Prideapplication/xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210815_ZW_S1_2.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210813_ZW_S4_1.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210813_ZW_UUO5_1.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210813_ZW_UUO1_1.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210813_ZW_S5_1.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210815_ZW_UUO4_2.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210815_ZW_S5_2.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210813_ZW_S3_1.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210815_ZW_UUO5_2.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210815_ZW_S3_2.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210815_ZW_UUO1_2.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210813_ZW_UUO2_1.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210813_ZW_S2_1.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210815_ZW_S2_2.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210813_ZW_S1_1.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210813_ZW_UUO4_1.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210815_ZW_S4_2.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210815_ZW_UUO2_2.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210815_ZW_UUO3_2.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/20210813_ZW_UUO3_1.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/09/PXD029310/txt.rarprimaryOK200wzhou@cpu.edu.cnWei ZhouMass SpectrometryShotgun proteomicsMaxQuantMouse kidney tissueMouse kidney tissue; label-free quantitative proteomics; uuolabel-free quantitative proteomicsuuohttp://www.ebi.ac.uk/pride/archive/projects/PXD029310KidneyEach mouse kidney tissue was ground into powder in nitrogen, then lysis buffer (0.1 M Tris-HCL, pH 7.5, 4% SDS, 0.1 M DTT) was added, and the mixture was sonicated with 20 cycles of pulses (30 s each on/off, 80% power; CosmoSonic II Ultra Sonicator). After heating for 10 min at 95 oC, the lysate was centrifuged at 16,000 g for 20 min at room temperature. The protein concentrations were determined by measuring tryptophan fluorescence. 100 μg protein was digested by the FASP method as previously described.63 Each sample peptides was loaded onto a 20-cm column packed in-house with C18 3 μM ReproSil particles (Dr. Maisch GmbH), with an EASY-nLC 1200 system (Thermo Fisher Scientific) coupled to the mass spectrometer (Q Exactive Plus, Thermo Fisher Scientific). Colmn temperature was maintained at 50 oC. Peptides were separated with a 120 min gradient at a flow rate of 300 nL/min. Each sample was detected twice.PrideNot availableNo PTMs are included in the datasetThe raw data files were processed using software MaxQuant (http://www.maxquant.org.) version 1.6.2.10 with an FDR < 0.01 at the levels of proteins and peptides. The MS/MS spectra were searched against the Homo sapiens protein database in UniProt (January 2021). Bioinformatics analyses were carried out with R (https://www.r-project.org/) statistical computing software.ProteomicsWei ZhouQ Exactive PlusPARTIALState Key Laboratory of Natural Medicines, School of Traditional Chinese Pharmacy, China Pharmaceutical University, Nanjing 211198, ChinaMus Musculus (mouse)Not availablezhouwei19860506@163.comChina Pharmaceutical University, Nanjing 211198, ChinaChina4-Dithiothreitol, F10B6_15, rac-Dithiothreitol, chlorure d'hydrogene, threo-1, Powder, Cleland's reagent, classic hairy cell leukaemia, SDH, Hydrogenchlorid, protein, lysis, protein-containing complex, PMS Tryptophan, ratio-Tryptophan, body system, Tryptacin, L Tryptophan ratiopharm, F10B6.15, CG7826, Buffer, peptide, SDS, Polypeptides, protein polypeptide chains, method, ratio Tryptophan, hydrogen chloride, peptido, polypeptide chain, method used in an experiment, B1, CG7835, HCL-C, 1, CG42273, Min, Trofan, system, protein aggregate, Separated, cloruro de hidrogeno, Pulses, DmelCG42273, (R*, portion of tissue, Divorced, anatomical systems, peptides, Hydrogen chloride, PMS-Tryptophan, N, Tissue, min, 4733401P19Rik, mAPC, proteins, Divorces, 4-dithiothreitol, L-Tryptophan, 3R)-1, study assay, AI047805, Wasserstoffchlorid, lysate, hairy cell leukemia, column, SOLO DANCERS, Ardeydorm, scientific