Global, in situ analysis of the structural proteome in individuals with Parkinson’s disease to identify a new class of biomarker
Parkinson’s disease (PD) is a prevalent neurodegenerative disease for which robust biomarkers are needed. Because protein structure reflects function, we tested whether global, in situ analysis of protein structural changes provides insight into PD pathophysiology and could inform a new concept of s...
Gespeichert in:
| Veröffentlicht in: | Nature structural & molecular biology 2022-10, Vol.29 (10), p.978-989 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 989 |
|---|---|
| container_issue | 10 |
| container_start_page | 978 |
| container_title | Nature structural & molecular biology |
| container_volume | 29 |
| creator | Mackmull, Marie-Therese Nagel, Luise Sesterhenn, Fabian Muntel, Jan Grossbach, Jan Stalder, Patrick Bruderer, Roland Reiter, Lukas van de Berg, Wilma D. J. de Souza, Natalie Beyer, Andreas Picotti, Paola |
| description | Parkinson’s disease (PD) is a prevalent neurodegenerative disease for which robust biomarkers are needed. Because protein structure reflects function, we tested whether global, in situ analysis of protein structural changes provides insight into PD pathophysiology and could inform a new concept of structural disease biomarkers. Using limited proteolysis–mass spectrometry (LiP–MS), we identified 76 structurally altered proteins in cerebrospinal fluid (CSF) of individuals with PD relative to healthy donors. These proteins were enriched in processes misregulated in PD, and some proteins also showed structural changes in PD brain samples. CSF protein structural information outperformed abundance information in discriminating between healthy participants and those with PD and improved the discriminatory performance of CSF measures of the hallmark PD protein α-synuclein. We also present the first analysis of inter-individual variability of a structural proteome in healthy individuals, identifying biophysical features of variable protein regions. Although independent validation is needed, our data suggest that global analyses of the human structural proteome will guide the development of novel structural biomarkers of disease and enable hypothesis generation about underlying disease processes.
This study identifies protein structural changes in cerebrospinal fluid of people with Parkinson’s disease relative to healthy individuals and proposes the concept of structural disease biomarkers. It also analyzes proteome structural variability in healthy people. |
| doi_str_mv | 10.1038/s41594-022-00837-0 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2724584241</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2724584241</sourcerecordid><originalsourceid>FETCH-LOGICAL-c375t-8fb258a9a0610df8de348e04d1cdf629c34fbd61620929547d4e6bbddc617b43</originalsourceid><addsrcrecordid>eNp9kc1qFjEUhoMotlZvwIUE3LhwNP-TWUrRKhR00X3ITM7Y1PmSmpOxfDvxLrw9r8S0Uyu4cJVAnvcN5zyEPOXsFWfSvkbF9aA6JkTHmJV9x-6RQ66V7obB6vt390EekEeIF4wJrXv5kBxII4SSvT0kP06WPPrlJY2JYqwr9ckve4xI80zrOVCsZZ3qWvxCL0uukHdwzcYU4rcYVr8gvYr1nH7y5UtMmNOv7z-RhojgEWjNNAZINc576mmCKzotHm_Kx5h3LQPlMXkwtxp4cnsekbN3b8-O33enH08-HL857SbZ69rZeRTa-sEzw1mYbQCpLDAV-BRmI4ZJqnkMhhvBBjFo1QcFZhxDmAzvRyWPyIutto3xdQWsbhdxgmXxCfKKTvRCaauE4g19_g96kdfSFrNR_WCM0I0SGzWVjFhgdpcltpH2jjN3LchtglwT5G4EOdZCz26r13EH4S7yx0gD5AZge0qfofz9-z-1vwGf8J4O</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2724796625</pqid></control><display><type>article</type><title>Global, in situ analysis of the structural proteome in individuals with Parkinson’s disease to identify a new class of biomarker</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><source>Nature</source><creator>Mackmull, Marie-Therese ; Nagel, Luise ; Sesterhenn, Fabian ; Muntel, Jan ; Grossbach, Jan ; Stalder, Patrick ; Bruderer, Roland ; Reiter, Lukas ; van de Berg, Wilma D. J. ; de Souza, Natalie ; Beyer, Andreas ; Picotti, Paola</creator><creatorcontrib>Mackmull, Marie-Therese ; Nagel, Luise ; Sesterhenn, Fabian ; Muntel, Jan ; Grossbach, Jan ; Stalder, Patrick ; Bruderer, Roland ; Reiter, Lukas ; van de Berg, Wilma D. J. ; de Souza, Natalie ; Beyer, Andreas ; Picotti, Paola</creatorcontrib><description>Parkinson’s disease (PD) is a prevalent neurodegenerative disease for which robust biomarkers are needed. Because protein structure reflects function, we tested whether global, in situ analysis of protein structural changes provides insight into PD pathophysiology and could inform a new concept of structural disease biomarkers. Using limited proteolysis–mass spectrometry (LiP–MS), we identified 76 structurally altered proteins in cerebrospinal fluid (CSF) of individuals with PD relative to healthy donors. These proteins were enriched in processes misregulated in PD, and some proteins also showed structural changes in PD brain samples. CSF protein structural information outperformed abundance information in discriminating between healthy participants and those with PD and improved the discriminatory performance of CSF measures of the hallmark PD protein α-synuclein. We also present the first analysis of inter-individual variability of a structural proteome in healthy individuals, identifying biophysical features of variable protein regions. Although independent validation is needed, our data suggest that global analyses of the human structural proteome will guide the development of novel structural biomarkers of disease and enable hypothesis generation about underlying disease processes.
