Understanding the dynamics of monomeric, dimeric, and tetrameric α‐synuclein structures in water
Identifieur interne : 000149 ( Main/Exploration ); précédent : 000148; suivant : 000150Understanding the dynamics of monomeric, dimeric, and tetrameric α‐synuclein structures in water
Auteurs : Jonathan Y. Mane ; Maria StepanovaSource :
- FEBS Open Bio [ 2211-5463 ] ; 2016.
Abstract
Human α‐synuclein (αS) is an intrinsically disordered protein associated with Parkinson's disease. Molecular mechanisms of corruptive misfolding and aggregation of αS resulting in the disease, as well as the structure and other properties of the corresponding oligomers are not entirely understood yet, preventing the development of efficient therapies. In this study, we investigate the folding dynamics of initially unfolded hypothetical αS constructs in water using all‐atom molecular dynamics simulations. We also employ the novel essential collective dynamics method to analyze the results obtained from the simulations. Our comparative analysis of monomeric, dimeric, and tetrameric αS models reveals pronounced differences in their structure and stability, emphasizing the importance of small oligomers, particularly dimers, in the process of misfolding.
Url:
DOI: 10.1002/2211-5463.12069
PubMed: 27398307
PubMed Central: 4932447
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Pmc, to step Corpus: 000136
- to stream Pmc, to step Curation: 000136
- to stream Pmc, to step Checkpoint: 000038
- to stream Ncbi, to step Merge: 002022
- to stream Ncbi, to step Curation: 002022
- to stream Ncbi, to step Checkpoint: 002022
- to stream Main, to step Merge: 000149
- to stream Main, to step Curation: 000149
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Understanding the dynamics of monomeric, dimeric, and tetrameric α‐synuclein structures in water</title><author><name sortKey="Mane, Jonathan Y" sort="Mane, Jonathan Y" uniqKey="Mane J" first="Jonathan Y." last="Mane">Jonathan Y. Mane</name><affiliation><nlm:aff id="feb412069-aff-0001"></nlm:aff></affiliation><affiliation><nlm:aff id="feb412069-aff-0002"></nlm:aff></affiliation></author><author><name sortKey="Stepanova, Maria" sort="Stepanova, Maria" uniqKey="Stepanova M" first="Maria" last="Stepanova">Maria Stepanova</name><affiliation><nlm:aff id="feb412069-aff-0001"></nlm:aff></affiliation><affiliation><nlm:aff id="feb412069-aff-0002"></nlm:aff></affiliation><affiliation><nlm:aff id="feb412069-aff-0003"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">27398307</idno><idno type="pmc">4932447</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4932447</idno><idno type="RBID">PMC:4932447</idno><idno type="doi">10.1002/2211-5463.12069</idno><date when="2016">2016</date><idno type="wicri:Area/Pmc/Corpus">000136</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000136</idno><idno type="wicri:Area/Pmc/Curation">000136</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000136</idno><idno type="wicri:Area/Pmc/Checkpoint">000038</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000038</idno><idno type="wicri:Area/Ncbi/Merge">002022</idno><idno type="wicri:Area/Ncbi/Curation">002022</idno><idno type="wicri:Area/Ncbi/Checkpoint">002022</idno><idno type="wicri:Area/Main/Merge">000149</idno><idno type="wicri:Area/Main/Curation">000149</idno><idno type="wicri:Area/Main/Exploration">000149</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Understanding the dynamics of monomeric, dimeric, and tetrameric α‐synuclein structures in water</title><author><name sortKey="Mane, Jonathan Y" sort="Mane, Jonathan Y" uniqKey="Mane J" first="Jonathan Y." last="Mane">Jonathan Y. Mane</name><affiliation><nlm:aff id="feb412069-aff-0001"></nlm:aff></affiliation><affiliation><nlm:aff id="feb412069-aff-0002"></nlm:aff></affiliation></author><author><name sortKey="Stepanova, Maria" sort="Stepanova, Maria" uniqKey="Stepanova M" first="Maria" last="Stepanova">Maria Stepanova</name><affiliation><nlm:aff id="feb412069-aff-0001"></nlm:aff></affiliation><affiliation><nlm:aff id="feb412069-aff-0002"></nlm:aff></affiliation><affiliation><nlm:aff id="feb412069-aff-0003"></nlm:aff></affiliation></author></analytic><series><title level="j">FEBS Open Bio</title><idno type="eISSN">2211-5463</idno><imprint><date when="2016">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Human α‐synuclein (αS) is an intrinsically disordered protein associated with Parkinson's disease. Molecular mechanisms of corruptive misfolding and aggregation of αS resulting in the disease, as well as the structure and other properties of the corresponding oligomers are not entirely understood yet, preventing the development of efficient therapies. In this study, we investigate the folding dynamics of initially unfolded hypothetical αS constructs in water using all‐atom molecular dynamics simulations. We also employ the novel essential collective dynamics method to analyze the results obtained from the simulations. Our comparative analysis of monomeric, dimeric, and tetrameric αS models reveals pronounced differences in their structure and stability, emphasizing the importance of small oligomers, particularly dimers, in the process of misfolding.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Pullman, B" uniqKey="Pullman B">B Pullman</name></author></analytic></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct></listBibl></div1></back></TEI><affiliations><list></list><tree><noCountry><name sortKey="Mane, Jonathan Y" sort="Mane, Jonathan Y" uniqKey="Mane J" first="Jonathan Y." last="Mane">Jonathan Y. Mane</name><name sortKey="Stepanova, Maria" sort="Stepanova, Maria" uniqKey="Stepanova M" first="Maria" last="Stepanova">Maria Stepanova</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Canada/explor/ParkinsonCanadaV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000149 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000149 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Canada
|area= ParkinsonCanadaV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= PMC:4932447
|texte= Understanding the dynamics of monomeric, dimeric, and tetrameric α‐synuclein structures in water
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:27398307" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a ParkinsonCanadaV1
| This area was generated with Dilib version V0.6.29. |  |