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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1449 [new locus tag: SACOL_RS07390 ]
  • pan locus tag?: SAUPAN003831000
  • symbol: sucA
  • pan gene symbol?: sucA
  • synonym:
  • product: 2-oxoglutarate dehydrogenase E1 component

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1449 [new locus tag: SACOL_RS07390 ]
  • symbol: sucA
  • product: 2-oxoglutarate dehydrogenase E1 component
  • replicon: chromosome
  • strand: -
  • coordinates: 1460973..1463771
  • length: 2799
  • essential: unknown other strains

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    541
    601
    661
    721
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    1261
    1321
    1381
    1441
    1501
    1561
    1621
    1681
    1741
    1801
    1861
    1921
    1981
    2041
    2101
    2161
    2221
    2281
    2341
    2401
    2461
    2521
    2581
    2641
    2701
    2761
    ATGACTAACGAAAGAAAAGAAGTTTCAGAGGCTCCTGTAAACTTCGGTGCGAATTTAGGT
    CTAATGTTAGATCTATATGATGACTTTTTACAAGATCCATCATCTGTACCAGAAGATTTA
    CAAGTCTTATTCAGCACAATTAAGAATGATGACTCAATTGTACCAGCTTTAAAAAGTACA
    AGTAGTCAAAATAGCGACGGCACAATTAAGCGTGTCATGCGTTTAATTGATAATATTCGC
    CAATACGGGCATCTTAAAGCCGATATTTATCCTGTAAATCCTCCAAAAAGGAAACATGTA
    CCTAAATTAGAGATTGAAGACTTTGATTTAGATCAACAGACTTTGGAAGGTATATCAGCA
    GGAATTGTTTCAGATCACTTTGCCGACATTTATGATAATGCTTATGAAGCAATTTTAAGA
    ATGGAAAAACGTTACAAAGGACCAATTGCATTTGAGTATACACATATTAATAACAATACC
    GAACGTGGTTGGTTAAAAAGAAGAATTGAAACGCCATATAAAGTAACGTTAAATAATAAC
    GAAAAAAGGGCACTATTCAAACAATTAGCGTATGTTGAAGGGTTTGAAAAATATCTTCAT
    AAAAACTTCGTTGGTGCAAAGCGTTTTTCAATTGAAGGGGTAGACGCACTTGTACCGATG
    TTACAACGTACTATTACGATTGCTGCGAAAGAAGGTATTAAAAATATACAAATAGGCATG
    GCTCACCGTGGACGTTTAAACGTTTTAACGCATGTCTTAGAAAAACCGTACGAAATGATG
    ATTTCAGAATTTATGCATACAGATCCAATGAAATTCTTACCTGAAGATGGTAGCTTGCAG
    TTAACTGCTGGATGGACTGGTGATGTGAAATATCACCTTGGTGGCATTAAAACTACTGAT
    TCATACGGTACAATGCAGCGTATTGCACTGGCTAACAATCCAAGTCACTTGGAAATTGTT
    GCACCTGTTGTTGAGGGGCGTACGAGAGCAGCACAAGATGATACACAACGAGCTGGGGCT
    CCGACGACTGATCATCATAAAGCAATGCCAATTATTATACATGGCGATGCTGCTTATCCT