This study identifies protein structural changes in cerebrospinal fluid of people with Parkinson’s disease relative to healthy individuals and proposes the concept of structural disease biomarkers. It also analyzes proteome structural variability in healthy people.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/s41594-022-00837-0</identifier><identifier>PMID: 36224378</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>101/58 ; 631/337/475 ; 631/80/470/2284 ; 692/699 ; 82/58 ; alpha-Synuclein - metabolism ; Biochemistry ; Biological Microscopy ; Biomarkers ; Biomedical and Life Sciences ; Cerebrospinal fluid ; Humans ; Life Sciences ; Mass spectrometry ; Mass spectroscopy ; Membrane Biology ; Movement disorders ; Neurodegenerative Diseases ; Parkinson Disease ; Parkinson's disease ; Protein Structure ; Proteins ; Proteolysis ; Proteome - metabolism ; Proteomes ; Structure-function relationships ; Synuclein ; Variability</subject><ispartof>Nature structural & molecular biology, 2022-10, Vol.29 (10), p.978-989</ispartof><rights>The Author(s), under exclusive licence to Springer Nature America, Inc. 2022. Springer Nature or its licensor holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2022. The Author(s), under exclusive licence to Springer Nature America, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-8fb258a9a0610df8de348e04d1cdf629c34fbd61620929547d4e6bbddc617b43</citedby><cites>FETCH-LOGICAL-c375t-8fb258a9a0610df8de348e04d1cdf629c34fbd61620929547d4e6bbddc617b43</cites><orcidid>0000-0002-9394-5665 ; 0000-0003-2928-1144 ; 0000-0002-4109-3552 ; 0000-0002-3891-2123 ; 0000-0003-2320-5829</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/s41594-022-00837-0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/s41594-022-00837-0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36224378$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mackmull, Marie-Therese</creatorcontrib><creatorcontrib>Nagel, Luise</creatorcontrib><creatorcontrib>Sesterhenn, Fabian</creatorcontrib><creatorcontrib>Muntel, Jan</creatorcontrib><creatorcontrib>Grossbach, Jan</creatorcontrib><creatorcontrib>Stalder, Patrick</creatorcontrib><creatorcontrib>Bruderer, Roland</creatorcontrib><creatorcontrib>Reiter, Lukas</creatorcontrib><creatorcontrib>van de Berg, Wilma D. J.</creatorcontrib><creatorcontrib>de Souza, Natalie</creatorcontrib><creatorcontrib>Beyer, Andreas</creatorcontrib><creatorcontrib>Picotti, Paola</creatorcontrib><title>Global, in situ analysis of the structural proteome in individuals with Parkinson’s disease to identify a new class of biomarker</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>Parkinson’s disease (PD) is a prevalent neurodegenerative disease for which robust biomarkers are needed. Because protein structure reflects function, we tested whether global, in situ analysis of protein structural changes provides insight into PD pathophysiology and could inform a new concept of structural disease biomarkers. Using limited proteolysis–mass spectrometry (LiP–MS), we identified 76 structurally altered proteins in cerebrospinal fluid (CSF) of individuals with PD relative to healthy donors. These proteins were enriched in processes misregulated in PD, and some proteins also showed structural changes in PD brain samples. CSF protein structural information outperformed abundance information in discriminating between healthy participants and those with PD and improved the discriminatory performance of CSF measures of the hallmark PD protein α-synuclein. We also present the first analysis of inter-individual variability of a structural proteome in healthy individuals, identifying biophysical features of variable protein regions. Although independent validation is needed, our data suggest that global analyses of the human structural proteome will guide the development of novel structural biomarkers of disease and enable hypothesis generation about underlying disease processes.
