Understanding Rad51 function is a prerequisite for progress in cancer research

The human protein Rad51 is double-edged in cancer contexts: on one hand, preventing tumourigenesis by eliminating potentially carcinogenic DNA damage and, on the other, promoting tumours by introducing new mutations. Understanding mechanistic details of Rad51 in homologous recombination (HR) and rep...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Bengt Nordén [verfasserIn] Masayuki Takahashi [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	Rad51 homologous recombination cancer DNA repair RecA DNA strand exchange

Übergeordnetes Werk:	In: QRB Discovery - Cambridge University Press, 2021, 1(2020)
Übergeordnetes Werk:	volume:1 ; year:2020

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1017/qrd.2020.13

Katalog-ID:	DOAJ088084523

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520			\|a The human protein Rad51 is double-edged in cancer contexts: on one hand, preventing tumourigenesis by eliminating potentially carcinogenic DNA damage and, on the other, promoting tumours by introducing new mutations. Understanding mechanistic details of Rad51 in homologous recombination (HR) and repair could facilitate design of novel methods, including CRISPR, for Rad51-targeted cancer treatment. Despite extensive research, however, we do not yet understand the mechanism of HR in sufficient detail, partly due to complexity, a large number of Rad51 protein units being involved in the exchange of long DNA segments. Another reason for lack of understanding could be that current recognition models of DNA interactions focus only on hydrogen bond-directed base pair formation. A more complete model may need to include, for example, the kinetic effects of DNA base stacking and unstacking (‘longitudinal breathing’). These might explain how Rad51 can recognize sequence identity of DNA over several bases long stretches with high accuracy, despite the fact that a single base mismatch could be tolerated if we consider only the hydrogen bond energy. We here propose that certain specific hydrophobic effects, recently discovered destabilizing stacking of nucleobases, may play a central role in this context for the function of Rad51.
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allfields	10.1017/qrd.2020.13 doi (DE-627)DOAJ088084523 (DE-599)DOAJe9f4ddc765864a88bc703f320008b794 DE-627 ger DE-627 rakwb eng TP248.13-248.65 QH301-705.5 Bengt Nordén verfasserin aut Understanding Rad51 function is a prerequisite for progress in cancer research 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The human protein Rad51 is double-edged in cancer contexts: on one hand, preventing tumourigenesis by eliminating potentially carcinogenic DNA damage and, on the other, promoting tumours by introducing new mutations. Understanding mechanistic details of Rad51 in homologous recombination (HR) and repair could facilitate design of novel methods, including CRISPR, for Rad51-targeted cancer treatment. Despite extensive research, however, we do not yet understand the mechanism of HR in sufficient detail, partly due to complexity, a large number of Rad51 protein units being involved in the exchange of long DNA segments. Another reason for lack of understanding could be that current recognition models of DNA interactions focus only on hydrogen bond-directed base pair formation. A more complete model may need to include, for example, the kinetic effects of DNA base stacking and unstacking (‘longitudinal breathing’). These might explain how Rad51 can recognize sequence identity of DNA over several bases long stretches with high accuracy, despite the fact that a single base mismatch could be tolerated if we consider only the hydrogen bond energy. We here propose that certain specific hydrophobic effects, recently discovered destabilizing stacking of nucleobases, may play a central role in this context for the function of Rad51. Rad51 homologous recombination cancer DNA repair RecA DNA strand exchange Biotechnology Biology (General) Masayuki Takahashi verfasserin aut In QRB Discovery Cambridge University Press, 2021 1(2020) (DE-627)1744202591 (DE-600)3049859-4 26332892 nnns volume:1 year:2020 https://doi.org/10.1017/qrd.2020.13 kostenfrei https://doaj.org/article/e9f4ddc765864a88bc703f320008b794 kostenfrei https://www.cambridge.org/core/product/identifier/S2633289220000137/type/journal_article kostenfrei https://doaj.org/toc/2633-2892 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_374 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2014 GBV_ILN_2110 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 1 2020
