Evidence map›Paper›PMID 27479186›Full record

ArticleProtein science : a publication of the Protein Society2016

The dye SYPRO orange binds to amylin amyloid fibrils but not pre-fibrillar intermediates.

Amy G Wong, Daniel P Raleigh

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 32% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
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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 at 1 institution in 1 country.

Amy G WongDepartment of Chemistry, Stony Brook University, Stony Brook, New York, 11794-3400.
Daniel P RaleighDepartment of Chemistry, Stony Brook University, Stony Brook, New York, 11794-3400. daniel.raleigh@stonybrook.edu.
Stony Brook University · US

Funding

Biophysical Studies of Amyloid Formation by Polypeptide HormonesR01GM078114 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI RALEIGH, DANIEL P · 2008 to 2024
$5.1M
NIGMS NIH HHS R01 GM078114
6 · The paper itself

Abstract

Amyloid deposition underlies a broad range of diseases including multiple neurodegenerative diseases, systemic amyloidosis and type-2 diabetes. Amyloid sensitive dyes, particularly thioflavin-T, are widely used to detect ex-vivo amyloid deposits, to monitor amyloid formation in vitro and to follow the kinetics of amyloid self-assembly. We show that the dye SYPRO-orange binds to amyloid fibrils formed by human amylin, the polypeptide responsible for islet amyloid formation in type-2 diabetes. No fluorescence enhancement is observed in the presence of pre-fibrillar species or in the presence of non-amyloidogenic rat amylin. The kinetics of human amylin amyloid formation can be monitored by SYPRO-orange fluorescence and match the time course determined with thioflavin-T assays. Thus, SYPRO-orange offers an alternative to thioflavin-T assays of amylin amyloid formation. The implications for the interpretation of SYPRO-orange-based assays of protein stability and protein-ligand interactions are discussed.

Indexed as

AmyloidBenzothiazolesFluorescent DyesHumansIslet Amyloid PolypeptideKineticsThiazolesAmyloidBenzothiazolesFluorescent DyesIslet Amyloid PolypeptideThiazolesthioflavin Tamylinamyloidislet amyloid polypeptideSYPRO-orangethioflavin-T

Identifiers

PMID27479186
PMCPMC5029533
OpenAlexW2489435651

What OpenQuestion holds

Textmetadata
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.