This study identifies protein structural changes in cerebrospinal fluid of people with Parkinson’s disease relative to healthy individuals and proposes the concept of structural disease biomarkers. It also analyzes proteome structural variability in healthy people.</description><subject>101/58</subject><subject>631/337/475</subject><subject>631/80/470/2284</subject><subject>692/699</subject><subject>82/58</subject><subject>alpha-Synuclein - metabolism</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomarkers</subject><subject>Biomedical and Life Sciences</subject><subject>Cerebrospinal fluid</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Membrane Biology</subject><subject>Movement disorders</subject><subject>Neurodegenerative Diseases</subject><subject>Parkinson Disease</subject><subject>Parkinson's disease</subject><subject>Protein Structure</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Proteome - metabolism</subject><subject>Proteomes</subject><subject>Structure-function relationships</subject><subject>Synuclein</subject><subject>Variability</subject><issn>1545-9993</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kc1qFjEUhoMotlZvwIUE3LhwNP-TWUrRKhR00X3ITM7Y1PmSmpOxfDvxLrw9r8S0Uyu4cJVAnvcN5zyEPOXsFWfSvkbF9aA6JkTHmJV9x-6RQ66V7obB6vt390EekEeIF4wJrXv5kBxII4SSvT0kP06WPPrlJY2JYqwr9ckve4xI80zrOVCsZZ3qWvxCL0uukHdwzcYU4rcYVr8gvYr1nH7y5UtMmNOv7z-RhojgEWjNNAZINc576mmCKzotHm_Kx5h3LQPlMXkwtxp4cnsekbN3b8-O33enH08-HL857SbZ69rZeRTa-sEzw1mYbQCpLDAV-BRmI4ZJqnkMhhvBBjFo1QcFZhxDmAzvRyWPyIutto3xdQWsbhdxgmXxCfKKTvRCaauE4g19_g96kdfSFrNR_WCM0I0SGzWVjFhgdpcltpH2jjN3LchtglwT5G4EOdZCz26r13EH4S7yx0gD5AZge0qfofz9-z-1vwGf8J4O</recordid><startdate>20221001</startdate><enddate>20221001</enddate><creator>Mackmull, Marie-Therese</creator><creator>Nagel, Luise</creator><creator>Sesterhenn, Fabian</creator><creator>Muntel, Jan</creator><creator>Grossbach, Jan</creator><creator>Stalder, Patrick</creator><creator>Bruderer, Roland</creator><creator>Reiter, Lukas</creator><creator>van de Berg, Wilma D. J.</creator><creator>de Souza, Natalie</creator><creator>Beyer, Andreas</creator><creator>Picotti, Paola</creator><general>Nature Publishing Group US</general><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PADUT</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-9394-5665</orcidid><orcidid>https://orcid.org/0000-0003-2928-1144</orcidid><orcidid>https://orcid.org/0000-0002-4109-3552</orcidid><orcidid>https://orcid.org/0000-0002-3891-2123</orcidid><orcidid>https://orcid.org/0000-0003-2320-5829</orcidid></search><sort><creationdate>20221001</creationdate><title>Global, in situ analysis of the structural proteome in individuals with Parkinson’s disease to identify a new class of biomarker</title><author>Mackmull, Marie-Therese ; Nagel, Luise ; Sesterhenn, Fabian ; Muntel, Jan ; Grossbach, Jan ; Stalder, Patrick ; Bruderer, Roland ; Reiter, Lukas ; van de Berg, Wilma D. J. ; de Souza, Natalie ; Beyer, Andreas ; Picotti, Paola</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-8fb258a9a0610df8de348e04d1cdf629c34fbd61620929547d4e6bbddc617b43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>101/58</topic><topic>631/337/475</topic><topic>631/80/470/2284</topic><topic>692/699</topic><topic>82/58</topic><topic>alpha-Synuclein - metabolism</topic><topic>Biochemistry</topic><topic>Biological Microscopy</topic><topic>Biomarkers</topic><topic>Biomedical and Life Sciences</topic><topic>Cerebrospinal fluid</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Membrane Biology</topic><topic>Movement disorders</topic><topic>Neurodegenerative Diseases</topic><topic>Parkinson Disease</topic><topic>Parkinson's disease</topic><topic>Protein Structure</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Proteome - metabolism</topic><topic>Proteomes</topic><topic>Structure-function relationships</topic><topic>Synuclein</topic><topic>Variability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mackmull, Marie-Therese</creatorcontrib><creatorcontrib>Nagel, Luise</creatorcontrib><creatorcontrib>Sesterhenn, Fabian</creatorcontrib><creatorcontrib>Muntel, Jan</creatorcontrib><creatorcontrib>Grossbach, Jan</creatorcontrib><creatorcontrib>Stalder, Patrick</creatorcontrib><creatorcontrib>Bruderer, Roland</creatorcontrib><creatorcontrib>Reiter, Lukas</creatorcontrib><creatorcontrib>van de Berg, Wilma D. J.