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PangenomeCOLN315NCTC8325NewmanUSA300_FPR375704-0298108BA0217611819-97685071193ECT-R 2ED133ED98HO 5096 0412JH1JH9JKD6008JKD6159JSNZLGA251M013MRSA252MSHR1132MSSA476MW2Mu3Mu50RF122ST398T0131TCH60TW20USA300_TCH1516VC40

NCBI: 01-MAR-2011 (discontinued in NCBI 03-AUG-2016)

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⊟Summary[edit | edit source]

Contents

  • 1 Summary
  • 2 Genome View
  • 3 Gene
    • 3.1 General
    • 3.2 Accession numbers
    • 3.3 Phenotype
    • 3.4 DNA sequence
  • 4 Protein
    • 4.1 General
    • 4.2 Function
    • 4.3 Structure, modifications & cofactors
    • 4.4 Localization
    • 4.5 Accession numbers
    • 4.6 Protein sequence
    • 4.7 Experimental data
  • 5 Expression & Regulation
    • 5.1 Operon
    • 5.2 Regulation
    • 5.3 Transcription pattern
    • 5.4 Protein synthesis (provided by Aureolib)
    • 5.5 Protein stability
  • 6 Biological Material
    • 6.1 Mutants
    • 6.2 Expression vector
    • 6.3 lacZ fusion
    • 6.4 GFP fusion
    • 6.5 two-hybrid system
    • 6.6 FLAG-tag construct
    • 6.7 Antibody
  • 7 Other Information
  • 8 Literature
    • 8.1 References
    • 8.2 Relevant publications
  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_01232
  • pan locus tag?: SAUPAN003555000
  • symbol: rpsB
  • pan gene symbol?: rpsB
  • synonym:
  • product: 30S ribosomal protein S2

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_01232
  • symbol: rpsB
  • product: 30S ribosomal protein S2
  • replicon: chromosome
  • strand: +
  • coordinates: 1180820..1181588
  • length: 768
  • essential: yes [1] DEG other strains
  • comment: The sequence of SAOUHSC_01232 was corrected based on the resequencing performed by Berscheid et al., 2012 [2], resulting in a longer CDS.

⊟Accession numbers[edit | edit source]

  • Gene ID: 3920257 NCBI
  • RefSeq: YP_499765 NCBI
  • BioCyc: G1I0R-3561 BioCyc
  • MicrobesOnline: 1289679 MicrobesOnline

⊟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
    ATGGCAGTAATTTCAATGAAACAATTACTAGAAGCGGGTGTTCACTTCGGTCACCAAACA
    CGTCGTTGGAACCCAAAAATGAAAAAATATATCTTCACTGAGAGAAATGGTATTTATATC
    ATCGACTTACAAAAAACAGTGAAAAAAGTAGACGAGGCATACAACTTCTTGAAACAAGTT
    TCAGAAGATGGTGGACAAGTCTTATTCGTAGGAACTAAAAAACAAGCACAAGAATCAGTT
    AAATCTGAAGCAGAACGTGCTGGTCAATTCTACATTAACCAAAGATGGTTAGGTGGATTA
    TTAACTAACTATAAAACGATCTCAAAACGAATCAAACGTATTTCTGAAATTGAAAAAATG
    GAAGAAGATGGTTTATTCGAAGTATTACCTAAAAAAGAAGTAGTAGAACTTAAAAAAGAA
    TACGACCGTTTAATCAAATTCTTAGGCGGAATTCGTGATATGAAATCAATGCCTCAAGCA
    TTATTCGTAGTTGACCCACGTAAAGAGCGTAATGCAATTGCTGAAGCTCGTAAATTAAAT
    ATTCCTATCGTAGGTATCGTTGACACTAACTGTGATCCTGACGAAATTGACTACGTTATC
    CCAGCAAACGACGATGCTATCCGTGCGGTTAAATTATTAACTGCTAAAATGGCAGATGCA
    ATCTTAGAAGGTCAACAAGGCGTTTCTAATGAAGAAGTAGCTGCAGAACAAAACATCGAT
    TTAGATGAAAAAGAAAAATCAGAAGAAACAGAAGCAACTGAAGAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    768

⊟Protein[edit | edit source]

  • 5LI0
    PDB
  • 5ND8
    PDB
  • 5ND9
    PDB
Protein Data Bank: 5LI0
Protein Data Bank: 5ND8
Protein Data Bank: 5ND9

⊟General[edit | edit source]

  • locus tag: SAOUHSC_01232
  • symbol: RpsB
  • description: 30S ribosomal protein S2
  • length: 255
  • theoretical pI: 5.17378
  • theoretical MW: 29094.1
  • GRAVY: -0.529804

⊟Function[edit | edit source]

