Pub Date : 2019-01-01DOI: 10.1016/s0065-2296(19)30075-8
{"title":"Acknowledgments","authors":"","doi":"10.1016/s0065-2296(19)30075-8","DOIUrl":"https://doi.org/10.1016/s0065-2296(19)30075-8","url":null,"abstract":"","PeriodicalId":7282,"journal":{"name":"Advances in Botanical Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/s0065-2296(19)30075-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"55854692","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2017-12-31DOI: 10.1016/BS.ABR.2016.11.002
B. Schatz, N. Sauvion, F. Kjellberg, A. Nel
{"title":"Chapter One – Plant–Insect Interactions: A Palaeontological and an Evolutionary Perspective","authors":"B. Schatz, N. Sauvion, F. Kjellberg, A. Nel","doi":"10.1016/BS.ABR.2016.11.002","DOIUrl":"https://doi.org/10.1016/BS.ABR.2016.11.002","url":null,"abstract":"","PeriodicalId":7282,"journal":{"name":"Advances in Botanical Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2017-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/BS.ABR.2016.11.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46170451","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2017-12-31DOI: 10.1016/BS.ABR.2016.12.006
R. Chaney, I. A. Baklanov
{"title":"Chapter Five – Phytoremediation and Phytomining: Status and Promise","authors":"R. Chaney, I. A. Baklanov","doi":"10.1016/BS.ABR.2016.12.006","DOIUrl":"https://doi.org/10.1016/BS.ABR.2016.12.006","url":null,"abstract":"","PeriodicalId":7282,"journal":{"name":"Advances in Botanical Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2017-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/BS.ABR.2016.12.006","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46091058","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2017-08-14DOI: 10.1016/BS.ABR.2017.06.008
A. N. Vanclova, Lucia Hadariová, Š. Hrdá, V. Hampl
{"title":"Secondary Plastids of Euglenophytes","authors":"A. N. Vanclova, Lucia Hadariová, Š. Hrdá, V. Hampl","doi":"10.1016/BS.ABR.2017.06.008","DOIUrl":"https://doi.org/10.1016/BS.ABR.2017.06.008","url":null,"abstract":"","PeriodicalId":7282,"journal":{"name":"Advances in Botanical Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2017-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/BS.ABR.2017.06.008","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47483635","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2015-01-01DOI: 10.1016/bs.abr.2015.08.006
Yilong Li, Tao Bi, Julio A Camarero
Cyclotides are fascinating naturally occurring micro-proteins (≈30 residues long) present in several plant families, and display various biological properties such as protease inhibitory, anti-microbial, insecticidal, cytotoxic, anti-HIV and hormone-like activities. Cyclotides share a unique head-to-tail circular knotted topology of three disulfide bridges, with one disulfide penetrating through a macrocycle formed by the two other disulfides and interconnecting peptide backbones, forming what is called a cystine knot topology. This cyclic cystine knot (CCK) framework gives the cyclotides exceptional rigidity, resistance to thermal and chemical denaturation, and enzymatic stability against degradation. Interestingly, cyclotides have been shown to be orally bioavailable, and other cyclotides have been shown to cross the cell membranes. Moreover, recent reports have also shown that engineered cyclotides can be efficiently used to target extracellular and intracellular protein-protein interactions, therefore making cyclotides ideal tools for drug development to selectively target protein-protein interactions. In this work we will review all the available methods for production of these interesting proteins using chemical or biological methods.
