cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5517/ccdc.csd.cc273mww
title: CCDC 2059078: Experimental Crystal Structure Determination

description: Related Article: Nagham Ibrahim, Chady Moussallem, Magali Allain, Olivier Segut, Frédéric Gohier, Pierre Frère|2021|ChemPlusChem|86|475|doi:10.1002/cplu.202100062
DOI: 10.5517/ccdc.csd.cc273myy
title: CCDC 2059080: Experimental Crystal Structure Determination

description: Related Article: Nagham Ibrahim, Chady Moussallem, Magali Allain, Olivier Segut, Frédéric Gohier, Pierre Frère|2021|ChemPlusChem|86|475|doi:10.1002/cplu.202100062
DOI: 10.5517/ccdc.csd.cc273mzz
title: CCDC 2059081: Experimental Crystal Structure Determination

description: Related Article: Nagham Ibrahim, Chady Moussallem, Magali Allain, Olivier Segut, Frédéric Gohier, Pierre Frère|2021|ChemPlusChem|86|475|doi:10.1002/cplu.202100062
DOI: 10.5517/ccdc.csd.cc273z3g
title: CCDC 2059395: Experimental Crystal Structure Determination

description: Related Article: Sinem-Fatma Schmiel, Holger Butenschön|2021|Eur.J.Org.Chem.|2021|2388|doi:10.1002/ejoc.202100335
DOI: 10.5517/ccdc.csd.cc273zp1
title: CCDC 2059413: Experimental Crystal Structure Determination

description: Related Article: Boris A. Worp, Mikhail D. Kosobokov, Alexander D. Dilman|2021|ChemPhotoChem|5|565|doi:10.1002/cptc.202100042
DOI: 10.5517/ccdc.csd.cc27498z
title: CCDC 2059710: Experimental Crystal Structure Determination

description: Related Article: Lei Li, William L. Turnbull, Robert McDonald, F. G. West|2021|Eur.J.Org.Chem.|2021|2294|doi:10.1002/ejoc.202100122
DOI: 10.5517/ccdc.csd.cc274s28
title: CCDC 2060169: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274s39
title: CCDC 2060170: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.25909/14978817.v1
title: Untitled Item

description: Data collected from systematic review used to generate GRAFT recommendations
DOI: 10.6084/m9.figshare.14978823
title: s5.bw

description: test data
DOI: 10.6084/m9.figshare.14978823.v1
title: s5.bw

description: test data
DOI: 10.5281/zenodo.5100491
title: Demo data for SEER-FISH

description: This is the demo data for SEER-FISH at https://github.com/JacobZuo/SEER-FISH.
DOI: 10.15468/zjqnug
title: A new species of Erythroxylum (Erythroxylaceae) from the Brazilian semiarid region

description: This dataset contains the digitized treatments in Plazi based on the original journal article Loiola, Maria Iracema Bezerra (2013): A new species of Erythroxylum (Erythroxylaceae) from the Brazilian semiarid region. Phytotaxa 150 (1): 61-64, DOI: 10.11646/phytotaxa.150.1.5, URL: http://dx.doi.org/10.11646/phytotaxa.150.1.5
DOI: 10.15468/825udz
title: Planothidium galaicum sp. nov. (Bacillariophyta, Achnanthidiaceae), a new diatom species from Galician coast, Spain

description: This dataset contains the digitized treatments in Plazi based on the original journal article Álvarez-Blanco, Irene, Blanco, Saúl (2013): Planothidium galaicum sp. nov. (Bacillariophyta, Achnanthidiaceae), a new diatom species from Galician coast, Spain. Phytotaxa 151 (1): 44-52, DOI: 10.11646/phytotaxa.151.1.4, URL: http://dx.doi.org/10.11646/phytotaxa.151.1.4
DOI: 10.6084/m9.figshare.14978796.v1
title: s4.bw

description: test data
DOI: 10.6084/m9.figshare.14978796
title: s4.bw

description: test data
DOI: 10.21227/kt94-yj43
title: A Fuzzy Decision Variables Framework for Large-scale Multiobjective Optimization

