Loading…
Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction
Arrestin-dependent pathways are a central component of G protein-coupled receptor (GPCRs) signaling. However, the molecular processes regulating arrestin binding are to be further illuminated, in particular with regard to the structural impact of GPCR C-terminal disordered regions. Here, we used an...
Saved in:
Published in: | Biomolecules (Basel, Switzerland) Switzerland), 2022-04, Vol.12 (5), p.617 |
---|---|
Main Authors: | , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c512t-c59bd8caa950eb96aa8b5d989f90d8e2957e4f793dcb0bbc2875bc6c5f1de4513 |
---|---|
cites | cdi_FETCH-LOGICAL-c512t-c59bd8caa950eb96aa8b5d989f90d8e2957e4f793dcb0bbc2875bc6c5f1de4513 |
container_end_page | |
container_issue | 5 |
container_start_page | 617 |
container_title | Biomolecules (Basel, Switzerland) |
container_volume | 12 |
creator | Guillien, Myriam Mouhand, Assia Fournet, Aurélie Gontier, Amandine Martí Navia, Aleix Cordeiro, Tiago N Allemand, Frédéric Thureau, Aurélien Banères, Jean-Louis Bernadó, Pau Sibille, Nathalie |
description | Arrestin-dependent pathways are a central component of G protein-coupled receptor (GPCRs) signaling. However, the molecular processes regulating arrestin binding are to be further illuminated, in particular with regard to the structural impact of GPCR C-terminal disordered regions. Here, we used an integrated biophysical strategy to describe the basal conformations of the C-terminal domains of three class A GPCRs, the vasopressin V2 receptor (V2R), the growth hormone secretagogue or ghrelin receptor type 1a (GHSR) and the β2-adernergic receptor (β2AR). By doing so, we revealed the presence of transient secondary structures in these regions that are potentially involved in the interaction with arrestin. These secondary structure elements differ from those described in the literature in interaction with arrestin. This suggests a mechanism where the secondary structure conformational preferences in the C-terminal regions of GPCRs could be a central feature for optimizing arrestins recognition. |
doi_str_mv | 10.3390/biom12050617 |
format | article |
fullrecord | <record><control><sourceid>proquest_doaj_</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_1595edf4faf3410b84a10f7e944cbad6</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_1595edf4faf3410b84a10f7e944cbad6</doaj_id><sourcerecordid>2671273607</sourcerecordid><originalsourceid>FETCH-LOGICAL-c512t-c59bd8caa950eb96aa8b5d989f90d8e2957e4f793dcb0bbc2875bc6c5f1de4513</originalsourceid><addsrcrecordid>eNpdkt9rFDEQxxdRbKl981kWfFHoan5sdpMX4Ti1PThRagXfQn7M3uXY3bRJ9qD_vbm7Wq4NIQmTz3wzmZmieIvRJ0oF-qydHzBBDDW4fVGcEoJ5RVr69-XR-aQ4j3GD8uB5Evq6OKGsIYwxdFpsf6cwmTQF1ZeLMbrVOsXSjcmXaQ3ZkoLLVqP6_r786qIPFgLY8vLX_LqcVzcQBjdm12tYOT9elD_UxodyZlJe3VjOQoCY3Fjt-awGQZmUyTfFq071Ec4f9rPiz_dvN_OravnzcjGfLSvDMEl5Fdpyo5RgCLRolOKaWcFFJ5DlQARroe5aQa3RSGtDeMu0aQzrsIWaYXpWLA661quNvA1uUOFeeuXk3uDDSqqQnOlBYiYY2K7uVEdrjDSvFUZdC6KujVa2yVpfDlq3kx7AGsjJUf0T0ac3o1vLld9KgSmnZBfMx4PA-pnb1WwpdzZE25rXiG937IeHx4K_m3IS5eCigb5XI_gpStK0OBe3QW1G3z9DN34KuSp7KpecEYYydXGgTPAxBugeI8BI7npJHvdSxt8df_YR_t859B_Si8V-</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2670085250</pqid></control><display><type>article</type><title>Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction</title><source>Publicly Available Content Database</source><source>PubMed</source><creator>Guillien, Myriam ; Mouhand, Assia ; Fournet, Aurélie ; Gontier, Amandine ; Martí Navia, Aleix ; Cordeiro, Tiago N ; Allemand, Frédéric ; Thureau, Aurélien ; Banères, Jean-Louis ; Bernadó, Pau ; Sibille, Nathalie</creator><creatorcontrib>Guillien, Myriam ; Mouhand, Assia ; Fournet, Aurélie ; Gontier, Amandine ; Martí Navia, Aleix ; Cordeiro, Tiago N ; Allemand, Frédéric ; Thureau, Aurélien ; Banères, Jean-Louis ; Bernadó, Pau ; Sibille, Nathalie</creatorcontrib><description>Arrestin-dependent pathways are a central component of G protein-coupled receptor (GPCRs) signaling. However, the molecular processes regulating arrestin binding are