  • ⊞TIGRFAM:
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uS2 (TIGR01011; HMM-score: 365.1)
    and 1 more
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uS2 (TIGR01012; HMM-score: 97.3)
  • TheSEED  :
    • SSU ribosomal protein S2p (SAe)
    Protein Metabolism Protein biosynthesis Ribosome SSU bacterial  SSU ribosomal protein S2p (SAe)
  • PFAM:
    SIS (CL0067) Ribosomal_S2; Ribosomal protein S2 (PF00318; HMM-score: 344.8)

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

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • ⊞PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.97
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0.01
    • Extracellular Score: 0.02
    • Internal Helices: 0
  • ⊞DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.6485
    • Cytoplasmic Membrane Score: 0.0302
    • Cell wall & surface Score: 0.0007
    • Extracellular Score: 0.3206
  • ⊞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): 0.001567
    • TAT(Tat/SPI): 0.000142
    • LIPO(Sec/SPII): 0.000329
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

  • GI: 88194965 NCBI
  • RefSeq: YP_499765 NCBI
  • UniProt: Q2FZ25 UniProt
  • STRING: 93061.SAOUHSC_01232 STRING

⊟Protein sequence[edit | edit source]

  • MAVISMKQLLEAGVHFGHQTRRWNPKMKKYIFTERNGIYIIDLQKTVKKVDEAYNFLKQVSEDGGQVLFVGTKKQAQESVKSEAERAGQFYINQRWLGGLLTNYKTISKRIKRISEIEKMEEDGLFEVLPKKEVVELKKEYDRLIKFLGGIRDMKSMPQALFVVDPRKERNAIAEARKLNIPIVGIVDTNCDPDEIDYVIPANDDAIRAVKLLTAKMADAILEGQQGVSNEEVAAEQNIDLDEKEKSEETEATEE