spelling	10.1017/qrd.2020.13 doi (DE-627)DOAJ088084523 (DE-599)DOAJe9f4ddc765864a88bc703f320008b794 DE-627 ger DE-627 rakwb eng TP248.13-248.65 QH301-705.5 Bengt Nordén verfasserin aut Understanding Rad51 function is a prerequisite for progress in cancer research 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The human protein Rad51 is double-edged in cancer contexts: on one hand, preventing tumourigenesis by eliminating potentially carcinogenic DNA damage and, on the other, promoting tumours by introducing new mutations. Understanding mechanistic details of Rad51 in homologous recombination (HR) and repair could facilitate design of novel methods, including CRISPR, for Rad51-targeted cancer treatment. Despite extensive research, however, we do not yet understand the mechanism of HR in sufficient detail, partly due to complexity, a large number of Rad51 protein units being involved in the exchange of long DNA segments. Another reason for lack of understanding could be that current recognition models of DNA interactions focus only on hydrogen bond-directed base pair formation. A more complete model may need to include, for example, the kinetic effects of DNA base stacking and unstacking (‘longitudinal breathing’). These might explain how Rad51 can recognize sequence identity of DNA over several bases long stretches with high accuracy, despite the fact that a single base mismatch could be tolerated if we consider only the hydrogen bond energy. We here propose that certain specific hydrophobic effects, recently discovered destabilizing stacking of nucleobases, may play a central role in this context for the function of Rad51. Rad51 homologous recombination cancer DNA repair RecA DNA strand exchange Biotechnology Biology (General) Masayuki Takahashi verfasserin aut In QRB Discovery Cambridge University Press, 2021 1(2020) (DE-627)1744202591 (DE-600)3049859-4 26332892 nnns volume:1 year:2020 https://doi.org/10.1017/qrd.2020.13 kostenfrei https://doaj.org/article/e9f4ddc765864a88bc703f320008b794 kostenfrei https://www.cambridge.org/core/product/identifier/S2633289220000137/type/journal_article kostenfrei https://doaj.org/toc/2633-2892 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_374 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2014 GBV_ILN_2110 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 1 2020
allfields_unstemmed	10.1017/qrd.2020.13 doi (DE-627)DOAJ088084523 (DE-599)DOAJe9f4ddc765864a88bc703f320008b794 DE-627 ger DE-627 rakwb eng TP248.13-248.65 QH301-705.5 Bengt Nordén verfasserin aut Understanding Rad51 function is a prerequisite for progress in cancer research 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The human protein Rad51 is double-edged in cancer contexts: on one hand, preventing tumourigenesis by eliminating potentially carcinogenic DNA damage and, on the other, promoting tumours by introducing new mutations. Understanding mechanistic details of Rad51 in homologous recombination (HR) and repair could facilitate design of novel methods, including CRISPR, for Rad51-targeted cancer treatment. Despite extensive research, however, we do not yet understand the mechanism of HR in sufficient detail, partly due to complexity, a large number of Rad51 protein units being involved in the exchange of long DNA segments. Another reason for lack of understanding could be that current recognition models of DNA interactions focus only on hydrogen bond-directed base pair formation. A more complete model may need to include, for example, the kinetic effects of DNA base stacking and unstacking (‘longitudinal breathing’). These might explain how Rad51 can recognize sequence identity of DNA over several bases long stretches with high accuracy, despite the fact that a single base mismatch could be tolerated if we consider only the hydrogen bond energy. We here propose that certain specific hydrophobic effects, recently discovered destabilizing stacking of nucleobases, may play a central role in this context for the function of Rad51. Rad51 homologous recombination cancer DNA repair RecA DNA strand exchange Biotechnology Biology (General) Masayuki Takahashi verfasserin aut In QRB Discovery Cambridge University Press, 2021 1(2020) (DE-627)1744202591 (DE-600)3049859-4 26332892 nnns volume:1 year:2020 https://doi.org/10.1017/qrd.2020.13 kostenfrei https://doaj.org/article/e9f4ddc765864a88bc703f320008b794 kostenfrei https://www.cambridge.org/core/product/identifier/S2633289220000137/type/journal_article kostenfrei https://doaj.org/toc/2633-2892 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_374 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2014 GBV_ILN_2110 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 1 2020
