Loading…
Proteomic Profiling of Antimalarial Plasmodione Using 3‐Benz(o)ylmenadione Affinity‐Based Probes
Understanding the mechanisms of drug action in malarial parasites is crucial for the development of new drugs to combat infection and to counteract drug resistance. Proteomics is a widely used approach to study host‐pathogen systems and to identify drug protein targets. Plasmodione is an antiplasmod...
Saved in:
| Published in: | Chembiochem : a European journal of chemical biology 2024-08, Vol.25 (15), p.e202400187-n/a |
|---|---|
| Main Authors: | , , , , , , , , , , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | |
|---|---|
| cites | cdi_FETCH-LOGICAL-c2987-c27d73544d44d217818c4ed1d7357a84b8790a10607db32a18e9a8bd607ae95e3 |
| container_end_page | n/a |
| container_issue | 15 |
| container_start_page | e202400187 |
| container_title | Chembiochem : a European journal of chemical biology |
| container_volume | 25 |
| creator | Iacobucci, Ilaria Monaco, Vittoria Hovasse, Agnès Dupouy, Baptiste Keumoe, Rodrigue Cichocki, Bogdan Elhabiri, Mourad Meunier, Brigitte Strub, Jean‐Marc Monti, Maria Cianférani, Sarah Blandin, Stéphanie A. Schaeffer‐Reiss, Christine Davioud‐Charvet, Elisabeth |
| description | Understanding the mechanisms of drug action in malarial parasites is crucial for the development of new drugs to combat infection and to counteract drug resistance. Proteomics is a widely used approach to study host‐pathogen systems and to identify drug protein targets. Plasmodione is an antiplasmodial early‐lead drug exerting potent activities against young asexual and sexual blood stages in vitro with low toxicity to host cells. To elucidate its molecular mechanisms, an affinity‐based protein profiling (AfBPP) approach was applied to yeast and P. falciparum proteomes. New (pro‐) AfBPP probes based on the 3‐benz(o)yl‐6‐fluoro‐menadione scaffold were synthesized. With optimized conditions of both photoaffinity labeling and click reaction steps, the AfBPP protocol was then applied to a yeast proteome, yielding 11 putative drug‐protein targets. Among these, we found four proteins associated with oxidoreductase activities, the hypothesized type of targets for plasmodione and its metabolites, and other proteins associated with the mitochondria. In Plasmodium parasites, the MS analysis revealed 44 potential plasmodione targets that need to be validated in further studies. Finally, the localization of a 3‐benzyl‐6‐fluoromenadione AfBPP probe was studied in the subcellular structures of the parasite at the trophozoite stage.
We describe here the design, synthesis and evaluation of an antiplasmodial 3‐benzyl‐6‐fluoro‐menadione probe for affinity‐based protein profiling experiments using yeast and P. falciparum parasite lysates. These studies allowed us to identify a first list of proteins interacting with plasmodione in both yeast and P. falciparum late trophozoites. |
| doi_str_mv | 10.1002/cbic.202400187 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_3043073930</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3043073930</sourcerecordid><originalsourceid>FETCH-LOGICAL-c2987-c27d73544d44d217818c4ed1d7357a84b8790a10607db32a18e9a8bd607ae95e3</originalsourceid><addsrcrecordid>eNqFkMtKAzEUhoMotla3LmXATV205jIzSZZt8VIo2IVdD5nJGUnJTOqkRerKR_AZfRIztFZwI4TkJOc7P-FD6JLgIcGY3ha5KYYU0xhjIvgR6pKYyQFPGTve1zGlvIPOvF9ijGXKyCnqMJEySQntIj1v3BpcZYooVKWxpn6JXBmN6rWplFWNUTaaW-Urp42rIVr4lmBfH59jqN_77mZrK6jVrjkqS1Ob9bbtKg-6zczBn6OTUlkPF_uzhxb3d8-Tx8Hs6WE6Gc0GBZWCh51rzpI41mFRwgURRQyatI9ciTgXXGJFcIq5zhlVRIBUItfhrkAmwHqov8tdNe51A36dVcYXYK2qwW18xnDMMGeS4YBe_0GXbtPU4XeBEpzIRPIkUMMdVTTO-wbKbNUELc02Izhr_Wet_-zgPwxc7WM3eQX6gP8ID4DcAW_GwvafuGwynk5-w78BbBCSfQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>3087195975</pqid></control><display><type>article</type><title>Proteomic Profiling