to be further illuminated, in particular with regard to the structural impact of GPCR C-terminal disordered regions. Here, we used an integrated biophysical strategy to describe the basal conformations of the C-terminal domains of three class A GPCRs, the vasopressin V2 receptor (V2R), the growth hormone secretagogue or ghrelin receptor type 1a (GHSR) and the β2-adernergic receptor (β2AR). By doing so, we revealed the presence of transient secondary structures in these regions that are potentially involved in the interaction with arrestin. These secondary structure elements differ from those described in the literature in interaction with arrestin. This suggests a mechanism where the secondary structure conformational preferences in the C-terminal regions of GPCRs could be a central feature for optimizing arrestins recognition.</description><identifier>ISSN: 2218-273X</identifier><identifier>EISSN: 2218-273X</identifier><identifier>DOI: 10.3390/biom12050617</identifier><identifier>PMID: 35625550</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Arrestin ; Biochemistry, Molecular Biology ; Cloning ; G protein-coupled receptors ; Ghrelin ; GPCR ; Growth hormones ; intrinsically disordered proteins or regions (IDPs/IDRs) ; Kinases ; Life Sciences ; NMR ; Nuclear magnetic resonance ; Phosphorylation ; Protein structure ; Proteins ; Secondary structure ; Sensors ; Signal transduction ; Vasopressin ; Vasopressin V2 receptors ; X-rays</subject><ispartof>Biomolecules (Basel, Switzerland), 2022-04, Vol.12 (5), p.617</ispartof><rights>2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>2022 by the authors. 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c512t-c59bd8caa950eb96aa8b5d989f90d8e2957e4f793dcb0bbc2875bc6c5f1de4513</citedby><cites>FETCH-LOGICAL-c512t-c59bd8caa950eb96aa8b5d989f90d8e2957e4f793dcb0bbc2875bc6c5f1de4513</cites><orcidid>0000-0002-6600-2784 ; 0000-0003-2663-3220 ; 0000-0002-0798-3180 ; 0000-0001-8145-6795 ; 0000-0001-5666-260X ; 0000-0001-7078-1285 ; 0000-0003-0396-6145 ; 0000-0001-7395-5922</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2670085250/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2670085250?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,74998</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35625550$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-03748408$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Guillien, Myriam</creatorcontrib><creatorcontrib>Mouhand, Assia</creatorcontrib><creatorcontrib>Fournet, Aurélie</creatorcontrib><creatorcontrib>Gontier, Amandine</creatorcontrib><creatorcontrib>Martí Navia, Aleix</creatorcontrib><creatorcontrib>Cordeiro, Tiago N</creatorcontrib><creatorcontrib>Allemand, Frédéric</creatorcontrib><creatorcontrib>Thureau, Aurélien</creatorcontrib><creatorcontrib>Banères, Jean-Louis</creatorcontrib><creatorcontrib>Bernadó, Pau</creatorcontrib><creatorcontrib>Sibille, Nathalie</creatorcontrib><title>Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction</title><title>Biomolecules (Basel, Switzerland)</title><addtitle>Biomolecules</addtitle><description>Arrestin-dependent pathways are a central component of G protein-coupled receptor (GPCRs) signaling. However, the molecular processes regulating arrestin binding are to be further illuminated, in particular with regard to the structural impact of GPCR C-terminal disordered regions. Here, we used an integrated biophysical strategy to describe the basal conformations of the C-terminal domains of three class A GPCRs, the vasopressin V2 receptor (V2R), the growth hormone secretagogue or ghrelin receptor type 1a (GHSR) and the β2-adernergic receptor (β2AR). By doing so, we revealed the presence of transient secondary structures in these regions that are potentially involved in the interaction with arrestin. These secondary structure elements differ from those described in the literature in interaction with arrestin. This suggests a mechanism where the secondary structure conformational preferences in the C-terminal regions of GPCRs could be a central feature for optimizing arrestins recognition.