allfieldsGer	10.1017/qrd.2020.13 doi (DE-627)DOAJ088084523 (DE-599)DOAJe9f4ddc765864a88bc703f320008b794 DE-627 ger DE-627 rakwb eng TP248.13-248.65 QH301-705.5 Bengt Nordén verfasserin aut Understanding Rad51 function is a prerequisite for progress in cancer research 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The human protein Rad51 is double-edged in cancer contexts: on one hand, preventing tumourigenesis by eliminating potentially carcinogenic DNA damage and, on the other, promoting tumours by introducing new mutations. Understanding mechanistic details of Rad51 in homologous recombination (HR) and repair could facilitate design of novel methods, including CRISPR, for Rad51-targeted cancer treatment. Despite extensive research, however, we do not yet understand the mechanism of HR in sufficient detail, partly due to complexity, a large number of Rad51 protein units being involved in the exchange of long DNA segments. Another reason for lack of understanding could be that current recognition models of DNA interactions focus only on hydrogen bond-directed base pair formation. A more complete model may need to include, for example, the kinetic effects of DNA base stacking and unstacking (‘longitudinal breathing’). These might explain how Rad51 can recognize sequence identity of DNA over several bases long stretches with high accuracy, despite the fact that a single base mismatch could be tolerated if we consider only the hydrogen bond energy. We here propose that certain specific hydrophobic effects, recently discovered destabilizing stacking of nucleobases, may play a central role in this context for the function of Rad51. Rad51 homologous recombination cancer DNA repair RecA DNA strand exchange Biotechnology Biology (General) Masayuki Takahashi verfasserin aut In QRB Discovery Cambridge University Press, 2021 1(2020) (DE-627)1744202591 (DE-600)3049859-4 26332892 nnns volume:1 year:2020 https://doi.org/10.1017/qrd.2020.13 kostenfrei https://doaj.org/article/e9f4ddc765864a88bc703f320008b794 kostenfrei https://www.cambridge.org/core/product/identifier/S2633289220000137/type/journal_article kostenfrei https://doaj.org/toc/2633-2892 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_374 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2014 GBV_ILN_2110 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 1 2020
allfieldsSound	10.1017/qrd.2020.13 doi (DE-627)DOAJ088084523 (DE-599)DOAJe9f4ddc765864a88bc703f320008b794 DE-627 ger DE-627 rakwb eng TP248.13-248.65 QH301-705.5 Bengt Nordén verfasserin aut Understanding Rad51 function is a prerequisite for progress in cancer research 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The human protein Rad51 is double-edged in cancer contexts: on one hand, preventing tumourigenesis by eliminating potentially carcinogenic DNA damage and, on the other, promoting tumours by introducing new mutations. Understanding mechanistic details of Rad51 in homologous recombination (HR) and repair could facilitate design of novel methods, including CRISPR, for Rad51-targeted cancer treatment. Despite extensive research, however, we do not yet understand the mechanism of HR in sufficient detail, partly due to complexity, a large number of Rad51 protein units being involved in the exchange of long DNA segments. Another reason for lack of understanding could be that current recognition models of DNA interactions focus only on hydrogen bond-directed base pair formation. A more complete model may need to include, for example, the kinetic effects of DNA base stacking and unstacking (‘longitudinal breathing’). These might explain how Rad51 can recognize sequence identity of DNA over several bases long stretches with high accuracy, despite the fact that a single base mismatch could be tolerated if we consider only the hydrogen bond energy. We here propose that certain specific hydrophobic effects, recently discovered destabilizing stacking of nucleobases, may play a central role in this context for the function of Rad51. Rad51 homologous recombination cancer DNA repair RecA DNA strand exchange Biotechnology Biology (General) Masayuki Takahashi verfasserin aut In QRB Discovery Cambridge University Press, 2021 1(2020) (DE-627)1744202591 (DE-600)3049859-4 26332892 nnns volume:1 year:2020 https://doi.org/10.1017/qrd.2020.13 kostenfrei https://doaj.org/article/e9f4ddc765864a88bc703f320008b794 kostenfrei https://www.cambridge.org/core/product/identifier/S2633289220000137/type/journal_article kostenfrei https://doaj.org/toc/2633-2892 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_374 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2014 GBV_ILN_2110 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 1 2020
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container_title	QRB Discovery
authorswithroles_txt_mv	Bengt Nordén @@aut@@ Masayuki Takahashi @@aut@@
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callnumber-first	T - Technology
author	Bengt Nordén
spellingShingle	Bengt Nordén misc TP248.13-248.65 misc QH301-705.5 misc Rad51 misc homologous recombination misc cancer misc DNA repair misc RecA misc DNA strand exchange misc Biotechnology misc Biology (General) Understanding Rad51 function is a prerequisite for progress in cancer research
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topic_title	TP248.13-248.65 QH301-705.5 Understanding Rad51 function is a prerequisite for progress in cancer research Rad51 homologous recombination cancer DNA repair RecA DNA strand exchange
topic	misc TP248.13-248.65 misc QH301-705.5 misc Rad51 misc homologous recombination misc cancer misc DNA repair misc RecA misc DNA strand exchange misc Biotechnology misc Biology (General)
