Exploring the sequence determinants of amyloid structure using position-specific scoring matrices (Q44106880)

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scientific article published on 14 February 2010

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English	Exploring the sequence determinants of amyloid structure using position-specific scoring matrices	scientific article published on 14 February 2010

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scholarly article

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

title

Exploring the sequence determinants of amyloid structure using position-specific scoring matrices (English)

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

corrigendum / erratum

Erratum: Corrigendum: Exploring the sequence determinants of amyloid structure using position-specific scoring matrices

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Crossref

DOI

10.1038/NMETH1010-855A

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12 July 2019

reference URL

http://api.crossref.org/works?select=update-to&filter=doi:10.1038/NMETH1010-855A

author

Louise Serpell

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9

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

Joost Schymkowitz

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11

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

Ivo C Martins

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Ivo Cristiano Martins

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5

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Joke Reumers

object named as

Joke Reumers

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6

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Alastair Copland

object named as

Alastair Copland

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8

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author name string

Sebastian Maurer-Stroh

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1

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

Maja Debulpaep

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2

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

Nico Kuemmerer

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3

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

Manuela Lopez de la Paz

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4

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

Kyle L Morris

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7

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

Luis Serrano

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10

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

Frederic Rousseau

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12

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

language of work or name

English

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publication date

14 February 2010

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

published in

Nature Methods

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

volume

7

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

issue

3

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

page(s)

237-242

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Europe PubMed Central

PubMed publication ID

20154676

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29 November 2017

cites work

Structural integrity of beta-sheet assembly

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Sequence determinants of bacterial amyloid formation

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Protein aggregation and amyloidosis: confusion of the kinds?

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Consensus prediction of amyloidogenic determinants in amyloid fibril-forming proteins.

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Sequence properties of GPI-anchored proteins near the omega-site: constraints for the polypeptide binding site of the putative transamidase

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Sequence determinants of amyloid fibril formation

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Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases

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Analysis of amino acid indices and mutation matrices for sequence comparison and structure prediction of proteins

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Atomic structures of amyloid cross-beta spines reveal varied steric zippers

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Huntingtin and mutant SOD1 form aggregate structures with distinct molecular properties in human cells

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Refinement and prediction of protein prenylation motifs

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A simple algorithm locates beta-strands in the amyloid fibril core of alpha-synuclein, Abeta, and tau using the amino acid sequence alone

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A striking quality control subcompartment in Saccharomyces cerevisiae: the endoplasmic reticulum-associated compartment

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Prediction of amyloidogenic and disordered regions in protein chains

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Molecular basis for amyloid fibril formation and stability

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Protein misfolding, functional amyloid, and human disease

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Misfolded proteins partition between two distinct quality control compartments

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Interaction-based evaluation of the propensity for amyloid formation with cross-beta structure

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Rationalization of the effects of mutations on peptide and protein aggregation rates.

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Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

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Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case

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https://pubmed.ncbi.nlm.nih.gov/20154676

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Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences

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Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

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Dissection and design of yeast prions

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Amyloid-like properties of bacterial inclusion bodies.

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Prediction of "hot spots" of aggregation in disease-linked polypeptides

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Kinetic partitioning of protein folding and aggregation.

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/20154676

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The PROSITE database.

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/20154676

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12 December 2020

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X-ray diffraction studies of amyloid structure

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CLEARER: a new tool for the analysis of X-ray fibre diffraction patterns and diffraction simulation from atomic structural models

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Identifiers

DOI

10.1038/NMETH.1432

1 reference

stated in

Europe PubMed Central

PubMed publication ID

20154676

retrieved

29 November 2017

PubMed publication ID

20154676

1 reference

stated in

Europe PubMed Central

PubMed publication ID

20154676

retrieved

29 November 2017

ResearchGate publication ID

41429071

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