observation, sample, D1, peptidos, autolysin activity, necrosis, house mouse, PTHB1, reniculate kidney, Naturruhe, 3-butanediol, measuring, DYRK1, L-Tryptophan-ratiopharm, protein complex, mouse, Dmel_CG7826, AI836084, chloridohydrogen, 4-dimercapto-2, 4-disulfanylbutane-2, Tryptophan Metabolism Alterations, Mischung, classic hairy cell leukemia, buffer, Dithiothreitol, Peptide, Dithiotreitol, polypeptide, [HCl], any method, Temperatures, native protein, Stickstoff, Dm1, natural protein, Mus, C18, Protein, DL-threo-1, HCL, Chlorwasserstoff, Hydrochloride, tissue portion, bacteriocin activity, rel-(2R, simple tissue, Dyrk1, connected anatomical system, leukemic reticuloendotheliosis, L Tryptophan, Dmel_CG7835, DTL, Tryptan, Ardeytropin, Mnb, MNB, AU020952, Separation, DTT, holin, Levotryptophan, 3-diol, mice, Separations, HCl, CC1, Optimax, SWDS, azote, CGI-97, AW124434, lysed material, sample population, nitrogeno, ME-IV, Lyphan, plan specification, organ system, R*)-1, Kidneys, sample., nitrogen, lysin activity, bacteriolytic toxin activity, Peptid, Mouse, Polypeptide, 7N, chlorane, 4-Dimercapto-2, hydrochloric acidApplications Software, Gpi, Open Source, Bru, data, human being, Computer Software, Raw, AI461847, protein complex, Proteins, Gene, protein, Computer, MF, protein-containing complex, Amf, Source Softwares, Peptide, Software Tools, Tool, Programs, polypeptide, peptide, Program, Computer Applications, Polypeptides, protein polypeptide chains, Software Tool, mOC-X, native protein, peptido, natural protein, polypeptide chain, Computer Applications Software, Protein, Computer Applications Softwares, Gene Products, Pgi, Del(8)44H, Software Engineering, NK|GPI, Softwares, Gpi-1, protein aggregate, Software, Computer Program, tandem MS, Application, NK, Data Base, Svc, Open Source Softwares, ORG, Org, Software Applications, Col4a-1, peptides, Gpi-1r, Nlk, MS/MS, Source Software, Software Application, Gpi-1s, MS2, Open, Phi, Engineering, Gpi-1t, Open Source Software, Computer Programs and Programming, Gpi1-r, Gpi1-s, proteins, Gpi1-t, man, human, Computer Software Application, Protein Gene Products, Computer Programs, Gene Proteins, Applications, Applications Softwares, Tools, Computer Software Applications., Peptid, peptidos, Polypeptide, Bglap-rs1, Gpi1s, Computer Software Applications, NK/GPIprojections, Gene., 3.4.22.-, anatomical protrusion, Peptidomics, Laboratory, protein complex, lamellae, anatomical process, Mus domesticus, Proteins, number, mouse, lamina, flanges, Gene, mini-ICE, CASP-14, protein, protein-containing complex, presence, process of organ, House Mouse, protrusion, lamella, count in organism, protein polypeptide chains, salicylhydroxamate, native protein, natural protein, polypeptide chain, Mus, House, Protein, Mini-ICE, shelf, Gene Products, tissue portion, Mus musculus domesticus, simple tissue, protein aggregate, Mice, flange, organ process, portion of tissue, Mus musculus, study, Caspase-14 subunit p10, Swiss, mice, shelves, Tissue, Swiss Mouse, House Mice, Swiss Mice, proteins, Caspase-14 subunit p19, ridges, MICE, projection, free, ridge, Laboratory Mice, domesticus, Protein Gene Products, Gene Proteins, processes, process, Kidneys, SHAM, spine, papilla, renal fibrosis, kidney fibrosis, processus, Mouse, quantitative, house mouse, laminae, Laboratory Mouse, presence or absence in organism, reniculate kidneyportion of tissue, Kidneys, count in organism, salicylhydroxamate, Mus, Peptidomics, mice, Obstruction, number, mouse, tissue portion, Tissue, Ureteral Obstructions, Ureteral, Obstructions, Mouse, simple tissue, quantitative, house mouse, free, presence, SHAM., presence or absence in organism, reniculate kidneyfalseLabel-free quantitative proteomics for mouse kidney tissue of unilateral ureteral obstruction (UUO) vs Sham.Label-free quantitative proteomics for mouse kidney tissue of UUO vs Sham was used for discovery of differential expressed proteins in the process of renal fibrosis. Compared to sham mice, we found that 216 upregulated proteins and 215 downregulated proteins in UUO mice according to fold change ≥ 5, adjusted-p ≤ 0.01. Then, we will study the potential mechanism according to differential expressed 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