Amyloid

"Amyloid" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease.

Descriptor ID	D000682
MeSH Number(s)	D05.500.049 D12.776.049
Concept/Terms	Amyloid Amyloid Amyloid Substance Substance, Amyloid Amyloid Fibrils Amyloid Fibrils Fibrils, Amyloid

Below are MeSH descriptors whose meaning is more general than "Amyloid".

Chemicals and Drugs [D]
Macromolecular Substances [D05]
Multiprotein Complexes [D05.500]
Amyloid [D05.500.049]
Amino Acids, Peptides, and Proteins [D12]
Proteins [D12.776]
Amyloid [D12.776.049]

Below are MeSH descriptors whose meaning is related to "Amyloid".

Below are MeSH descriptors whose meaning is more specific than "Amyloid".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Amyloid" by people in this website by year, and whether "Amyloid" was a major or minor topic of these publications.

Bar chart showing 32 publications over 19 distinct years, with a maximum of 3 publications in 2012

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
1991	1	1	2
1993	1	0	1
1997	2	0	2
2002	0	1	1
2003	1	1	2
2004	1	1	2
2005	1	1	2
2006	1	1	2
2007	2	0	2
2008	2	0	2
2009	1	1	2
2010	1	0	1
2011	1	0	1
2012	0	3	3
2013	1	0	1
2015	2	0	2
2016	1	0	1
2017	2	0	2
2019	1	0	1

Below are the most recent publications written about "Amyloid" by people in Profiles.

Sreenivasan S, Narayan M. Learnings from Protein Folding Projected onto Amyloid Misfolding. ACS Chem Neurosci. 2019 09 18; 10(9):3911-3913.

View in: PubMed
Rodriguez RA, Chen LY, Plascencia-Villa G, Perry G. Thermodynamics of Amyloid-ß Fibril Elongation: Atomistic Details of the Transition State. ACS Chem Neurosci. 2018 04 18; 9(4):783-789.

View in: PubMed
Rodriguez RA, Chen LY, Plascencia-Villa G, Perry G. Elongation affinity, activation barrier, and stability of Aß42 oligomers/fibrils in physiological saline. Biochem Biophys Res Commun. 2017 05 27; 487(2):444-449.

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Plascencia-Villa G, Ponce A, Collingwood JF, Arellano-Jiménez MJ, Zhu X, Rogers JT, Betancourt I, José-Yacamán M, Perry G. High-resolution analytical imaging and electron holography of magnetite particles in amyloid cores of Alzheimer's disease. Sci Rep. 2016 04 28; 6:24873.

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Hayden EY, Kaur P, Williams TL, Matsui H, Yeh SR, Rousseau DL. Heme Stabilization of a-Synuclein Oligomers during Amyloid Fibril Formation. Biochemistry. 2015 Aug 04; 54(30):4599-610.

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Torres L, Ortiz T, Tang Q. Enhancement of herpes simplex virus (HSV) infection by seminal plasma and semen amyloids implicates a new target for the prevention of HSV infection. Viruses. 2015 Apr 20; 7(4):2057-73.

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Hou L, Lee HG, Han F, Tedesco JM, Perry G, Smith MA, Zagorski MG. Modification of amyloid-ß1-42 fibril structure by methionine-35 oxidation. J Alzheimers Dis. 2013; 37(1):9-18.

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Babcock JJ, Brancaleon L. Bovine serum albumin oligomers in the E- and B-forms at low protein concentration and ionic strength. Int J Biol Macromol. 2013 Feb; 53:42-53.

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Buchman AS, Nag S, Shulman JM, Lim AS, VanderHorst VG, Leurgans SE, Schneider JA, Bennett DA. Locus coeruleus neuron density and parkinsonism in older adults without Parkinson's disease. Mov Disord. 2012 Nov; 27(13):1625-31.

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Poduslo JF, Howell KG, Olson NC, Ramirez-Alvarado M, Kandimalla KK. Alzheimer's disease amyloid ß-protein mutations and deletions that define neuronal binding/internalization as early stage nonfibrillar/fibrillar aggregates and late stage fibrils. Biochemistry. 2012 May 15; 51(19):3993-4003.

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