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oai:figshare.com:article/33969994 2026-09-23T03:42:07Z category_4 category_915 category_7 category_8 category_12 category_13 category_14 category_734 category_64 portal_81 item_type_3 month_year_09_2026

Additional file 2 of A comprehensive proteome and the first phosphoproteome reveal extensive phosphorylation of carbohydrate metabolism in Cryptosporidium parvum sporozoites Dongqiang Wang (11828690) Meng Li (79487) Chenchen Wang (12690) Haitao Li (305080) Jigang Yin (142145) Guan Zhu (25093411) Biochemistry Physical Sciences not elsewhere classified Medicine Microbiology Cell Biology Genetics Molecular Biology Biological Sciences not elsewhere classified Cancer remains poorly understood public health importance based mass spectrometry parasite invasive stage obligate apicomplexan parasite relative phosphorylation index phosphoproteomics identified 8 highly abundant pathways predicted parasite proteome parvum sporozoites translate highly abundant parasite metabolism protein phosphorylation varied degrees translational level study reveals study aims representing 58 representing 36 phosphoproteomic profiles phosphoproteomic levels molecular regulation major cause intensity filtering independent acquisition graphical abstract functional regulation functional enrichment fermentative enzymes downstream analysis diarrheal disease cytoskeletal organization comparative assessment comparative analysis coding genes carbohydrate metabolism animals worldwide 833 phosphoproteins Supplementary material 2. Table S1. Abundance of excysted sporozoite proteome mapped to GenBank accession numbers and CryptoDB gene IDs. Table S2. Phosphorylation sites in peptides and mass spectrum signal intensities. Table S3. Motif logos at the Ser/S and Thr/T phosphorylated sites in Cryptosporidium parvum sporozoites and statistical parameters based on motif-x algorithm. Table S4. Merged phosphoproteome and proteome datasets with abundances, protein IDs and descriptions. In the phosphoproteome dataset, phosphopeptides with intensities lower than 400 were filtered to reduce potential contributions from low-intensity signals and non-specific peptide binding during immobilized metal affinity chromatography enrichment. Table S5. Enzymes in the glycolytic and connected pathways: proteome and phosphoproteome abundances, and relative phosphorylation index. 2026-07-02T05:00:00Z Dataset Dataset 10.6084/m9.figshare.33969994.v1 https://figshare.com/articles/dataset/Additional_file_2_of_A_comprehensive_proteome_and_the_first_phosphoproteome_reveal_extensive_phosphorylation_of_carbohydrate_metabolism_in_Cryptosporidium_parvum_sporozoites/33969994 CC BY + CC0