MassIVEapplication/xmlftp://massive-ftp.ucsd.edu/v04/MSV000088386/primary200OK0000Tyler EvansDietmar Kueltzhttps://massive.ucsd.edu/ProteoSAFe/dataset.jsp?task=7559b32c04e54d43b12d7affeb416047tyler.evans@csueastbay.edudkueltz@ucdavis.eduMassIVE98UNIMOD:21 - "Phosphorylation."UNIMOD:4 - "Iodoacetamide derivative."UNIMOD:23 - "Dehydration."UNIMOD:5 - "Carbamylation."UNIMOD:34 - "Methylation."UNIMOD:1 - "Acetylation."UNIMOD:35 - "Oxidation or Hydroxylation."Proteomicsimpact HDOstrea Lurida (ncbitaxon:627230)California State University East Bay, HaywardUniversity of California, Davisl(3)Ca, Procedures, Laboratory, AI461847, Peptidomics, AW549739, mCRY, L Isomer, 26S protease, d-titin, Spectrum Analyses, Mbh1, SLS, Sls, CG3629, DOI, Intervention or Procedure, Alkylations, ingensin, Techniques, method, large multicatalytic protease, biological_replicate, l(2)387, Method, HEL-S-66, method used in an experiment, Studies, Mass, DmelCG1915, Pgi, Titin, Crry, Analysis, Gpi-1, multicatalytic endopeptidase complex, Work Flow, anon-CREST, Technique, Ket, CFU-Mast, Mass Spectroscopy, l(3)j1D7, doi, C79691, Mass Spectrum Analysis, A, Art, Analyses, interventionDescription, Gpi-1r, Nlk, AFCP, Gpi-1s, Phi, beta-Trypsin, Gpi-1t, colony forming unit mast cell, Interventional, alanina, CG18857, ket, SURGICAL AND MEDICAL PROCEDURES, Ba, Lccp, Study, mKIAA0989, Alanine, l(3)dre8, lens neutral proteinase, Methodological Studies, sample, KZ, polyhedral organelle, l(3)rL182, ALA, AHUS2, TRA2.10, Mcp, MCP, 2.7, multicatalytic proteinase, NK/GPI, Gpi, Intervention Strategies, dl, Laboratory., titin, L Alanine, l(3)62Ca, L-Alanine, 0020/01, threonine endopeptidase activity, Procedure, MF, CG33075, L-Isomer, Amf, not genetically inherited, Spectrum Analysis, Abufène, Spectroscopy, 2-Aminopropionic acid, l(2)01092, kettin, Workflows, MS, CFU-MC, mOC-X, DmelCG3629, BcDNA:LP01770, NK|GPI, prosome, laboratory, L-Isomer Alanine, Mass Spectrum Analyses, NK, tricorn proteinase, D-titin, (L)-Alanine, Intervention, Mass Spectrum, Org, ORG, DLL, PRSS, Tripcellim, Spectrometry, Gpi1-r, Gpi1-s, MASCOT, 2-Aminopropanoic acid, Methodological, Alanin, D-Titin, MIC10, study protocol, Gpi1-t, Methodological Study, beta Trypsin, E(Arp), En(Arp), sample population, sam, sal, plan specification, TLX, Trypure, CG1915, biological replicate, dll, CG14208, CT41299, multicatalytic proteinase (complex), l(3)S002001, CG18242, tricorn protease, DmelCG14208, alkaline protease, Bglap-rs1, Work Flows, Gpi1s, CG18245, proteasome endopeptidase complex0PXD029757falseProteomic changes associated with predator induced morphological defenses in Olympia oystersSamples were collected and experiments performed by the laboratories of Tyler Evans and Eric Sanford. Samples represent a single biological replicate processed using an identical procedure, i.e., reduction/ alkylation and trypsin digestion as described in a previously published protocol (https://doi.org/10.1074/mcp.M113.029827). Data for each sample were acquired using regular bottom-up DDA proteomics. Biological mass spectrometry was performed and data analyzed using a workflow consisting of Compass Hystar 4.1, DataAnalysis 4.4, PEAKS Studio 8.5, Mascot 2.2.7, X!Tandem Alanine, and Scaffold 4.8 in the K&uumlltz laboratory.Mon Nov 15 19:27:00 GMT 2021MSV000088386