description: In large-scale multiobjective optimization, too many decision variables hinder the convergence search of evolutionary algorithms. Reducing the search range of the decision space will significantly alleviate this puzzle. With this in mind, this paper proposes a fuzzy decision variables framework for large-scale multiobjective optimization. The framework divides the entire evolutionary process into two main stages: fuzzy evolution and precise evolution. In fuzzy evolution, we blur the decision variables of the original solution to reduce the search range of the evolutionary algorithm in the decision space so that the evolutionary population can quickly converge. The degree of fuzzification gradually decreases with the evolutionary process. Once the population approximately converges, the framework will turn to precise evolution. In precise evolution, the actual decision variables of the solution are directly optimized to increase the diversity of the population so as to be closer to the true Pareto optimal front. Finally, this paper embeds some representative algorithms into the proposed framework and verifies the framework's effectiveness through comparative experiments on various large-scale multiobjective problems with 500 to 5000 decision variables. Experimental results show that in large-scale multiobjective optimization, the framework proposed in this paper can significantly improve the performance and computational efficiency of multiobjective optimization algorithms.
DOI: 10.5517/ccdc.csd.cc274s4b
title: CCDC 2060171: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274s5c
title: CCDC 2060172: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274s6d
title: CCDC 2060173: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274s7f
title: CCDC 2060174: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274s8g
title: CCDC 2060175: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274s9h
title: CCDC 2060176: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274sbj
title: CCDC 2060177: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274sck
title: CCDC 2060178: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274sdl
title: CCDC 2060179: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274sfm
title: CCDC 2060180: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274sgn
title: CCDC 2060181: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274shp
title: CCDC 2060182: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274sjq
title: CCDC 2060183: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274skr
title: CCDC 2060184: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274sls
title: CCDC 2060185: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274smt
title: CCDC 2060186: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274snv
title: CCDC 2060187: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274spw
title: CCDC 2060188: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc274sqx
title: CCDC 2060189: Experimental Crystal Structure Determination

description: Related Article: Steffen A. Föhrenbacher, Vivien Zeh, Mirjam J. Krahfuss, Nikolai V. Ignat'ev, Maik Finze, Udo Radius|2021|Eur.J.Inorg.Chem.|2021|1941|doi:10.1002/ejic.202100183
DOI: 10.5517/ccdc.csd.cc275cyr
title: CCDC 2060754: Experimental Crystal Structure Determination

description: Related Article: Carolin Hoyer, Peter Schwerk, Lisa Suntrup, Julia Beerhues, Maite Nössler, Uta Albold, Jens Dernedde, Karsten Tedin, Biprajit Sarkar|2021|Eur.J.Inorg.Chem.|2021|1373|doi:10.1002/ejic.202100024
DOI: 10.5517/ccdc.csd.cc275d0v
title: CCDC 2060756: Experimental Crystal Structure Determination

description: Related Article: Carolin Hoyer, Peter Schwerk, Lisa Suntrup, Julia Beerhues, Maite Nössler, Uta Albold, Jens Dernedde, Karsten Tedin, Biprajit Sarkar|2021|Eur.J.Inorg.Chem.|2021|1373|doi:10.1002/ejic.202100024
DOI: 10.5517/ccdc.csd.cc27669z
title: CCDC 2061540: Experimental Crystal Structure Determination

description: Related Article: Martin Jakubec, David Novák, Martina Zatloukalová, Ivana Císařová, Radek Cibulka, Ludovic Favereau, Jeanne Crassous, Adrianna Cytryniak, Renata Bilewicz, Jan Hrbáč, Jan Storch, Jaroslav Žádný, Jan Vacek|2021|ChemPlusChem|86|982|doi:10.1002/cplu.202100092
DOI: 10.5517/ccdc.csd.cc276wzb
title: CCDC 2062212: Experimental Crystal Structure Determination

description: Related Article: Sinem-Fatma Schmiel, Holger Butenschön|2021|Eur.J.Org.Chem.|2021|2388|doi:10.1002/ejoc.202100335
DOI: 10.5517/ccdc.csd.cc278l7c
title: CCDC 2063832: Experimental Crystal Structure Determination

