StAmP-DB: A platform for structures of polymorphic amyloid fibril cores

Nikolaos Louros; Rob Van Der Kant; Joost Schymkowitz; Frederic Rousseau

doi:10.1093/bioinformatics/btac126

StAmP-DB: A platform for structures of polymorphic amyloid fibril cores

Nikolaos Louros, Rob Van Der Kant, Joost Schymkowitz, Frederic Rousseau

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

Amyloid polymorphism is emerging as a key property that is differentially linked to various conformational diseases, including major neurodegenerative disorders, but also as a feature that potentially relates to complex structural mechanisms mediating transmissibility barriers and selective vulnerability of amyloids. In response to the rapidly expanding number of amyloid fibril structures formed by full-length proteins, we here have developed StAmP-DB, a public database that supports the curation and cross-comparison of experimentally determined three-dimensional amyloid polymorph structures.

Original language	English (US)
Pages (from-to)	2636-2638
Number of pages	3
Journal	Bioinformatics
Volume	38
Issue number	9
DOIs	https://doi.org/10.1093/bioinformatics/btac126
State	Published - May 1 2022
Externally published	Yes

ASJC Scopus subject areas

Statistics and Probability
Biochemistry
Molecular Biology
Computer Science Applications
Computational Theory and Mathematics
Computational Mathematics

Access to Document

10.1093/bioinformatics/btac126

Cite this

@article{074ff1f064004bfca3b3a3bc348206a0,

title = "StAmP-DB: A platform for structures of polymorphic amyloid fibril cores",

abstract = "Amyloid polymorphism is emerging as a key property that is differentially linked to various conformational diseases, including major neurodegenerative disorders, but also as a feature that potentially relates to complex structural mechanisms mediating transmissibility barriers and selective vulnerability of amyloids. In response to the rapidly expanding number of amyloid fibril structures formed by full-length proteins, we here have developed StAmP-DB, a public database that supports the curation and cross-comparison of experimentally determined three-dimensional amyloid polymorph structures.",

author = "Nikolaos Louros and {Van Der Kant}, Rob and Joost Schymkowitz and Frederic Rousseau",

year = "2022",

month = may,

day = "1",

doi = "10.1093/bioinformatics/btac126",

language = "English (US)",

volume = "38",

pages = "2636--2638",

journal = "Bioinformatics",

issn = "1367-4803",

publisher = "Oxford University Press",

number = "9",

}

TY - JOUR

T1 - StAmP-DB

T2 - A platform for structures of polymorphic amyloid fibril cores

AU - Louros, Nikolaos

AU - Van Der Kant, Rob

AU - Schymkowitz, Joost

AU - Rousseau, Frederic

PY - 2022/5/1

Y1 - 2022/5/1

N2 - Amyloid polymorphism is emerging as a key property that is differentially linked to various conformational diseases, including major neurodegenerative disorders, but also as a feature that potentially relates to complex structural mechanisms mediating transmissibility barriers and selective vulnerability of amyloids. In response to the rapidly expanding number of amyloid fibril structures formed by full-length proteins, we here have developed StAmP-DB, a public database that supports the curation and cross-comparison of experimentally determined three-dimensional amyloid polymorph structures.

AB - Amyloid polymorphism is emerging as a key property that is differentially linked to various conformational diseases, including major neurodegenerative disorders, but also as a feature that potentially relates to complex structural mechanisms mediating transmissibility barriers and selective vulnerability of amyloids. In response to the rapidly expanding number of amyloid fibril structures formed by full-length proteins, we here have developed StAmP-DB, a public database that supports the curation and cross-comparison of experimentally determined three-dimensional amyloid polymorph structures.

UR - http://www.scopus.com/inward/record.url?scp=85132651090&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85132651090&partnerID=8YFLogxK

U2 - 10.1093/bioinformatics/btac126

DO - 10.1093/bioinformatics/btac126

M3 - Article

C2 - 35199146

AN - SCOPUS:85132651090

SN - 1367-4803

VL - 38

SP - 2636

EP - 2638

JO - Bioinformatics

JF - Bioinformatics

IS - 9

ER -

StAmP-DB: A platform for structures of polymorphic amyloid fibril cores

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this