taxonID	type	format	identifier	references	title	description	created	creator	contributor	publisher	audience	source	license	rightsHolder	datasetID
BB74B629FFE1FFCCE651FB9904586981.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8293510/files/figure.png	https://doi.org/10.5281/zenodo.8293510	Fig. 1. Protein length distribution in the G. sinense proteome.	Fig. 1. Protein length distribution in the G. sinense proteome.	2020-11-30	Zheng, Sheng;Zhu, Ning;Shi, Cheng;Zheng, Heng		Zenodo	biologists	Zheng, Sheng;Zhu, Ning;Shi, Cheng;Zheng, Heng			
BB74B629FFE1FFCCE651FB9904586981.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8293512/files/figure.png	https://doi.org/10.5281/zenodo.8293512	Fig. 2. Experimental flowchart. (A) Blast search and alignment of G. sinense proteins with known anticancer peptides. (B) An example of a Hit sequence. (C) Hit sequences were cleaved by in silico enzyme digestion of trypsin. (D) The digested fragments were screened by mACPpred, an SVM-based algorithm, to identify putative ACPs. (E) The resulting peptides were then subjected to sequence comparison to known ACPs.	Fig. 2. Experimental flowchart. (A) Blast search and alignment of G. sinense proteins with known anticancer peptides. (B) An example of a Hit sequence. (C) Hit sequences were cleaved by in silico enzyme digestion of trypsin. (D) The digested fragments were screened by mACPpred, an SVM-based algorithm, to identify putative ACPs. (E) The resulting peptides were then subjected to sequence comparison to known ACPs.	2020-11-30	Zheng, Sheng;Zhu, Ning;Shi, Cheng;Zheng, Heng		Zenodo	biologists	Zheng, Sheng;Zhu, Ning;Shi, Cheng;Zheng, Heng			
BB74B629FFE1FFCCE651FB9904586981.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8293514/files/figure.png	https://doi.org/10.5281/zenodo.8293514	Fig. 3. The number of parent proteins containing putative ACPs.	Fig. 3. The number of parent proteins containing putative ACPs.	2020-11-30	Zheng, Sheng;Zhu, Ning;Shi, Cheng;Zheng, Heng		Zenodo	biologists	Zheng, Sheng;Zhu, Ning;Shi, Cheng;Zheng, Heng			
BB74B629FFE1FFCCE651FB9904586981.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8293516/files/figure.png	https://doi.org/10.5281/zenodo.8293516	Fig. 4. Length distributions of cleaved peptides. The parent proteins were cleaved by in silico enzyme digestion with trypsin. The length distributions of peptides between 7 and 19 amino acids in length are shown.	Fig. 4. Length distributions of cleaved peptides. The parent proteins were cleaved by in silico enzyme digestion with trypsin. The length distributions of peptides between 7 and 19 amino acids in length are shown.	2020-11-30	Zheng, Sheng;Zhu, Ning;Shi, Cheng;Zheng, Heng		Zenodo	biologists	Zheng, Sheng;Zhu, Ning;Shi, Cheng;Zheng, Heng			
BB74B629FFE1FFCCE651FB9904586981.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8293518/files/figure.png	https://doi.org/10.5281/zenodo.8293518	Fig. 5. Energy change in 100-ns molecular dynamic simulation of putative ACPs P14 and P15 (trypsin-digested fragments from parent proteins No. 14 and 15 in the G. sinense proteome). Molecular dynamic simulation was performed by AMBER14.	Fig. 5. Energy change in 100-ns molecular dynamic simulation of putative ACPs P14 and P15 (trypsin-digested fragments from parent proteins No. 14 and 15 in the G. sinense proteome). Molecular dynamic simulation was performed by AMBER14.	2020-11-30	Zheng, Sheng;Zhu, Ning;Shi, Cheng;Zheng, Heng		Zenodo	biologists	Zheng, Sheng;Zhu, Ning;Shi, Cheng;Zheng, Heng			
BB74B629FFE1FFCCE651FB9904586981.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8293520/files/figure.png	https://doi.org/10.5281/zenodo.8293520	Fig. 6. Three-dimensional structures of P14 and P15, shown in cartoon representation; red represents α-helix, yellow represents β-sheet, and blue represents turn structure. Structures were extracted from the trajectory of molecular dynamic simulation from 20 ns to 100 ns. The lowest energy conformation is presented. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)	Fig. 6. Three-dimensional structures of P14 and P15, shown in cartoon representation; red represents α-helix, yellow represents β-sheet, and blue represents turn structure. Structures were extracted from the trajectory of molecular dynamic simulation from 20 ns to 100 ns. The lowest energy conformation is presented. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)	2020-11-30	Zheng, Sheng;Zhu, Ning;Shi, Cheng;Zheng, Heng		Zenodo	biologists	Zheng, Sheng;Zhu, Ning;Shi, Cheng;Zheng, Heng			
