowicz, Shobini Jayaraman, Olga Gursky

Abstract read
In one paragraph

Article in Trends in biochemical sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
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  11. Review
  12. Article
  13. RNA tailing machinery drives amyloidogenic phase transition.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Role of complementarity-determining regions 1 and 3 in pathologic amyloid formation by human immunoglobulin κ1 light chains.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. 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

3 authors.

Emily LewkowiczDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118, USA.
Shobini JayaramanDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118, USA.
Olga GurskyDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118, USA. Electronic address: gursky@bu.edu.

Funding

Structural Thermodynamics of Human Apolipoprotein C-1R01GM067260 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI GURSKY, OLGA · 2003 to 2024
$7.4M
TRAINING PROGRAM IN ENDOCRINE AND METABOLIC RESEARCHT32DK007201 · NIDDK · BOSTON UNIVERSITY MEDICAL CAMPUS · PI CORKEY, BARBARA E., KANDROR, KONSTANTIN V · 1986 to 2023
$6.4M
Structure and Function of Serum Amyloid A in Health and DiseaseR01GM135158 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI Olga Gursky · 2020 to 2026
$2.4M
NIDDK NIH HHS T32 DK007201NIGMS NIH HHS R01 GM067260NIGMS NIH HHS R01 GM135158
6 · The paper itself

Abstract

Recent advances in high-resolution structural studies of protein amyloids have revealed parallel in-register cross-β-sheets with periodic arrays of closely spaced identical residues. What do these structures tell us about the mechanisms of action of common amyloid-promoting factors, such as heparan sulfate (HS), nucleic acids, polyphosphates, anionic phospholipids, and acidic pH?

Indexed as

AmyloidAmyloidamyloid nucleationcross-β-sheetelectrostatic interactionsflexible dockingheparan sulfateperiodic polyanions

Identifiers

PMID34210544
PMCPMC8415129

What OpenQuestion holds

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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.