    GGTCAAGGAATTAACTTCGAAACAATGAACTTAGGAAACTTGAAAGGCTATTCTACGGGT
    GGTTCATTGCATATTATTACTAACAATAGAATTGGATTTACTACAGAACCAATTGATGCA
    CGTTCAACAACTTATTCTACAGATGTGGCCAAAGGTTATGATGTGCCAATATTCCATGTC
    AATGCAGATGACGTTGAAGCTACTATTGAAGCAATTGATATTGCAATGGAATTTAGAAAA
    GAGTTTCATAAAGACGTCGTTATTGATTTAGTAGGTTATCGTCGTTTCGGACATAACGAA
    ATGGATGAACCATCAATTACTAATCCAGTTCCTTATCAGAATATTCGCAAACATGACTCT
    GTTGAATATGTGTTTGGTAAAAAGCTTGTTAATGAAGGTGTCATTTCAGAAGATGAAATG
    CATTCATTTATAGAACAAGTCCAAAAGGAACTAAGACAAGCTCATGATAAAATTAATAAA
    GCTGATAAAATGGATAATCCAGATATGGAAAAGCCTGCAGATCTTGCATTACCGTTACAA
    GCAGACGAACAATCATTTACTTTTGATCACTTGAAAGAAATAAATGATGCATTGTTAACA
    TATCCGGATGGCTTTAACATTTTGAAAAAGTTAAACAAAGTTCTTGAGAAGCGTCATGAG
    CCGTTTAATAAAGAAGATGGTTTAGTTGATTGGGCACAAGCAGAACAACTTGCATTTGCG
    ACAATTTTACAAGATGGTACACCGATTCGCTTAACTGGTCAAGATAGTGAACGTGGTACA
    TTCAGTCATAGGCATGCCGTGTTACATGATGAGCAAACAGGTGAAACATATACACCTTTA
    CATCATGTTCCTGATCAAAAAGCGACATTTGATATACACAATTCTCCGCTTTCAGAAGCA
    GCAGTAGTTGGTTTTGAATACGGCTATAATGTGGAAAACAAAAAAAGCTTCAATATTTGG
    GAAGCACAATATGGTGATTTTGCAAATATGTCACAAATGATTTTTGACAACTTCTTATTC
    AGTTCTCGCTCAAAATGGGGAGAACGTTCAGGATTAACATTATTCTTACCTCATGCATAT
    GAGGGTCAAGGGCCTGAACATTCATCAGCAAGATTAGAGCGATTTTTACAATTAGCTGCT
    GAAAATAATTGCACAGTTGTCAACTTATCTAGTTCAAGTAATTATTTCCACTTATTGCGT
    GCACAAGCGGCTAGTTTAGATTCTGAACAAATGCGACCATTGGTTGTTATGTCACCAAAA
    AGCTTACTGAGAAATAAAACAGTTGCAAAACCAATTGATGAATTTACTTCTGGTGGATTT
    GAGCCAATTTTGACAGAATCATATCAAGCGGATAAGGTTACAAAAGTTATTTTGGCAACT
    GGTAAAATGTTCATTGATTTAAAAGAAGCATTAGCTAAAAATCCAGACGAATCAGTATTA
    CTCGTTGCGATTGAAAGATTGTATCCATTCCCAGAGGAAGAGATTGAAGCATTACTAGCA
    CAATTGCCAAACCTTGAAGAAGTGTCATGGGTACAAGAAGAACCTAAAAATCAAGGTGCA
    TGGTTATATGTCTATCCATATGTTAAAGTGCTAGTTGCAGATAAATATGATTTAAGTTAT
    CATGGCAGAATTCAAAGGGCTGCTCCAGCTGAAGGCGATGGAGAAATTCATAAACTTGTT
    CAAAATAAAATTATAGAAAATGCATTAAAAAATAACTAG
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1380
    1440
    1500
    1560
    1620
    1680
    1740
    1800
    1860
    1920
    1980
    2040
    2100
    2160
    2220
    2280
    2340
    2400
    2460
    2520
    2580
    2640
    2700
    2760
    2799