description: Related Article: Eva Kran, Christian Mück-Lichtenfeld, Constantin G. Daniliuc, Armido Studer|2021|Chem.-Eur.J.|27|9281|doi:10.1002/chem.202101124
DOI: 10.5517/ccdc.csd.cc278l8d
title: CCDC 2063833: Experimental Crystal Structure Determination

description: Related Article: Eva Kran, Christian Mück-Lichtenfeld, Constantin G. Daniliuc, Armido Studer|2021|Chem.-Eur.J.|27|9281|doi:10.1002/chem.202101124
DOI: 10.5517/ccdc.csd.cc279ppy
title: CCDC 2064900: Experimental Crystal Structure Determination

description: Related Article: Ewelina I. Śliwa, Dmytro S. Nesterov, Marina V. Kirillova, Julia Kak, Alexander M. Kirillov, Piotr Smoleński|2021|Inorg.Chem.|60|9631|doi:10.1021/acs.inorgchem.1c00868
DOI: 10.5517/ccdc.csd.cc279pqz
title: CCDC 2064901: Experimental Crystal Structure Determination

description: Related Article: Ewelina I. Śliwa, Dmytro S. Nesterov, Marina V. Kirillova, Julia Kak, Alexander M. Kirillov, Piotr Smoleński|2021|Inorg.Chem.|60|9631|doi:10.1021/acs.inorgchem.1c00868
DOI: 10.5517/ccdc.csd.cc27cqt5
title: CCDC 2066857: Experimental Crystal Structure Determination

description: Related Article: Mehdi Elsayed Moussa, Martin Fleischmann, Gábor Balázs, Alexander V. Virovets, Eugenia Peresypkina, Pavel A. Shelyganov, Michael Seidl, Stephan Reichl, Manfred Scheer|2021|Chem.-Eur.J.|27|9742|doi:10.1002/chem.202101096
DOI: 10.5517/ccdc.csd.cc27cqw7
title: CCDC 2066859: Experimental Crystal Structure Determination

description: Related Article: Mehdi Elsayed Moussa, Martin Fleischmann, Gábor Balázs, Alexander V. Virovets, Eugenia Peresypkina, Pavel A. Shelyganov, Michael Seidl, Stephan Reichl, Manfred Scheer|2021|Chem.-Eur.J.|27|9742|doi:10.1002/chem.202101096
DOI: 10.5517/ccdc.csd.cc27bdkk
title: CCDC 2065578: Experimental Crystal Structure Determination

description: Related Article: Johnathan J. C. Lee, Chunyan Chi, Jishan Wu|2021|ChemPlusChem|86|836|doi:10.1002/cplu.202100098
DOI: 10.5517/ccdc.csd.cc27d7jf
title: CCDC 2067344: Experimental Crystal Structure Determination

description: Related Article: Nathan P. Bowling, Erin D. Speetzen, Eric Bosch|2021|ChemPlusChem|86|745|doi:10.1002/cplu.202100104
DOI: 10.5517/ccdc.csd.cc27ddmp
title: CCDC 2067502: Experimental Crystal Structure Determination

description: Related Article: Merlin Heß, Ivo Krummenacher, Theresa Dellermann, Holger Braunschweig|2021|Chem.-Eur.J.|27|9503|doi:10.1002/chem.202100795
DOI: 10.5517/ccdc.csd.cc27ddnq
title: CCDC 2067503: Experimental Crystal Structure Determination

description: Related Article: Merlin Heß, Ivo Krummenacher, Theresa Dellermann, Holger Braunschweig|2021|Chem.-Eur.J.|27|9503|doi:10.1002/chem.202100795
DOI: 10.5517/ccdc.csd.cc27ddpr
title: CCDC 2067504: Experimental Crystal Structure Determination

description: Related Article: Merlin Heß, Ivo Krummenacher, Theresa Dellermann, Holger Braunschweig|2021|Chem.-Eur.J.|27|9503|doi:10.1002/chem.202100795
DOI: 10.5517/ccdc.csd.cc27ddqs
title: CCDC 2067505: Experimental Crystal Structure Determination