</description><subject>Arrestin</subject><subject>Biochemistry, Molecular Biology</subject><subject>Cloning</subject><subject>G protein-coupled receptors</subject><subject>Ghrelin</subject><subject>GPCR</subject><subject>Growth hormones</subject><subject>intrinsically disordered proteins or regions (IDPs/IDRs)</subject><subject>Kinases</subject><subject>Life Sciences</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Phosphorylation</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>Secondary structure</subject><subject>Sensors</subject><subject>Signal transduction</subject><subject>Vasopressin</subject><subject>Vasopressin V2 receptors</subject><subject>X-rays</subject><issn>2218-273X</issn><issn>2218-273X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNpdkt9rFDEQxxdRbKl981kWfFHoan5sdpMX4Ti1PThRagXfQn7M3uXY3bRJ9qD_vbm7Wq4NIQmTz3wzmZmieIvRJ0oF-qydHzBBDDW4fVGcEoJ5RVr69-XR-aQ4j3GD8uB5Evq6OKGsIYwxdFpsf6cwmTQF1ZeLMbrVOsXSjcmXaQ3ZkoLLVqP6_r786qIPFgLY8vLX_LqcVzcQBjdm12tYOT9elD_UxodyZlJe3VjOQoCY3Fjt-awGQZmUyTfFq071Ec4f9rPiz_dvN_OravnzcjGfLSvDMEl5Fdpyo5RgCLRolOKaWcFFJ5DlQARroe5aQa3RSGtDeMu0aQzrsIWaYXpWLA661quNvA1uUOFeeuXk3uDDSqqQnOlBYiYY2K7uVEdrjDSvFUZdC6KujVa2yVpfDlq3kx7AGsjJUf0T0ac3o1vLld9KgSmnZBfMx4PA-pnb1WwpdzZE25rXiG937IeHx4K_m3IS5eCigb5XI_gpStK0OBe3QW1G3z9DN34KuSp7KpecEYYydXGgTPAxBugeI8BI7npJHvdSxt8df_YR_t859B_Si8V-</recordid><startdate>20220421</startdate><enddate>20220421</enddate><creator>Guillien, Myriam</creator><creator>Mouhand, Assia</creator><creator>Fournet, Aurélie</creator><creator>Gontier, Amandine</creator><creator>Martí Navia, Aleix</creator><creator>Cordeiro, Tiago N</creator><creator>Allemand, Frédéric</creator><creator>Thureau, Aurélien</creator><creator>Banères, Jean-Louis</creator><creator>Bernadó, Pau</creator><creator>Sibille, Nathalie</creator><general>MDPI AG</general><general>MDPI</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-6600-2784</orcidid><orcidid>https://orcid.org/0000-0003-2663-3220</orcidid><orcidid>https://orcid.org/0000-0002-0798-3180</orcidid><orcidid>https://orcid.org/0000-0001-8145-6795</orcidid><orcidid>https://orcid.org/0000-0001-5666-260X</orcidid><orcidid>https://orcid.org/0000-0001-7078-1285</orcidid><orcidid>https://orcid.org/0000-0003-0396-6145</orcidid><orcidid>https://orcid.org/0000-0001-7395-5922</orcidid></search><sort><creationdate>20220421</creationdate><title>Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction</title><author>Guillien, Myriam ; Mouhand, Assia ; Fournet, Aurélie ; Gontier, Amandine ; Martí Navia, Aleix ; Cordeiro, Tiago N ; Allemand, Frédéric ; Thureau, Aurélien ; Banères, Jean-Louis ; Bernadó, Pau ; Sibille, Nathalie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c512t-c59bd8caa950eb96aa8b5d989f90d8e2957e4f793dcb0bbc2875bc6c5f1de4513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Arrestin</topic><topic>Biochemistry, Molecular Biology</topic><topic>Cloning</topic><topic>G protein-coupled receptors</topic><topic>Ghrelin</topic><topic>GPCR</topic><topic>Growth hormones</topic><topic>intrinsically disordered proteins or regions (IDPs/IDRs)</topic><topic>Kinases</topic><topic>Life Sciences</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>Phosphorylation</topic><topic>Protein structure</topic><topic>Proteins</topic><topic>Secondary structure</topic><topic>Sensors</topic><topic>Signal transduction</topic><topic>Vasopressin</topic><topic>Vasopressin V2 receptors</topic><topic>X-rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Guillien, Myriam</creatorcontrib><creatorcontrib>Mouhand, Assia</creatorcontrib><creatorcontrib>Fournet, Aurélie</creatorcontrib><creatorcontrib>Gontier, Amandine</creatorcontrib><creatorcontrib>Martí Navia, Aleix</creatorcontrib><creatorcontrib>Cordeiro, Tiago N</creatorcontrib><creatorcontrib>Allemand, Frédéric</creatorcontrib><creatorcontrib>Thureau, Aurélien</creatorcontrib><creatorcontrib>Banères, Jean-Louis</creatorcontrib><creatorcontrib>Bernadó, Pau</creatorcontrib><creatorcontrib>Sibille, Nathalie</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>ProQuest Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</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>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</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 