</creatorcontrib><creatorcontrib>de Souza, Natalie</creatorcontrib><creatorcontrib>Beyer, Andreas</creatorcontrib><creatorcontrib>Picotti, Paola</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest_Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Research Library China</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature structural & molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mackmull, Marie-Therese</au><au>Nagel, Luise</au><au>Sesterhenn, Fabian</au><au>Muntel, Jan</au><au>Grossbach, Jan</au><au>Stalder, Patrick</au><au>Bruderer, Roland</au><au>Reiter, Lukas</au><au>van de Berg, Wilma D. J.</au><au>de Souza, Natalie</au><au>Beyer, Andreas</au><au>Picotti, Paola</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Global, in situ analysis of the structural proteome in individuals with Parkinson’s disease to identify a new class of biomarker</atitle><jtitle>Nature structural & molecular biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2022-10-01</date><risdate>2022</risdate><volume>29</volume><issue>10</issue><spage>978</spage><epage>989</epage><pages>978-989</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Parkinson’s disease (PD) is a prevalent neurodegenerative disease for which robust biomarkers are needed. Because protein structure reflects function, we tested whether global, in situ analysis of protein structural changes provides insight into PD pathophysiology and could inform a new concept of structural disease biomarkers. Using limited proteolysis–mass spectrometry (LiP–MS), we identified 76 structurally altered proteins in cerebrospinal fluid (CSF) of individuals with PD relative to healthy donors. These proteins were enriched in processes misregulated in PD, and some proteins also showed structural changes in PD brain samples. CSF protein structural information outperformed abundance information in discriminating between healthy participants and those with PD and improved the discriminatory performance of CSF measures of the hallmark PD protein α-synuclein. We also present the first analysis of inter-individual variability of a structural proteome in healthy individuals, identifying biophysical features of variable protein regions. Although independent validation is needed, our data suggest that global analyses of the human structural proteome will guide the development of novel structural biomarkers of disease and enable hypothesis generation about underlying disease processes.
This study identifies protein structural changes in cerebrospinal fluid of people with Parkinson’s disease relative to healthy individuals and proposes the concept of structural disease biomarkers. It also analyzes proteome structural variability in healthy people.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>36224378</pmid><doi>10.1038/s41594-022-00837-0</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-9394-5665</orcidid><orcidid>https://orcid.org/0000-0003-2928-1144</orcidid><orcidid>https://orcid.org/0000-0002-4109-3552</orcidid><orcidid>https://orcid.org/0000-0002-3891-2123</orcidid><orcidid>https://orcid.org/0000-0003-2320-5829</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1545-9993 |
| ispartof | Nature structural & molecular biology, 2022-10, Vol.29 (10), p.978-989 |
| issn | 1545-9993 1545-9985 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2724584241 |
| source | MEDLINE; Springer Nature - Complete Springer Journals; Nature |
| subjects | 101/58 631/337/475 631/80/470/2284 692/699 82/58 alpha-Synuclein - metabolism Biochemistry Biological Microscopy Biomarkers Biomedical and Life Sciences Cerebrospinal fluid Humans Life Sciences Mass spectrometry Mass spectroscopy Membrane Biology Movement disorders Neurodegenerative Diseases Parkinson Disease Parkinson's disease Protein Structure Proteins Proteolysis Proteome - metabolism Proteomes Structure-function relationships Synuclein Variability |
| title | Global, in situ analysis of the structural proteome in individuals with Parkinson’s disease to identify a new class of biomarker |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T15%3A08%3A04IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Global,%20in%20situ%20analysis%20of%20the%20structural%20proteome%20in%20individuals%20with%20Parkinson%E2%80%99s%20disease%20to%20identify%20a%20new%20class%20of%20biomarker&rft.jtitle=Nature%20structural%20&%20molecular%20biology&rft.au=Mackmull,%20Marie-Therese&rft.date=2022-10-01&rft.volume=29&rft.issue=10&rft.spage=978&rft.epage=989&rft.pages=978-989&rft.issn=1545-9993&rft.eissn=1545-9985&rft_id=info:doi/10.1038/s41594-022-00837-0&rft_dat=%3Cproquest_cross%3E2724584241%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2724796625&rft_id=info:pmid/36224378&rfr_iscdi=true |