{"title":"Chemical and biological production of cyclotides.","authors":"Yilong Li, Tao Bi, Julio A Camarero","doi":"10.1016/bs.abr.2015.08.006","DOIUrl":"https://doi.org/10.1016/bs.abr.2015.08.006","url":null,"abstract":"<p><p>Cyclotides are fascinating naturally occurring micro-proteins (≈30 residues long) present in several plant families<i>,</i> and display various biological properties such as protease inhibitory, anti-microbial, insecticidal, cytotoxic, anti-HIV and hormone-like activities. Cyclotides share a unique head-to-tail circular knotted topology of three disulfide bridges, with one disulfide penetrating through a macrocycle formed by the two other disulfides and interconnecting peptide backbones, forming what is called a cystine knot topology. This cyclic cystine knot (CCK) framework gives the cyclotides exceptional rigidity, resistance to thermal and chemical denaturation, and enzymatic stability against degradation. Interestingly, cyclotides have been shown to be orally bioavailable, and other cyclotides have been shown to cross the cell membranes. Moreover, recent reports have also shown that engineered cyclotides can be efficiently used to target extracellular and intracellular protein-protein interactions, therefore making cyclotides ideal tools for drug development to selectively target protein-protein interactions. In this work we will review all the available methods for production of these interesting proteins using chemical or biological methods.</p>","PeriodicalId":7282,"journal":{"name":"Advances in Botanical Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.abr.2015.08.006","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34389231","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Book chapter postprint DOI: 10.1016/bs.abr.2015.08.005 License: Sherpa/Romeo 0065-2296 Abstract: Cyclotides are gene-encoded, ribosomally produced cyclic proteins. Their biosynthesis is a multistep process involving several enzymes for translation, disulphide isomerization, transport, cleavage and, finally, cyclization. Here, we describe this process, focusing on the cyclization step and the vacuolar processing enzyme (VPE) that performs it. Cyclotide precursor proteins contain prodomains that direct organelle targeting and contain sequences necessary for cyclization in addition to the one or more domains that make up the final cyclic product. The VPEs are a family of cysteine proteases that perform cyclization by an adaptation of their more commonly described proteolysis mechanism. VPE-mediated cyclization is dependent on the presence of short recognition sequences (within and flanking the mature cyclotide domain) which have been characterized in vivo and in vitro for the prototypical cyclotide kalata B1. Finally, we compare cyclization by VPEs to other methods of protein cyclization found in nature or developed for biotechnology. Understanding cyclotide biosynthesis is important for both fundamental science, and for broader protein cyclization applications.
{"title":"Biosynthesis of cyclotides","authors":"Thomas M A Shafee, K. Harris, M. Anderson","doi":"10.26181/5E3A3D90E6328","DOIUrl":"https://doi.org/10.26181/5E3A3D90E6328","url":null,"abstract":"Book chapter postprint DOI: 10.1016/bs.abr.2015.08.005 License: Sherpa/Romeo 0065-2296 Abstract: Cyclotides are gene-encoded, ribosomally produced cyclic proteins. Their biosynthesis is a multistep process involving several enzymes for translation, disulphide isomerization, transport, cleavage and, finally, cyclization. Here, we describe this process, focusing on the cyclization step and the vacuolar processing enzyme (VPE) that performs it. Cyclotide precursor proteins contain prodomains that direct organelle targeting and contain sequences necessary for cyclization in addition to the one or more domains that make up the final cyclic product. The VPEs are a family of cysteine proteases that perform cyclization by an adaptation of their more commonly described proteolysis mechanism. VPE-mediated cyclization is dependent on the presence of short recognition sequences (within and flanking the mature cyclotide domain) which have been characterized in vivo and in vitro for the prototypical cyclotide kalata B1. Finally, we compare cyclization by VPEs to other methods of protein cyclization found in nature or developed for biotechnology. Understanding cyclotide biosynthesis is important for both fundamental science, and for broader protein cyclization applications.","PeriodicalId":7282,"journal":{"name":"Advances in Botanical Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69262406","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-01-01DOI: 10.1016/B978-0-12-417162-6.00009-2
B. Thompson
{"title":"Genetic and Hormonal Regulation of Maize Inflorescence Development","authors":"B. Thompson","doi":"10.1016/B978-0-12-417162-6.00009-2","DOIUrl":"https://doi.org/10.1016/B978-0-12-417162-6.00009-2","url":null,"abstract":"","PeriodicalId":7282,"journal":{"name":"Advances in Botanical Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/B978-0-12-417162-6.00009-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54122831","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-01-01DOI: 10.1016/B978-0-12-397940-7.00007-0
Thibaut Payen, C. Murat, G. Bonito
{"title":"Truffle Phylogenomics: New Insights into Truffle Evolution and Truffle Life Cycle","authors":"Thibaut Payen, C. Murat, G. Bonito","doi":"10.1016/B978-0-12-397940-7.00007-0","DOIUrl":"https://doi.org/10.1016/B978-0-12-397940-7.00007-0","url":null,"abstract":"","PeriodicalId":7282,"journal":{"name":"Advances in Botanical Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/B978-0-12-397940-7.00007-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54103640","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2014-01-01DOI: 10.1016/B978-0-12-408062-1.00011-1
J. Dumay, M. Morançais, M. Munier, C. Guillard, J. Fleurence
{"title":"Phycoerythrins: Valuable Proteinic Pigments in Red Seaweeds","authors":"J. Dumay, M. Morançais, M. Munier, C. Guillard, J. Fleurence","doi":"10.1016/B978-0-12-408062-1.00011-1","DOIUrl":"https://doi.org/10.1016/B978-0-12-408062-1.00011-1","url":null,"abstract":"","PeriodicalId":7282,"journal":{"name":"Advances in Botanical Research","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/B978-0-12-408062-1.00011-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54113035","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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