description: Related Article: Merlin Heß, Ivo Krummenacher, Theresa Dellermann, Holger Braunschweig|2021|Chem.-Eur.J.|27|9503|doi:10.1002/chem.202100795
DOI: 10.5517/ccdc.csd.cc27ddrt
title: CCDC 2067506: Experimental Crystal Structure Determination

description: Related Article: Merlin Heß, Ivo Krummenacher, Theresa Dellermann, Holger Braunschweig|2021|Chem.-Eur.J.|27|9503|doi:10.1002/chem.202100795
DOI: 10.5517/ccdc.csd.cc27ddsv
title: CCDC 2067507: Experimental Crystal Structure Determination

description: Related Article: Merlin Heß, Ivo Krummenacher, Theresa Dellermann, Holger Braunschweig|2021|Chem.-Eur.J.|27|9503|doi:10.1002/chem.202100795
DOI: 10.5517/ccdc.csd.cc27ddtw
title: CCDC 2067508: Experimental Crystal Structure Determination

description: Related Article: Merlin Heß, Ivo Krummenacher, Theresa Dellermann, Holger Braunschweig|2021|Chem.-Eur.J.|27|9503|doi:10.1002/chem.202100795
DOI: 10.5517/ccdc.csd.cc27dt9s
title: CCDC 2067895: Experimental Crystal Structure Determination

description: Related Article: Toshikazu Ono, Kazuki Kimura, Megumi Ihara, Yuri Yamanaka, Miori Sasaki, Hirotoshi Mori, Yoshio Hisaeda|2021|Chem.-Eur.J.|27|9535|doi:10.1002/chem.202100906
DOI: 10.5517/ccdc.csd.cc27dtbt
title: CCDC 2067896: Experimental Crystal Structure Determination

description: Related Article: Toshikazu Ono, Kazuki Kimura, Megumi Ihara, Yuri Yamanaka, Miori Sasaki, Hirotoshi Mori, Yoshio Hisaeda|2021|Chem.-Eur.J.|27|9535|doi:10.1002/chem.202100906
DOI: 10.5517/ccdc.csd.cc27f4b5
title: CCDC 2068206: Experimental Crystal Structure Determination

description: Related Article: Alexander G. Harter, Thomas M. Klapötke, Christian Riedelsheimer, Jörg Stierstorfer, Michael Voggenreiter|2021|Eur.J.Inorg.Chem.|2021|2241|doi:10.1002/ejic.202100212
DOI: 10.5517/ccdc.csd.cc27f4c6
title: CCDC 2068207: Experimental Crystal Structure Determination

description: Related Article: Alexander G. Harter, Thomas M. Klapötke, Christian Riedelsheimer, Jörg Stierstorfer, Michael Voggenreiter|2021|Eur.J.Inorg.Chem.|2021|2241|doi:10.1002/ejic.202100212
DOI: 10.5517/ccdc.csd.cc27f4d7
title: CCDC 2068208: Experimental Crystal Structure Determination

description: Related Article: Alexander G. Harter, Thomas M. Klapötke, Christian Riedelsheimer, Jörg Stierstorfer, Michael Voggenreiter|2021|Eur.J.Inorg.Chem.|2021|2241|doi:10.1002/ejic.202100212
DOI: 10.5517/ccdc.csd.cc27f4f8
title: CCDC 2068209: Experimental Crystal Structure Determination

description: Related Article: Alexander G. Harter, Thomas M. Klapötke, Christian Riedelsheimer, Jörg Stierstorfer, Michael Voggenreiter|2021|Eur.J.Inorg.Chem.|2021|2241|doi:10.1002/ejic.202100212
DOI: 10.15468/xqqn34
title: A new species of the genus Mallomonas (Chrysophyceae: Synurales), Mallomonas kuzminii sp. nov., from lake Frolikha (Russia, Baikal region)

