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Alpi"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Not available"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PRD000154"],"tissue":["Erythrocyte"],"sample_protocol":["Not available"],"repository":["Pride"],"quantification_method":["Not available"],"modification":["15.994915","57.021464"],"data_protocol":["Not available"],"omics_type":["Proteomics"],"labhead":["Emanuele Alpi"],"instrument_platform":["","LTQ-Orbitrap"],"labhead_affiliation":["Biological Mass Spectrometry Unit"],"submission_type":["PRIDE"],"species":["Homo Sapiens (human)"],"publication":["18399644 Simó C, Bachi A, Cattaneo A, Guerrier L, Fortis F, Boschetti E, Podtelejnikov A, Righetti PG; Performance of combinatorial peptide libraries in capturing the low-abundance proteome of red blood cells. 1. Behavior of mono- to hexapeptides., Anal Chem, 2008 May 15, 80, 10, 3547-56,  10.1021/ac702635v","18410134 Bachi A, Simó C, Restuccia U, Guerrier L, Fortis F, Boschetti E, Masseroli M, Righetti PG; Performance of combinatorial peptide libraries in capturing the low-abundance proteome of red blood cells. 2. Behavior of resins containing individual amino acids., Anal Chem, 2008 May 15, 80, 10, 3557-65,  10.1021/ac8001353"],"submitter_mail":["lcaph@aim.com"],"submitter_affiliation":["Biological Mass Spectrometry Unit"],"submitter_country":["United Kingdom"],"pubmed_abstract":["<h4>Unlabelled</h4>Sixteen different amino acids (Arg, Asn, Asp, Gln, Glu, Gly, His, Ile, Lys, Phe, Pro, Ser, Thr, Trp, Tyr, Val) have been separately linked to chromatographic beads and used for studying the mechanism of binding of such baits to proteins, as represented by the cytoplasmic proteome of the human red blood cell (RBC). The 16 different amino acid columns were confronted with equal amounts of RBC lysate, washed to remove unbound material, and eluted with denaturing agents. All eluates were analyzed by nanoLC-MS/MS.<h4>The results</h4>there appears to be a dichotomy between a class of \"Grand Catchers\" (Arg, His, Ile, Lys, Phe, Trp, Tyr, Val), all able to bind from 330 up to 441 unique gene products, and the \"Petite Catchers\" (Asn, Asp, Gln, Glu, Gly, Pro, Ser, Thr), that bind in general half as much, with the notable exception of Glu that under the described conditions seems to bind only traces of proteins. By comparing homogeneous classes of amino acids (e.g., the basic, the hydrophobic aromatic, the neutral hydrophilic, etc.), it is found that, in general, more than half as many proteins are held in common among the members of each family. In a 16-way comparison, 72 proteins (less than 10% of the total amount, which amounts to 800 unique, nonredundant, identified proteins) appear to be the common catch of all 16 amino acids, suggesting that such proteins might have either multiple binding sites or general motifs recognized by any generic bait. By far, it would appear that the strongest interactions and thus the strongest catches occur with the three aromatic moieties of Phe, Trp, and Tyr, all able to capture a practically identical number of proteins. Ionic interactions, which in principle should be the strongest ones, appear to behave in a peculiar way: they are quite strong with the three basic amino acids (Arg, His, Lys) but almost inexistent with their acidic counterparts. This suggests a peculiar mechanism of interaction: upon formation of the ion pair, the linkage between the protein and the bait is stabilized by the hydrophobicity of the underlying chain (e.g., a butyl in the case of Lys).","<h4>Unlabelled</h4>For a better understanding of the behavior of solid-phase combinatorial peptide ligands for capturing the red blood cell low-abundance soluble proteome, combinatorial peptides of different lengths from a single amino acid up to a hexapeptide were evaluated. A red blood cell lysate (6 g total protein) was loaded in a cascade fashion to the six columns, which were individually eluted with 8 M urea, 2% 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (v/w), and 50 mM citric acid. Each eluate was analyzed via sodium dodecyl sulfate polyacrylamide gel electrophoresis, two-dimensional maps, and nanoLC-MS/MS.