of Antimalarial Plasmodione Using 3‐Benz(o)ylmenadione Affinity‐Based Probes</title><source>Wiley Online Library</source><creator>Iacobucci, Ilaria ; Monaco, Vittoria ; Hovasse, Agnès ; Dupouy, Baptiste ; Keumoe, Rodrigue ; Cichocki, Bogdan ; Elhabiri, Mourad ; Meunier, Brigitte ; Strub, Jean‐Marc ; Monti, Maria ; Cianférani, Sarah ; Blandin, Stéphanie A. ; Schaeffer‐Reiss, Christine ; Davioud‐Charvet, Elisabeth</creator><creatorcontrib>Iacobucci, Ilaria ; Monaco, Vittoria ; Hovasse, Agnès ; Dupouy, Baptiste ; Keumoe, Rodrigue ; Cichocki, Bogdan ; Elhabiri, Mourad ; Meunier, Brigitte ; Strub, Jean‐Marc ; Monti, Maria ; Cianférani, Sarah ; Blandin, Stéphanie A. ; Schaeffer‐Reiss, Christine ; Davioud‐Charvet, Elisabeth</creatorcontrib><description>Understanding the mechanisms of drug action in malarial parasites is crucial for the development of new drugs to combat infection and to counteract drug resistance. Proteomics is a widely used approach to study host‐pathogen systems and to identify drug protein targets. Plasmodione is an antiplasmodial early‐lead drug exerting potent activities against young asexual and sexual blood stages in vitro with low toxicity to host cells. To elucidate its molecular mechanisms, an affinity‐based protein profiling (AfBPP) approach was applied to yeast and P. falciparum proteomes. New (pro‐) AfBPP probes based on the 3‐benz(o)yl‐6‐fluoro‐menadione scaffold were synthesized. With optimized conditions of both photoaffinity labeling and click reaction steps, the AfBPP protocol was then applied to a yeast proteome, yielding 11 putative drug‐protein targets. Among these, we found four proteins associated with oxidoreductase activities, the hypothesized type of targets for plasmodione and its metabolites, and other proteins associated with the mitochondria. In Plasmodium parasites, the MS analysis revealed 44 potential plasmodione targets that need to be validated in further studies. Finally, the localization of a 3‐benzyl‐6‐fluoromenadione AfBPP probe was studied in the subcellular structures of the parasite at the trophozoite stage.
We describe here the design, synthesis and evaluation of an antiplasmodial 3‐benzyl‐6‐fluoro‐menadione probe for affinity‐based protein profiling experiments using yeast and P. falciparum parasite lysates. These studies allowed us to identify a first list of proteins interacting with plasmodione in both yeast and P. falciparum late trophozoites.</description><identifier>ISSN: 1439-4227</identifier><identifier>ISSN: 1439-7633</identifier><identifier>EISSN: 1439-7633</identifier><identifier>DOI: 10.1002/cbic.202400187</identifier><identifier>PMID: 38639212</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Activity-Based Protein Profiling ; Affinity ; Antiprotozoal agents ; Biological Chemistry and Chemical Biology ; Blood parasites ; Chemical synthesis ; Drug development ; Drug resistance ; Localization ; Menadione ; Metabolites ; Molecular modelling ; Oxidoreductase ; Parasite resistance ; Parasites ; Photoaffinity Labeling ; Probes ; Proteins ; Proteomes ; Proteomics ; Toxicity ; Yeast ; Yeasts</subject><ispartof>Chembiochem : a European journal of chemical biology, 2024-08, Vol.25 (15), p.e202400187-n/a</ispartof><rights>2024 The Author(s). ChemBioChem published by Wiley-VCH GmbH</rights><rights>2024 The Author(s). ChemBioChem published by Wiley-VCH GmbH.