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Cells were collected by scraping and pelleted by centrifugation at 900 x g for 5 min at 4ºC. Cells were washed three times with 1X ice-cold PBS followed by permeabilization with 0.25% Triton X-100 in PBS for 30 min at RT. Cells were pelleted by centrifugation at 900 x g for 5 min at 4 ºC and washed with 0.5% BSA in 1X PBS. Cell pellets were resuspended in click reaction cocktails (20 μM biotin-azide, 2 mM CuSO4, 10 mM sodium L-ascorbate in 1X PBS), vortexed and incubated for 2 h at RT with rotation. For no-click negative control, biotin-azide was not included in the click reaction cocktails. Cells were pelleted by centrifugation at 900 x g for 5 min at 4 ºC and washed with 0.5% BSA in 1X PBS. Cell pellets were resuspended in lysis buffer (1% SDS in 50 mM Tris-HCl, pH 8.0) at a concentration of 100 X 106 cells per 4 ml and sonicated using a microtip sonicator (Branson 150) set at 35% amplitude with 5 pulses (20 S on and 40 S pause). Lysates were clarified twice by centrifugation at 16100 x g for 10 min at RT, filtered through an 80 µm nylon membrane (NY8004700, Millipore Sigma) and diluted 1:1 (v/v) with 1X ice-cold PBS containing protease inhibitors. Lysates were incubated with streptavidin agarose beads (69203, Millipore Sigma) at a concentration of 50 µl (packed volume) beads per 100 X 106 cells overnight at RT with rotation. Beads were washed once with cold lysis buffer, once with 1 M NaCl and final two washes with cold lysis buffer. Proteins were eluted by boiling the beads in 4X LDS sample buffer (NP0007, Thermo Scientific) at 95ºC, and iPOND purification was evaluated by either silver staining or Western blotting using antibodies for replication fork associated proteins.  Mass spectrometry analysis of iPOND purified protein samples was carried out in Taplin Biological Mass Spectrometry Facility, Harvard Medical School. Briefly, beads were washed at least five times with 100 µl 50 mM ammonium bicarbonate then 5 µl (200 ng/µl) of modified sequencing-grade trypsin (Promega, Madison, WI) was spiked in and the samples were placed in a 37ºC room overnight.  The samples were then centrifuged and the liquid removed.  The extracts were then dried in a speed-vac (~1 h).  Samples were re-suspended in 50 µl of HPLC solvent A (2.5% acetonitrile, 0.1% formic acid) and desalted by STAGE tip115. On the day of analysis, the samples were reconstituted in 10 µl of HPLC solvent A.  A nano-scale reverse-phase HPLC capillary column was created by packing 2.6 µm C18 spherical silica beads into a fused silica capillary (100 µm inner diameter x ~30 cm length) with a flame-drawn tip.  After equilibrating the column, each sample was loaded via a Famos auto sampler (LC Packings, San Francisco CA) onto the column.  A gradient was formed, and peptides were eluted with increasing concentrations of solvent B (97.5% acetonitrile, 0.1% formic acid).  As peptides eluted, they were subjected to electrospray ionization and then entered into a Velos Orbitrap Elite ion-trap mass spectrometer (Thermo Fisher Scientific, Waltham, MA).  Peptides were detected, isolated, and fragmented to produce a tandem mass spectrum of specific fragment ions for each peptide. Peptide sequences (and hence protein identity) were determined by matching protein databases with the acquired fragmentation pattern by the software program, Sequest (Thermo Fisher Scientific, Waltham, MA). All databases include a reversed version of all the sequences and the data was filtered to between a one and two percent peptide false discovery rate."],"repository":["Pride"],"labhead":["Roger A."],"instrument_platform":[""],"labhead_affiliation":["Department of Cancer Biology, University of Pennsylvania"],"submission_type":["COMPLETE"],"publication":["Not available"],"submitter_affiliation":["University of Pennsylvania"],"labhead_mail":["rogergr@pennmedicine.upenn.edu"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Disease Free"],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077767"],"modification":[""],"quantification_method":[""],"data_protocol":["Peptides were detected, isolated, and fragmented to produce a tandem mass spectrum of specific fragment ions for each peptide. Peptide sequences (and hence protein identity) were determined by matching protein databases with the acquired fragmentation pattern by the software program, Sequest (Thermo Fisher Scientific, Waltham, MA)117. All databases include a reversed version of all the sequences and the data was filtered to between a one and two percent peptide false discovery rate."],"omics_type":["Proteomics"],"species":["Homo Sapiens (human)"],"submitter_mail":["arindam.datta@pennmedicine.upenn.edu"],"submitter_country":["United States"],"doi":["10.6019/PXD077767"],"additional_accession":[]},"is_claimable":false,"name":"iPOND mass sepctrometry (iPOND-MS) in BRCA1-A complex deficient cells treated with CPT in combination with an ATM inhibitor","description":"iPOND Mass spectrometry (iPOND-MS) was performed to identify replication fork proteome in wild type (WT) and ABARAXAS KO (ABX KO) HEK293T cells treated with 1 µM CPT in combination with 250 nM ATM inhibitor (AZD0156). An additional set of control cells were kept for no-click (NC) negative control. The experiment was done with 5 repeats and the samples were designated as: WT/1, WT/2, WT/3, WT/4, WT/5, ABX KO/1, ABX KO/2, ABX KO/3, ABX KO/4, ABX KO/5, NC/1, NC/2, NC/3, NC/4, 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