China</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Biomolecules (Basel, Switzerland)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Guillien, Myriam</au><au>Mouhand, Assia</au><au>Fournet, Aurélie</au><au>Gontier, Amandine</au><au>Martí Navia, Aleix</au><au>Cordeiro, Tiago N</au><au>Allemand, Frédéric</au><au>Thureau, Aurélien</au><au>Banères, Jean-Louis</au><au>Bernadó, Pau</au><au>Sibille, Nathalie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction</atitle><jtitle>Biomolecules (Basel, Switzerland)</jtitle><addtitle>Biomolecules</addtitle><date>2022-04-21</date><risdate>2022</risdate><volume>12</volume><issue>5</issue><spage>617</spage><pages>617-</pages><issn>2218-273X</issn><eissn>2218-273X</eissn><abstract>Arrestin-dependent pathways are a central component of G protein-coupled receptor (GPCRs) signaling. However, the molecular processes regulating arrestin binding are to be further illuminated, in particular with regard to the structural impact of GPCR C-terminal disordered regions. Here, we used an integrated biophysical strategy to describe the basal conformations of the C-terminal domains of three class A GPCRs, the vasopressin V2 receptor (V2R), the growth hormone secretagogue or ghrelin receptor type 1a (GHSR) and the β2-adernergic receptor (β2AR). By doing so, we revealed the presence of transient secondary structures in these regions that are potentially involved in the interaction with arrestin. These secondary structure elements differ from those described in the literature in interaction with arrestin. This suggests a mechanism where the secondary structure conformational preferences in the C-terminal regions of GPCRs could be a central feature for optimizing arrestins recognition.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>35625550</pmid><doi>10.3390/biom12050617</doi><orcidid>https://orcid.org/0000-0002-6600-2784</orcidid><orcidid>https://orcid.org/0000-0003-2663-3220</orcidid><orcidid>https://orcid.org/0000-0002-0798-3180</orcidid><orcidid>https://orcid.org/0000-0001-8145-6795</orcidid><orcidid>https://orcid.org/0000-0001-5666-260X</orcidid><orcidid>https://orcid.org/0000-0001-7078-1285</orcidid><orcidid>https://orcid.org/0000-0003-0396-6145</orcidid><orcidid>https://orcid.org/0000-0001-7395-5922</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 2218-273X |
ispartof | Biomolecules (Basel, Switzerland), 2022-04, Vol.12 (5), p.617 |
issn | 2218-273X 2218-273X |
language | eng |
recordid | cdi_doaj_primary_oai_doaj_org_article_1595edf4faf3410b84a10f7e944cbad6 |
source | Publicly Available Content Database; PubMed |
subjects | Arrestin Biochemistry, Molecular Biology Cloning G protein-coupled receptors Ghrelin GPCR Growth hormones intrinsically disordered proteins or regions (IDPs/IDRs) Kinases Life Sciences NMR Nuclear magnetic resonance Phosphorylation Protein structure Proteins Secondary structure Sensors Signal transduction Vasopressin Vasopressin V2 receptors X-rays |
title | Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T17%3A42%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_doaj_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structural%20Insights%20into%20the%20Intrinsically%20Disordered%20GPCR%20C-Terminal%20Region,%20Major%20Actor%20in%20Arrestin-GPCR%20Interaction&rft.jtitle=Biomolecules%20(Basel,%20Switzerland)&rft.au=Guillien,%20Myriam&rft.date=2022-04-21&rft.volume=12&rft.issue=5&rft.spage=617&rft.pages=617-&rft.issn=2218-273X&rft.eissn=2218-273X&rft_id=info:doi/10.3390/biom12050617&rft_dat=%3Cproquest_doaj_%3E2671273607%3C/proquest_doaj_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c512t-c59bd8caa950eb96aa8b5d989f90d8e2957e4f793dcb0bbc2875bc6c5f1de4513%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2670085250&rft_id=info:pmid/35625550&rfr_iscdi=true |