<h4>The results</h4>mixed beads with a single amino acid attached showed the capture of a non-negligible portion of the proteome. A progressive increasing of the length of the peptide bait enlarges the pool of captured proteins. Above a length of four amino acids, a plateau is progressively reached, suggesting that not much could be gained with baits longer than six amino acids. Interestingly, whereas the beads laden with a single amino acid seem to be able to capture large-size proteins (>40 kDa), beads with progressively longer peptides capture additional proteins in the smaller size range (10-50 kDa). This suggests that interactions already begin with a single amino acid, but selectivity requires baits of proper length, at least above four amino acids. Plain beads, with a spacer arm carrying a primary amino terminal group for anchoring the baits, are essentially unable to capture proteins, suggesting that the peptide baits do not act by a mechanism of ion exchange but rather via a complex mixed mode, yielding a specific capture."],"pubmed_title":["Performance of combinatorial peptide libraries in capturing the low-abundance proteome of red blood cells. 1. Behavior of mono- to hexapeptides.","Performance of combinatorial peptide libraries in capturing the low-abundance proteome of red blood cells. 2. Behavior of resins containing individual amino acids."],"pubmed_authors":["Bachi Angela A, Simó Carolina C, Restuccia Umberto U, Guerrier Luc L, Fortis Frederic F, Boschetti Egisto E, Masseroli Marco M, Righetti Pier Giorgio PG","Simó Carolina C, Bachi Angela A, Cattaneo Angela A, Guerrier Luc L, Fortis Frederic F, Boschetti Egisto E, Podtelejnikov Alexander A, Righetti Pier Giorgio PG"],"pubmed_title_synonyms":["DYRK5, Pfeiffer's disease (disorder), cou, Process, Processes, Blood, total expressed protein, Mononucleosis, Tl3, Tl2, Peptide, Cell, HMG-CoAR, CSA2, Acceptance Processes, polypeptide, peptide, Polypeptides, Acceptance Process, Lr, Mono, peptido, Corpuscles, Kissing disease, Low, Blood Corpuscle, Library, Gammaherpesviral mononucleosis (disorder), Acceptance, hYAK3-2, Blood Cell, me75, peptides, Glandular Fever, mononucleosis, D17Mit170, REDK, T1, Corpuscle, glandular fever, Infectious Mononucleosis, Pfeiffer's disease, Cells, Monocytic angina, Filatov's disease, Bra, RED, Red, monocytic angina, Peptid, peptidos, Polypeptide, Blood Corpuscles, Glandular fever, Gammaherpesviral mononucleosis, Behaviors, Proteomes, infectious mononucleosis., single-organism behavior"],"sample_synonyms":["Not Available, Unavailable."],"description_synonyms":["Human, humans., assay, human being, Man (Taxonomy), Homo sapiens, determination, Man, human, Modern Man, chemical analysis, Modern"],"pubmed_abstract_synonyms":["Voltage-gated calcium channel subunit alpha Cav1.2, DmGluClalpha, Materials, Kinship, ion, ARMD9, SMC4, AI326280, Glu, GLU, RBC, l(3)61Ea, Sialic acid-binding Ig-like lectin 1, Azemiopinae, P150, 2-amino-3-(1H-indol-3-yl)propanoic acid, CG17228, P270, glc, DmelCG6383, Hydrophobic Interactions, 1135/09, 1135/07, actin-dependent regulator of chromatin subfamily F member 1, protein polypeptide chains, DmGluT1, 2-Aminoglutaric acid, Tyrosinase-related protein 1, Calcium channel, p150, 0451/09, glu, Life Cycle, sry-beta, SER, strong, D, 0244/09, (S)-2-amino-5-guanidinopentanoic acid, E, amino acids, DmelCG6127, Htrp, Kinship Network, K, red blood corpuscle, anabolism, 2-amino-3-(4-hydroxyphenyl)propanoic acid, 3-(p-Hydroxyphenyl)alanine, DmGLUT1, DROPROSA, R, As, crumb, proteins, Catalase B, W, DrosGluCl, Y, THR, Thr, a, 671/2, ser, Bd, c, ACF, AHUS5, Acf, ch, LYS, Lys, CG10728, Complement C3f fragment, Lysin, Red, GLUCL, ELD, hAPG5, Dm Asp, Lzm, GluCl, hOSA1, Lzp, eye-lt-m03Jus-gt-, C3bc, CG13908, arginine, Red Blood Cell, A-lt-y-gt-, alpha-amino carboxylic acids, 0074/12, Interaction, European, 1316/02, 1.14.18.