</rights><rights>2024. This article is published under http://creativecommons.org/licenses/by-nc/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c2987-c27d73544d44d217818c4ed1d7357a84b8790a10607db32a18e9a8bd607ae95e3</cites><orcidid>0000-0001-7026-4034</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fcbic.202400187$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fcbic.202400187$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>315,786,790,27957,27958,50923,51032</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38639212$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Iacobucci, Ilaria</creatorcontrib><creatorcontrib>Monaco, Vittoria</creatorcontrib><creatorcontrib>Hovasse, Agnès</creatorcontrib><creatorcontrib>Dupouy, Baptiste</creatorcontrib><creatorcontrib>Keumoe, Rodrigue</creatorcontrib><creatorcontrib>Cichocki, Bogdan</creatorcontrib><creatorcontrib>Elhabiri, Mourad</creatorcontrib><creatorcontrib>Meunier, Brigitte</creatorcontrib><creatorcontrib>Strub, Jean‐Marc</creatorcontrib><creatorcontrib>Monti, Maria</creatorcontrib><creatorcontrib>Cianférani, Sarah</creatorcontrib><creatorcontrib>Blandin, Stéphanie A.</creatorcontrib><creatorcontrib>Schaeffer‐Reiss, Christine</creatorcontrib><creatorcontrib>Davioud‐Charvet, Elisabeth</creatorcontrib><title>Proteomic Profiling of Antimalarial Plasmodione Using 3‐Benz(o)ylmenadione Affinity‐Based Probes</title><title>Chembiochem : a European journal of chemical biology</title><addtitle>Chembiochem</addtitle><description>Understanding the mechanisms of drug action in malarial parasites is crucial for the development of new drugs to combat infection and to counteract drug resistance. Proteomics is a widely used approach to study host‐pathogen systems and to identify drug protein targets. Plasmodione is an antiplasmodial early‐lead drug exerting potent activities against young asexual and sexual blood stages in vitro with low toxicity to host cells. To elucidate its molecular mechanisms, an affinity‐based protein profiling (AfBPP) approach was applied to yeast and P. falciparum proteomes. New (pro‐) AfBPP probes based on the 3‐benz(o)yl‐6‐fluoro‐menadione scaffold were synthesized. With optimized conditions of both photoaffinity labeling and click reaction steps, the AfBPP protocol was then applied to a yeast proteome, yielding 11 putative drug‐protein targets. Among these, we found four proteins associated with oxidoreductase activities, the hypothesized type of targets for plasmodione and its metabolites, and other proteins associated with the mitochondria. In Plasmodium parasites, the MS analysis revealed 44 potential plasmodione targets that need to be validated in further studies. Finally, the localization of a 3‐benzyl‐6‐fluoromenadione AfBPP probe was studied in the subcellular structures of the parasite at the trophozoite stage.
We describe here the design, synthesis and evaluation of an antiplasmodial 3‐benzyl‐6‐fluoro‐menadione probe for affinity‐based protein profiling experiments using yeast and P. falciparum parasite lysates. These studies allowed us to identify a first list of proteins interacting with plasmodione in both yeast and P. falciparum late trophozoites.</description><subject>Activity-Based Protein Profiling</subject><subject>Affinity</subject><subject>Antiprotozoal agents</subject><subject>Biological Chemistry and Chemical Biology</subject><subject>Blood parasites</subject><subject>Chemical synthesis</subject><subject>Drug development</subject><subject>Drug resistance</subject><subject>Localization</subject><subject>Menadione</subject><subject>Metabolites</subject><subject>Molecular modelling</subject><subject>Oxidoreductase</subject><subject>Parasite resistance</subject><subject>Parasites</subject><subject>Photoaffinity