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1449 [new locus tag: SACOL_RS07390 ]
  • symbol: SucA
  • description: 2-oxoglutarate dehydrogenase E1 component
  • length: 932
  • theoretical pI: 5.40096
  • theoretical MW: 105342
  • GRAVY: -0.469957

⊟Function[edit | edit source]

  • reaction:
    EC 1.2.4.2?  ExPASy
    Oxoglutarate dehydrogenase (succinyl-transferring) 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
  • TIGRFAM:
    Metabolism Energy metabolism TCA cycle oxoglutarate dehydrogenase (succinyl-transferring), E1 component (TIGR00239; EC 1.2.4.2; HMM-score: 1033.1)
    and 2 more
    Metabolism Energy metabolism Pyruvate dehydrogenase pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit (TIGR03182; EC 1.2.4.1; HMM-score: 52.6)
    Metabolism Energy metabolism Pyruvate dehydrogenase pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit (TIGR03181; EC 1.2.4.1; HMM-score: 31.3)
  • TheSEED  :
    • 2-oxoglutarate dehydrogenase E1 component (EC 1.2.4.2)
    Carbohydrates Central carbohydrate metabolism Dehydrogenase complexes  2-oxoglutarate dehydrogenase E1 component (EC 1.2.4.2)
    and 1 more
    Carbohydrates Central carbohydrate metabolism TCA Cycle  2-oxoglutarate dehydrogenase E1 component (EC 1.2.4.2)
  • PFAM:
    THDP-binding (CL0254) E1_dh; Dehydrogenase E1 component (PF00676; HMM-score: 221.4)
    Transket_pyr; Transketolase, pyrimidine binding domain (PF02779; HMM-score: 180.2)
    and 5 more
    TKC_like (CL0591) OxoGdeHyase_C; 2-oxoglutarate dehydrogenase C-terminal (PF16870; HMM-score: 117.1)
    no clan defined 2-oxogl_dehyd_N; 2-oxoglutarate dehydrogenase N-terminus (PF16078; HMM-score: 20.7)
    B_GA (CL0598) DUF1542; Domain of Unknown Function (DUF1542) (PF07564; HMM-score: 13.2)
    no clan defined T3SS_HrpK1; Type III secretion system translocator protein, HrpF (PF16937; HMM-score: 13.2)
    DUF1840; Domain of unknown function (DUF1840) (PF08895; HMM-score: 12.7)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors: thiamine diphosphate
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.95
    • Cytoplasmic Membrane Score: 0.05
    • Cellwall Score: 0
    • Extracellular Score: 0
    • Internal Helices: 0
  • LocateP: Intracellular
    • Prediction by SwissProt Classification: Cytoplasmic
    • Pathway Prediction: No pathway
    • Intracellular possibility: 1
    • Signal peptide possibility: -1
    • N-terminally Anchored Score: 1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.002478
    • TAT(Tat/SPI): 0.000638
    • LIPO(Sec/SPII): 0.000551
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MTNERKEVSEAPVNFGANLGLMLDLYDDFLQDPSSVPEDLQVLFSTIKNDDSIVPALKSTSSQNSDGTIKRVMRLIDNIRQYGHLKADIYPVNPPKRKHVPKLEIEDFDLDQQTLEGISAGIVSDHFADIYDNAYEAILRMEKRYKGPIAFEYTHINNNTERGWLKRRIETPYKVTLNNNEKRALFKQLAYVEGFEKYLHKNFVGAKRFSIEGVDALVPMLQRTITIAAKEGIKNIQIGMAHRGRLNVLTHVLEKPYEMMISEFMHTDPMKFLPEDGSLQLTAGWTGDVKYHLGGIKTTDSYGTMQRIALANNPSHLEIVAPVVEGRTRAAQDDTQRAGAPTTDHHKAMPIIIHGDAAYPGQGINFETMNLGNLKGYSTGGSLHIITNNRIGFTTEPIDARSTTYSTDVAKGYDVPIFHVNADDVEATIEAIDIAMEFRKEFHKDVVIDLVGYRRFGHNEMDEPSITNPVPYQNIRKHDSVEYVFGKKLVNEGVISEDEMHSFIEQVQKELRQAHDKINKADKMDNPDMEKPADLALPLQADEQSFTFDHLKEINDALLTYPDGFNILKKLNKVLEKRHEPFNKEDGLVDWAQAEQLAFATILQDGTPIRLTGQDSERGTFSHRHAVLHDEQTGETYTPLHHVPDQKATFDIHNSPLSEAAVVGFEYGYNVENKKSFNIWEAQYGDFANMSQMIFDNFLFSSRSKWGERSGLTLFLPHAYEGQGPEHSSARLERFLQLAAENNCTVVNLSSSSNYFHLLRAQAASLDSEQMRPLVVMSPKSLLRNKTVAKPIDEFTSGGFEPILTESYQADKVTKVILATGKMFIDLKEALAKNPDESVLLVAIERLYPFPEEEIEALLAQLPNLEEVSWVQEEPKNQGAWLYVYPYVKVLVADKYDLSYHGRIQRAAPAEGDGEIHKLVQNKIIENALKNN