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title	Understanding Rad51 function is a prerequisite for progress in cancer research
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title_full	Understanding Rad51 function is a prerequisite for progress in cancer research
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title_sort	understanding rad51 function is a prerequisite for progress in cancer research
callnumber	TP248.13-248.65
title_auth	Understanding Rad51 function is a prerequisite for progress in cancer research
abstract	The human protein Rad51 is double-edged in cancer contexts: on one hand, preventing tumourigenesis by eliminating potentially carcinogenic DNA damage and, on the other, promoting tumours by introducing new mutations. Understanding mechanistic details of Rad51 in homologous recombination (HR) and repair could facilitate design of novel methods, including CRISPR, for Rad51-targeted cancer treatment. Despite extensive research, however, we do not yet understand the mechanism of HR in sufficient detail, partly due to complexity, a large number of Rad51 protein units being involved in the exchange of long DNA segments. Another reason for lack of understanding could be that current recognition models of DNA interactions focus only on hydrogen bond-directed base pair formation. A more complete model may need to include, for example, the kinetic effects of DNA base stacking and unstacking (‘longitudinal breathing’). These might explain how Rad51 can recognize sequence identity of DNA over several bases long stretches with high accuracy, despite the fact that a single base mismatch could be tolerated if we consider only the hydrogen bond energy. We here propose that certain specific hydrophobic effects, recently discovered destabilizing stacking of nucleobases, may play a central role in this context for the function of Rad51.
abstractGer	The human protein Rad51 is double-edged in cancer contexts: on one hand, preventing tumourigenesis by eliminating potentially carcinogenic DNA damage and, on the other, promoting tumours by introducing new mutations. Understanding mechanistic details of Rad51 in homologous recombination (HR) and repair could facilitate design of novel methods, including CRISPR, for Rad51-targeted cancer treatment. Despite extensive research, however, we do not yet understand the mechanism of HR in sufficient detail, partly due to complexity, a large number of Rad51 protein units being involved in the exchange of long DNA segments. Another reason for lack of understanding could be that current recognition models of DNA interactions focus only on hydrogen bond-directed base pair formation. A more complete model may need to include, for example, the kinetic effects of DNA base stacking and unstacking (‘longitudinal breathing’). These might explain how Rad51 can recognize sequence identity of DNA over several bases long stretches with high accuracy, despite the fact that a single base mismatch could be tolerated if we consider only the hydrogen bond energy. We here propose that certain specific hydrophobic effects, recently discovered destabilizing stacking of nucleobases, may play a central role in this context for the function of Rad51.
abstract_unstemmed	The human protein Rad51 is double-edged in cancer contexts: on one hand, preventing tumourigenesis by eliminating potentially carcinogenic DNA damage and, on the other, promoting tumours by introducing new mutations. Understanding mechanistic details of Rad51 in homologous recombination (HR) and repair could facilitate design of novel methods, including CRISPR, for Rad51-targeted cancer treatment. Despite extensive research, however, we do not yet understand the mechanism of HR in sufficient detail, partly due to complexity, a large number of Rad51 protein units being involved in the exchange of long DNA segments. Another reason for lack of understanding could be that current recognition models of DNA interactions focus only on hydrogen bond-directed base pair formation. A more complete model may need to include, for example, the kinetic effects of DNA base stacking and unstacking (‘longitudinal breathing’). These might explain how Rad51 can recognize sequence identity of DNA over several bases long stretches with high accuracy, despite the fact that a single base mismatch could be tolerated if we consider only the hydrogen bond energy. We here propose that certain specific hydrophobic effects, recently discovered destabilizing stacking of nucleobases, may play a central role in this context for the function of Rad51.
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title_short	Understanding Rad51 function is a prerequisite for progress in cancer research
url	https://doi.org/10.1017/qrd.2020.13 https://doaj.org/article/e9f4ddc765864a88bc703f320008b794 https://www.cambridge.org/core/product/identifier/S2633289220000137/type/journal_article https://doaj.org/toc/2633-2892
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