Labeling</subject><subject>Probes</subject><subject>Proteins</subject><subject>Proteomes</subject><subject>Proteomics</subject><subject>Toxicity</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>1439-4227</issn><issn>1439-7633</issn><issn>1439-7633</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><recordid>eNqFkMtKAzEUhoMotla3LmXATV205jIzSZZt8VIo2IVdD5nJGUnJTOqkRerKR_AZfRIztFZwI4TkJOc7P-FD6JLgIcGY3ha5KYYU0xhjIvgR6pKYyQFPGTve1zGlvIPOvF9ijGXKyCnqMJEySQntIj1v3BpcZYooVKWxpn6JXBmN6rWplFWNUTaaW-Urp42rIVr4lmBfH59jqN_77mZrK6jVrjkqS1Ob9bbtKg-6zczBn6OTUlkPF_uzhxb3d8-Tx8Hs6WE6Gc0GBZWCh51rzpI41mFRwgURRQyatI9ciTgXXGJFcIq5zhlVRIBUItfhrkAmwHqov8tdNe51A36dVcYXYK2qwW18xnDMMGeS4YBe_0GXbtPU4XeBEpzIRPIkUMMdVTTO-wbKbNUELc02Izhr_Wet_-zgPwxc7WM3eQX6gP8ID4DcAW_GwvafuGwynk5-w78BbBCSfQ</recordid><startdate>20240801</startdate><enddate>20240801</enddate><creator>Iacobucci, Ilaria</creator><creator>Monaco, Vittoria</creator><creator>Hovasse, Agnès</creator><creator>Dupouy, Baptiste</creator><creator>Keumoe, Rodrigue</creator><creator>Cichocki, Bogdan</creator><creator>Elhabiri, Mourad</creator><creator>Meunier, Brigitte</creator><creator>Strub, Jean‐Marc</creator><creator>Monti, Maria</creator><creator>Cianférani, Sarah</creator><creator>Blandin, Stéphanie A.</creator><creator>Schaeffer‐Reiss, Christine</creator><creator>Davioud‐Charvet, Elisabeth</creator><general>Wiley Subscription Services, Inc</general><scope>24P</scope><scope>WIN</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-7026-4034</orcidid></search><sort><creationdate>20240801</creationdate><title>Proteomic Profiling of Antimalarial Plasmodione Using 3‐Benz(o)ylmenadione Affinity‐Based Probes</title><author>Iacobucci, Ilaria ; Monaco, Vittoria ; Hovasse, Agnès ; Dupouy, Baptiste ; Keumoe, Rodrigue ; Cichocki, Bogdan ; Elhabiri, Mourad ; Meunier, Brigitte ; Strub, Jean‐Marc ; Monti, Maria ; Cianférani, Sarah ; Blandin, Stéphanie A. ; Schaeffer‐Reiss, Christine ; Davioud‐Charvet, Elisabeth</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2987-c27d73544d44d217818c4ed1d7357a84b8790a10607db32a18e9a8bd607ae95e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Activity-Based Protein Profiling</topic><topic>Affinity</topic><topic>Antiprotozoal agents</topic><topic>Biological Chemistry and Chemical Biology</topic><topic>Blood parasites</topic><topic>Chemical synthesis</topic><topic>Drug development</topic><topic>Drug resistance</topic><topic>Localization</topic><topic>Menadione</topic><topic>Metabolites</topic><topic>Molecular modelling</topic><topic>Oxidoreductase</topic><topic>Parasite resistance</topic><topic>Parasites</topic><topic>Photoaffinity Labeling</topic><topic>Probes</topic><topic>Proteins</topic><topic>Proteomes</topic><topic>Proteomics</topic><topic>Toxicity</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Iacobucci, Ilaria</creatorcontrib><creatorcontrib>Monaco, Vittoria</creatorcontrib><creatorcontrib>Hovasse, Agnès</creatorcontrib><creatorcontrib>Dupouy, Baptiste</creatorcontrib><creatorcontrib>Keumoe, Rodrigue</creatorcontrib><creatorcontrib>Cichocki, Bogdan</creatorcontrib><creatorcontrib>Elhabiri, Mourad</creatorcontrib><creatorcontrib>Meunier, Brigitte</creatorcontrib><creatorcontrib>Strub, Jean‐Marc</creatorcontrib><creatorcontrib>Monti, Maria</creatorcontrib><creatorcontrib>Cianférani, Sarah</creatorcontrib><creatorcontrib>Blandin, Stéphanie A.</creatorcontrib><creatorcontrib>Schaeffer‐Reiss, Christine</creatorcontrib><creatorcontrib>Davioud‐Charvet, Elisabeth</creatorcontrib><collection>Wiley-Blackwell Titles (Open access)</collection><collection>Wiley-Blackwell Backfiles (Open access)</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Chembiochem : a European journal of chemical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Iacobucci, Ilaria</au><au>Monaco, Vittoria</au><au>Hovasse, Agnès</au><au>Dupouy, Baptiste</au><au>Keumoe, Rodrigue</au><au>Cichocki, Bogdan</au><au>Elhabiri, Mourad</au><au>Meunier, Brigitte</au><au>Strub, Jean‐Marc</au><au>Monti, Maria</au><au>Cianférani, Sarah</au><au>Blandin, Stéphanie A.