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 581 [5]
  • interaction partners:
    SACOL0452(ahpC)alkyl hydroperoxide reductase subunit C  [6] (data from MRSA252)
    SACOL0557(cysK)cysteine synthase  [6] (data from MRSA252)
    SACOL2130(deoD)purine nucleoside phosphorylase  [6] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [6] (data from MRSA252)
    SACOL0634(eutD)phosphotransacetylase  [6] (data from MRSA252)
    SACOL1782(fhs)formate--tetrahydrofolate ligase  [6] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [6] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [6] (data from MRSA252)
    SACOL1734(gapA2)glyceraldehyde 3-phosphate dehydrogenase 2  [6] (data from MRSA252)
    SACOL1961(gatA)aspartyl/glutamyl-tRNA amidotransferase subunit A  [6] (data from MRSA252)
    SACOL1960(gatB)aspartyl/glutamyl-tRNA amidotransferase subunit B  [6] (data from MRSA252)
    SACOL1622(glyS)glycyl-tRNA synthetase  [6] (data from MRSA252)
    SACOL1554(gnd)6-phosphogluconate dehydrogenase  [6] (data from MRSA252)
    SACOL2016(groEL)chaperonin GroEL  [6] (data from MRSA252)
    SACOL0460(guaB)inosine-5'-monophosphate dehydrogenase  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL1206(ileS)isoleucyl-tRNA synthetase  [6] (data from MRSA252)
    SACOL1477(ilvA1)threonine dehydratase  [6] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [6] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [6] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [6] (data from MRSA252)
    SACOL0966(pgi)glucose-6-phosphate isomerase  [6] (data from MRSA252)
    SACOL0839(pgk)phosphoglycerate kinase  [6] (data from MRSA252)
    SACOL1091(ptsH)phosphocarrier protein HPr  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [6] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [6] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [6] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [6] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL2212(rplQ)50S ribosomal protein L17  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1725(rplT)50S ribosomal protein L20  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [6] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [6] (data from MRSA252)
    SACOL0545(rplY)50S ribosomal protein L25/general stress protein Ctc  [6] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [6] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL0437(rpsF)30S ribosomal protein S6  [6] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [6] (data from MRSA252)
    SACOL2225(rpsH)30S ribosomal protein S8  [6] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [6] (data from MRSA252)
    SACOL1292(rpsO)30S ribosomal protein S15  [6] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [6] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [6] (data from MRSA252)
    SACOL0095(spa)immunoglobulin G binding protein A precursor  [6] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [6] (data from MRSA252)
    SACOL1262(sucC)succinyl-CoA synthetase subunit beta  [6] (data from MRSA252)
    SACOL1729(thrS)threonyl-tRNA synthetase  [6] (data from MRSA252)
    SACOL1722(tig)trigger factor  [6] (data from MRSA252)
    SACOL1377(tkt)transketolase  [6] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0211acetyl-CoA acetyltransferase  [6] (data from MRSA252)
    SACOL0564pyridoxal biosynthesis lyase PdxS  [6] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [6] (data from MRSA252)
    SACOL0815ribosomal subunit interface protein  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL1753universal stress protein  [6] (data from MRSA252)
    SACOL1759universal stress protein  [6] (data from MRSA252)
    SACOL1952ferritins family protein  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

  • half-life: no data available

⊟Biological Material[edit | edit source]

⊟Mutants[edit | edit source]

⊟Expression vector[edit | edit source]

⊟lacZ fusion[edit | edit source]

⊟GFP fusion[edit | edit source]

⊟two-hybrid system[edit | edit source]

⊟FLAG-tag construct[edit | edit source]

⊟Antibody[edit | edit source]

⊟Other Information[edit | edit source]

You are kindly invited to share additional interesting facts.

⊟Literature[edit | edit source]

⊟References[edit | edit source]

  1. ↑ Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
    A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
    PLoS One: 2009, 4(12);e8176
    [PubMed:19997597] [WorldCat.org] [DOI] (I e)
  2. ↑ Kristina Hempel, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
    Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
    J Proteome Res: 2010, 9(3);1579-90
    [PubMed:20108986] [WorldCat.org] [DOI] (I p)
  3. ↑ Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
    Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
    J Proteome Res: 2011, 10(4);1657-66
    [PubMed:21323324] [WorldCat.org] [DOI] (I p)
  4. ↑ Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
    The Staphylococcus aureus proteome.
    Int J Med Microbiol: 2014, 304(2);110-20
    [PubMed:24439828] [WorldCat.org] [DOI] (I p)
  5. ↑ Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
    Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
    Sci Rep: 2016, 6;28172
    [PubMed:27344979] [WorldCat.org] [DOI] (I e)
  6. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 6.17 6.18 6.19 6.20 6.21 6.22 6.23 6.24 6.25 6.26 6.27 6.28 6.29 6.30 6.31 6.32 6.33 6.34 6.35 6.36 6.37 6.38 6.39 6.40 6.41 6.42 6.43 6.44 6.45 6.46 6.47 6.48 6.49 6.50 6.51 6.52 6.53 6.54 6.55 6.56 6.57 6.58 6.59 6.60 6.61 6.62 6.63 6.64 6.65 6.66 6.67 6.68 6.69 6.70 6.71 6.72 6.73 6.74 6.75 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
    Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
    J Proteome Res: 2011, 10(3);1139-50
    [PubMed:21166474] [WorldCat.org] [DOI] (I p)

⊟Relevant publications[edit | edit source]

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