description: This dataset contains the digitized treatments in Plazi based on the original journal article Gusev, Evgeniy S., Kulikovskiy, Maxim S. (2013): A new species of the genus Mallomonas (Chrysophyceae: Synurales), Mallomonas kuzminii sp. nov., from lake Frolikha (Russia, Baikal region). Phytotaxa 155 (1): 66-70, DOI: 10.11646/phytotaxa.155.1.6, URL: http://dx.doi.org/10.11646/phytotaxa.155.1.6
DOI: 10.6084/m9.figshare.14873066
title: Insights into the phylogeny and transcriptional response of serine proteases in a halotolerant cyanobacterium <i>Halothece</i> sp. PCC7418

description: Serine proteases are a class of versatile proteolytic enzymes. They are necessary for protein catabolism, intracellular amino acid turnover, and regulation of proteins involved in diverse molecular and cellular processes across taxa. In this study, bioinformatic analyses revealed a significantly large number of serine proteases in the halotolerant cyanobacterium <i>Halothece</i> sp. PCC7418 (hereafter referred to as <i>Halothece</i> 7418) compared to the model freshwater cyanobacterium <i>Synechococcus elongatus</i> PCC7942 (hereafter referred to as <i>S. elongatus</i> 7942). The cyanobacterial serine proteases are likely derived from different linages since no conserved motifs were detected. The presence of highly diverse serine proteases in <i>Halothece</i> 7418 implicated an evolutionary-mediated modification of several proteases, which may play numerous physiological roles. We also examined the gene expression patterns of 34 serine protease encoding genes in <i>Halothece</i> 7418 exposed to salt stress. Our results revealed that several serine protease genes were drastically up–regulated under salt with high concentration but remained unchanged under salt with low concentration. All four <i>clp</i> genes (<i>H1996, H1997, H0950</i>, and <i>H3375</i>) and <i>H3553</i> gene (which encodes a putative HtrA protease) were significantly induced upon salt stress. These responses support the roles of the housekeeping pathways in both the degradation of damaged proteins induced by salt stress and regulation of proteins involved in the molecular recovery from salt stress. Since serine proteases share several biochemical features and physiological functions, the results from this study provide an insight into diversification of serine proteases in cyanobacteria. Further, these results will increase our understanding of several mechanisms at the subcellular level.
DOI: 10.6084/m9.figshare.14873066.v1
title: Insights into the phylogeny and transcriptional response of serine proteases in a halotolerant cyanobacterium <i>Halothece</i> sp. PCC7418

description: Serine proteases are a class of versatile proteolytic enzymes. They are necessary for protein catabolism, intracellular amino acid turnover, and regulation of proteins involved in diverse molecular and cellular processes across taxa. In this study, bioinformatic analyses revealed a significantly large number of serine proteases in the halotolerant cyanobacterium <i>Halothece</i> sp. PCC7418 (hereafter referred to as <i>Halothece</i> 7418) compared to the model freshwater cyanobacterium <i>Synechococcus elongatus</i> PCC7942 (hereafter referred to as <i>S. elongatus</i> 7942). The cyanobacterial serine proteases are likely derived from different linages since no conserved motifs were detected. The presence of highly diverse serine proteases in <i>Halothece</i> 7418 implicated an evolutionary-mediated modification of several proteases, which may play numerous physiological roles. We also examined the gene expression patterns of 34 serine protease encoding genes in <i>Halothece</i> 7418 exposed to salt stress. Our results revealed that several serine protease genes were drastically up–regulated under salt with high concentration but remained unchanged under salt with low concentration. All four <i>clp</i> genes (<i>H1996, H1997, H0950</i>, and <i>H3375</i>) and <i>H3553</i> gene (which encodes a putative HtrA protease) were significantly induced upon salt stress. These responses support the roles of the housekeeping pathways in both the degradation of damaged proteins induced by salt stress and regulation of proteins involved in the molecular recovery from salt stress. Since serine proteases share several biochemical features and physiological functions, the results from this study provide an insight into diversification of serine proteases in cyanobacteria. Further, these results will increase our understanding of several mechanisms at the subcellular level.