</au><au>Schaeffer‐Reiss, Christine</au><au>Davioud‐Charvet, Elisabeth</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteomic Profiling of Antimalarial Plasmodione Using 3‐Benz(o)ylmenadione Affinity‐Based Probes</atitle><jtitle>Chembiochem : a European journal of chemical biology</jtitle><addtitle>Chembiochem</addtitle><date>2024-08-01</date><risdate>2024</risdate><volume>25</volume><issue>15</issue><spage>e202400187</spage><epage>n/a</epage><pages>e202400187-n/a</pages><issn>1439-4227</issn><issn>1439-7633</issn><eissn>1439-7633</eissn><notes>Authors contributed equally as first co‐authors</notes><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Understanding the mechanisms of drug action in malarial parasites is crucial for the development of new drugs to combat infection and to counteract drug resistance. Proteomics is a widely used approach to study host‐pathogen systems and to identify drug protein targets. Plasmodione is an antiplasmodial early‐lead drug exerting potent activities against young asexual and sexual blood stages in vitro with low toxicity to host cells. To elucidate its molecular mechanisms, an affinity‐based protein profiling (AfBPP) approach was applied to yeast and P. falciparum proteomes. New (pro‐) AfBPP probes based on the 3‐benz(o)yl‐6‐fluoro‐menadione scaffold were synthesized. With optimized conditions of both photoaffinity labeling and click reaction steps, the AfBPP protocol was then applied to a yeast proteome, yielding 11 putative drug‐protein targets. Among these, we found four proteins associated with oxidoreductase activities, the hypothesized type of targets for plasmodione and its metabolites, and other proteins associated with the mitochondria. In Plasmodium parasites, the MS analysis revealed 44 potential plasmodione targets that need to be validated in further studies. Finally, the localization of a 3‐benzyl‐6‐fluoromenadione AfBPP probe was studied in the subcellular structures of the parasite at the trophozoite stage.
We describe here the design, synthesis and evaluation of an antiplasmodial 3‐benzyl‐6‐fluoro‐menadione probe for affinity‐based protein profiling experiments using yeast and P. falciparum parasite lysates. These studies allowed us to identify a first list of proteins interacting with plasmodione in both yeast and P. falciparum late trophozoites.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>38639212</pmid><doi>10.1002/cbic.202400187</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0001-7026-4034</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1439-4227 |
| ispartof | Chembiochem : a European journal of chemical biology, 2024-08, Vol.25 (15), p.e202400187-n/a |
| issn | 1439-4227 1439-7633 1439-7633 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_3043073930 |
| source | Wiley Online Library |
| subjects | Activity-Based Protein Profiling Affinity Antiprotozoal agents Biological Chemistry and Chemical Biology Blood parasites Chemical synthesis Drug development Drug resistance Localization Menadione Metabolites Molecular modelling Oxidoreductase Parasite resistance Parasites Photoaffinity Labeling Probes Proteins Proteomes Proteomics Toxicity Yeast Yeasts |
| title | Proteomic Profiling of Antimalarial Plasmodione Using 3‐Benz(o)ylmenadione Affinity‐Based Probes |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-09-23T07%3A21%3A51IST&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=Proteomic%20Profiling%20of%20Antimalarial%20Plasmodione%20Using%203%E2%80%90Benz(o)ylmenadione%20Affinity%E2%80%90Based%20Probes&rft.jtitle=Chembiochem%20:%20a%20European%20journal%20of%20chemical%20biology&rft.au=Iacobucci,%20Ilaria&rft.date=2024-08-01&rft.volume=25&rft.issue=15&rft.spage=e202400187&rft.epage=n/a&rft.pages=e202400187-n/a&rft.issn=1439-4227&rft.eissn=1439-7633&rft_id=info:doi/10.1002/cbic.202400187&rft_dat=%3Cproquest_cross%3E3043073930%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c2987-c27d73544d44d217818c4ed1d7357a84b8790a10607db32a18e9a8bd607ae95e3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=3087195975&rft_id=info:pmid/38639212&rfr_iscdi=true |