Evidence map›Paper›PMID 16515450›Full record

ReviewProtein and peptide letters2006

Solid-state NMR as a probe of amyloid structure.

Robert Tycko

Abstract readReview
In one paragraph

Review in Protein and peptide letters, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Multi-Target Actions of Acridones fromPharmaceuticals (Basel, Switzerland) · 2021
    Article
  2. Article
  3. Acetylation of AβACS chemical neuroscience · 2020
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. High-resolution solid-state NMR structure of a 17.6 kDa protein.Journal of the American Chemical Society · 2010
    Article
  9. Article
  10. 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

1 author.

Robert TyckoLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA. robertty@niddk.nih.gov

Funding

Development of Solid State NMR Methods and TechnologyZIADK029029 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TYCKO, ROBERT · 2009 to 2025
$9.6M
Structural Studies of Alzheimer's beta-Amyloid FibrilsZIADK029061 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TYCKO, ROBERT · 2009 to 2025
$8.4M
NEW SOLID STATE NMR METHODOLOGY FOR STRUCTURAL STUDIES OF BIOPOLYMERSZ01DK029029 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TYCKO, ROBERT · 1997 to 2008
$673k
Structural Studies of Alzheimer's beta-Amyloid FibrilsZ01DK029061 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TYCKO, ROBERT · 2007 to 2008
$671k
NIDDK NIH HHS Z01 DK029029-09
6 · The paper itself

Abstract

Solid state nuclear magnetic resonance (NMR) has developed into one of the most informative and direct experimental approaches to the characterization of the molecular structures of amyloid fibrils, including those associated with Alzheimer's disease. In this article, essential aspects of solid state NMR methods are described briefly and results obtained to date regarding the supramolecular organization of amyloid fibrils and the conformations of peptides within amyloid fibrils are reviewed.

Indexed as

Nuclear Magnetic Resonance, BiomolecularAmyloidHumansProtein ConformationAmyloid

Identifiers

PMID16515450
PMCPMC1467577

What OpenQuestion holds

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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.