Evidence map›Paper›PMID 18487849›Full record

ReviewJournal of Alzheimer's disease : JAD2008

Amyloids: friend or foe?

Neal D Hammer, Xuan Wang, Bryan A McGuffie, Matthew R Chapman

Abstract readReview
In one paragraph

Review in Journal of Alzheimer's disease : JAD, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

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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

4 authors.

Neal D HammerDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109-0620, USA.
Xuan Wang
Bryan A McGuffie
Matthew R Chapman

Funding

Assembly of Curli Fibers by Escherichia coliR01AI073847 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHAPMAN, MATTHEW RICHARD · 2007 to 2011
$1.8M
Curli Fiber Assembly and FunctionR56AI073847 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHAPMAN, MATTHEW RICHARD · 2013 to 2013
$352k
NIAID NIH HHS AI073847-01NIAID NIH HHS R01 AI073847NIAID NIH HHS R56 AI073847PHS HHS P50-A608671
6 · The paper itself

Abstract

Amyloidogenesis is the aggregation of soluble proteins into structurally conserved fibers. Amyloid fibers are distinguished by their resistance to proteinase K, tinctorial properties and beta-sheet-rich secondary structure. Amyloid formation is a hallmark of many human diseases including Alzheimer's, Huntington's and the prion diseases. Therefore, understanding amyloidogenesis will provide insights into the development of therapeutics that target these debilitating diseases. A new class of ;functional' amyloids promises a unique glimpse at how nature has harnessed the amyloid fiber to accomplish important physiological tasks. Functional amyloids are produced by organisms spanning all aspects of cellular life. Herein we review amyloidogenesis, with special attention focused on the similarities and differences between the best characterized disease-associated amyloidogenic protein amyloid-beta and the formation of several functional amyloids. The implications of studying functional amyloidogenesis and the strategies organisms employ to limit exposure to toxic intermediates will also be discussed.

Indexed as

AmyloidAnti-Bacterial AgentsBacterial ProteinsBacteriocinsEscherichia coli Proteinsgp100 Melanoma AntigenHumansMembrane GlycoproteinsNeurodegenerative DiseasesAmyloidAnti-Bacterial AgentsBacterial ProteinsBacteriocinsCrl protein, BacteriacsgA protein, E coliEscherichia coli Proteinsgp100 Melanoma AntigenMembrane GlycoproteinsmicrocinPMEL protein, human

Identifiers

PMID18487849
PMCPMC2674399

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.