-, anon-96Aa, BcDNA:HL08040, Red Blood Corpuscle, CG18104, DmelCG7535, red blood cell count, Acid, OCA3, ASIP, DL-Asparagic acid, Amino acids, DmelCG43946, Dm-GluCl, C3a anaphylatoxin, TLF, 1167/13, OSA1, INSDC_feature:gene, alpha, Hydrophilic Interaction, Agouti switch protein, tryptophane, Tlp, Sheep erythrocyte receptor, CG107278, human, 2-aminobutanedioic acid, AW011832, Lysm, HEL-S-62p, Red Blood Cells, Material, 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Complement C3d fragment, t1, dGluCl-alpha, Family Life Cycle, multicellular organismal biosynthetic process, ARP, sry alpha, single-organism biosynthetic process, mKIAA0458, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, PPG, 1810073H04Rik, Man (Taxonomy), BcDNA:HL07853, MUB3_18, Hydrophobicity, ATN1L, Melanoma antigen gp75, (S)-2-Amino-5-guanidinovaleric acid, epsilon-diaminocaproic acid, arg, Complement C3dg fragment, MUB3.18, l(3)j6E2, SN, ASP, Hydrophobic Interaction, Asp, Dmglut1, DmSMC4, 0320/10, DMPROSPER, (+-)-Aspartic acid, Tyr, Sa, TRP-1, CG7535, Glutaminic acid, Family Life Cycles, Complement C3c alpha' chain fragment 1, Complement C3c alpha' chain fragment 2, HAT, D18347, L-Arginin, DrosGlu-Cl-alpha, APG5-LIKE, AI255234, l(3)rO534, CG6383, PRO, Pro, Aminokarbonsaeure, Modern, EG:171D11.4, 2-Amino-3-(p-hydroxyphenyl)propionic acid, Osa homolog 1, Brown locus protein, CYS, results, Binding, APOBEC1CF, Hydrophilic, PROS-1, PROS-2, Ionen, pro, p150/Glued, Genetic Materials, B120, Lzm-s1, Filiation, and GLY protein 2, DYNA_DROME, Genetic Material, OCAIA, CG11397, alpha-Amino-beta-(3-indolyl)-propionic acid, SHEP3, Amino Acid, Blood Cell, and GLY protein 1, Voila, MS/MS, Srybeta, erythrocyte number, red blood cell, 0664/07, common, TAF[[II]], C3-beta-c, BcDNA.LD20207, Life Cycles, GLP-1, Red Blood Corpuscles, CG17957, beta-3-indolylalanine, Erythrocyte, CG6127, anon-WO0118547.279, Cistron, Sry alpha, anon-WO0118547.156, Blood Corpuscles, isoform 1, Proteomes, l(3)S050920, P150[Glued], DL-Glutamic acid, VAL, CAS2, human being, Family Member, l(3)S007412, Aminocarbonsaeure, CG9206, Gene, sryalpha, far, Network, alpha-amino acid, Complement C3 beta chain, Complement C3 alpha chain, L-(+)-arginine, l(3)10419, val, dmTAF8, hELD, l(3)rQ526, dSMC4, (2S)-2-amino-5-(carbamimidamido)pentanoic acid, Homo sapiens, resilient, polypeptide chain, mel(3)8, Adder, SWI-like protein, HL-VIII, anon-WO0140519.15, F15E12.6, Hydrophilicity, Basic Amino Acid, l(3)j5E11, Site, PROS, 0585/13, Sryalpha, Genetic, DmelCG11397, Research, formation, Gm17754, MS2, iones, 1384/04, CG7128, CATB, AW742570, prod, Combining Site, DrosGluCl-alpha, alpha-amino-beta-3-indolepropionic acid, lysate, CMM8, DmAos, Kinship Networks, TAF, 0563/18, Family, l(3)j1B5, protein complex, TRF2, 4732475G08, total expressed protein, Binding Site, Cistrons, cardiac muscle, l(3)rJ806, Pros, l(3)07207, l(3)rJ812, TYRP, OCA1A, DmelCG9206, natural protein, European Viper, p150[glued], Protein, TFIID, glut1, l(3)S058104, MCPH5, AI414665, tandem MS, Blood Cells, Basic, sry-a, C1orf4, 2-aminopentanedioic acid, sry-b, gil, FCP-D, Amino, alpha-1 polypeptide, l(2)k08819, Protein Gene Products, sry-alpha, CG43946, DmelCG7128, BRG1-associated factor 250a, Ion, 38B.5, Modern Man, cardinality, AA536808, TAF8, DmelCG17957"],"data_synonyms":["Not Available, Unavailable."],"name_synonyms":["DYRK5, Voltage-gated calcium channel subunit alpha Cav1.2, red blood cell count, hYAK3-2, Blood Cell, me75, cou, peptides, red blood corpuscle, erythrocyte number, Blood, red blood cell, RBC, total expressed protein, alpha-1 polypeptide, Tl3, Rat brain class C, Tl2, D17Mit170, REDK, cardiac muscle, Peptide, T1, Cell, HMG-CoAR, CSA2, polypeptide, peptide, Polypeptides, Corpuscle, Lr, L type, peptido, Calcium channel, Cells, Bra, RED, Red, Blood Corpuscle., Corpuscles, Peptid, peptidos, Polypeptide, Low, Blood Corpuscles, isoform 1, Library, Proteomes"],"additional_accession":[]},"is_claimable":false,"name":"RBC -  Performance of combinatorial peptide libraries in capturing the low-abundance proteome of red blood cells","description":"GeLC-MS/MS analysis of human RBCs","dates":{"publication":"2009-12-01","submission":"2009-10-01"},"accession":"PRD000154","cross_references":{"TAXONOMY":["NEWT:68239","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:2003758","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:9900","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:9979","NEWT:130821","NEWT:2320211","NEWT:27606","NE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