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas [3] [4]
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • ⊟interaction partners:
    SAOUHSC_02490(adk)adenylate kinase  [5] (data from MRSA252)
    SAOUHSC_01471(asnC)asparaginyl-tRNA synthetase  [5] (data from MRSA252)
    SAOUHSC_01170(carB)carbamoyl phosphate synthase large subunit  [5] (data from MRSA252)
    SAOUHSC_01778(clpX)ATP-dependent protease ATP-binding subunit ClpX  [5] (data from MRSA252)
    SAOUHSC_02380(deoD)purine nucleoside phosphorylase  [5] (data from MRSA252)
    SAOUHSC_01683(dnaK)molecular chaperone DnaK  [5] (data from MRSA252)
    SAOUHSC_00799(eno)phosphopyruvate hydratase  [5] (data from MRSA252)
    SAOUHSC_02703(gpmA)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase  [5] (data from MRSA252)
    SAOUHSC_02255(groES)co-chaperonin GroES  [5] (data from MRSA252)
    SAOUHSC_00375(guaA)GMP synthase  [5] (data from MRSA252)
    SAOUHSC_01246(infB)translation initiation factor IF-2  [5] (data from MRSA252)
    SAOUHSC_00493(lysS)lysyl-tRNA synthetase  [5] (data from MRSA252)
    SAOUHSC_02919(panB)3-methyl-2-oxobutanoate hydroxymethyltransferase  [5] (data from MRSA252)
    SAOUHSC_00900(pgi)glucose-6-phosphate isomerase  [5] (data from MRSA252)
    SAOUHSC_00796(pgk)phosphoglycerate kinase  [5] (data from MRSA252)
    SAOUHSC_00519(rplA)50S ribosomal protein L1  [5] (data from MRSA252)
    SAOUHSC_02509(rplB)50S ribosomal protein L2  [5] (data from MRSA252)
    SAOUHSC_02512(rplC)50S ribosomal protein L3  [5] (data from MRSA252)
    SAOUHSC_02511(rplD)50S ribosomal protein L4  [5] (data from MRSA252)
    SAOUHSC_02500(rplE)50S ribosomal protein L5  [5] (data from MRSA252)
    SAOUHSC_02496(rplF)50S ribosomal protein L6  [5] (data from MRSA252)
    SAOUHSC_00017(rplI)50S ribosomal protein L9  [5] (data from MRSA252)
    SAOUHSC_00520(rplJ)50S ribosomal protein L10  [5] (data from MRSA252)
    SAOUHSC_00521(rplL)50S ribosomal protein L7/L12  [5] (data from MRSA252)
    SAOUHSC_02478(rplM)50S ribosomal protein L13  [5] (data from MRSA252)
    SAOUHSC_02492(rplO)50S ribosomal protein L15  [5] (data from MRSA252)
    SAOUHSC_02495(rplR)50S ribosomal protein L18  [5] (data from MRSA252)
    SAOUHSC_01211(rplS)50S ribosomal protein L19  [5] (data from MRSA252)
    SAOUHSC_01784(rplT)50S ribosomal protein L20  [5] (data from MRSA252)
    SAOUHSC_01757(rplU)50S ribosomal protein L21  [5] (data from MRSA252)
    SAOUHSC_02507(rplV)50S ribosomal protein L22  [5] (data from MRSA252)
    SAOUHSC_02510(rplW)50S ribosomal protein L23  [5] (data from MRSA252)
    SAOUHSC_02501(rplX)50S ribosomal protein L24  [5] (data from MRSA252)
    SAOUHSC_01755(rpmA)50S ribosomal protein L27  [5] (data from MRSA252)
    SAOUHSC_02361(rpmE2)50S ribosomal protein L31 type B  [5] (data from MRSA252)
    SAOUHSC_00524(rpoB)DNA-directed RNA polymerase subunit beta  [5] (data from MRSA252)
    SAOUHSC_01493(rpsA)30S ribosomal protein S1  [5] (data from MRSA252)
    SAOUHSC_02506(rpsC)30S ribosomal protein S3  [5] (data from MRSA252)
    SAOUHSC_01829(rpsD)30S ribosomal protein S4  [5] (data from MRSA252)
    SAOUHSC_02494(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SAOUHSC_02498(rpsH)30S ribosomal protein S8  [5] (data from MRSA252)
    SAOUHSC_02477(rpsI)30S ribosomal protein S9  [5] (data from MRSA252)
    SAOUHSC_02487(rpsM)30S ribosomal protein S13  [5] (data from MRSA252)
    SAOUHSC_01208(rpsP)30S ribosomal protein S16  [5] (data from MRSA252)
    SAOUHSC_02508(rpsS)30S ribosomal protein S19  [5] (data from MRSA252)
    SAOUHSC_01418(sucA)2-oxoglutarate dehydrogenase E1 component  [5] (data from MRSA252)
    SAOUHSC_01216(sucC)succinyl-CoA synthetase subunit beta  [5] (data from MRSA252)
    SAOUHSC_01779(tig)trigger factor  [5] (data from MRSA252)
    SAOUHSC_00797(tpiA)triosephosphate isomerase  [5] (data from MRSA252)
    SAOUHSC_01234(tsf)elongation factor Ts  [5] (data from MRSA252)
    SAOUHSC_00002DNA polymerase III subunit beta  [5] (data from MRSA252)
    SAOUHSC_00009seryl-tRNA synthetase  [5] (data from MRSA252)
    SAOUHSC_00069protein A  [5] (data from MRSA252)
    SAOUHSC_00187formate acetyltransferase  [5] (data from MRSA252)
    SAOUHSC_00206L-lactate dehydrogenase  [5] (data from MRSA252)
    SAOUHSC_00346GTP-dependent nucleic acid-binding protein EngD  [5] (data from MRSA252)
    SAOUHSC_00356hypothetical protein  [5] (data from MRSA252)
    SAOUHSC_00365alkyl hydroperoxide reductase subunit C  [5] (data from MRSA252)
    SAOUHSC_00371hypothetical protein  [5] (data from MRSA252)
    SAOUHSC_00374inosine-5'-monophosphate dehydrogenase  [5] (data from MRSA252)
    SAOUHSC_0047450S ribosomal protein L25/general stress protein Ctc  [5] (data from MRSA252)
    SAOUHSC_00488hypothetical protein  [5] (data from MRSA252)
    SAOUHSC_00499pyridoxal biosynthesis lyase PdxS  [5] (data from MRSA252)
    SAOUHSC_00525DNA-directed RNA polymerase subunit beta'  [5] (data from MRSA252)
    SAOUHSC_00529elongation factor G  [5] (data from MRSA252)
    SAOUHSC_00530elongation factor Tu  [5] (data from MRSA252)
    SAOUHSC_00608alcohol dehydrogenase  [5] (data from MRSA252)
    SAOUHSC_00634ABC transporter substrate-binding protein  [5] (data from MRSA252)
    SAOUHSC_00767hypothetical protein  [5] (data from MRSA252)
    SAOUHSC_00795glyceraldehyde-3-phosphate dehydrogenase  [5] (data from MRSA252)
    SAOUHSC_00871D-alanine--poly(phosphoribitol) ligase subunit 2  [5] (data from MRSA252)
    SAOUHSC_00878hypothetical protein  [5] (data from MRSA252)
    SAOUHSC_00895glutamate dehydrogenase  [5] (data from MRSA252)
    SAOUHSC_00906hypothetical protein  [5] (data from MRSA252)
    SAOUHSC_00947enoyl-(acyl carrier protein) reductase  [5] (data from MRSA252)
    SAOUHSC_009851,4-dihydroxy-2-naphthoyl-CoA synthase  [5] (data from MRSA252)
    SAOUHSC_01007bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [5] (data from MRSA252)
    SAOUHSC_01040pyruvate dehydrogenase complex, E1 component subunit alpha  [5] (data from MRSA252)
    SAOUHSC_01041pyruvate dehydrogenase complex, E1 component subunit beta  [5] (data from MRSA252)
    SAOUHSC_01042branched-chain alpha-keto acid dehydrogenase subunit E2  [5] (data from MRSA252)
    SAOUHSC_01043dihydrolipoamide dehydrogenase  [5] (data from MRSA252)
    SAOUHSC_01100thioredoxin  [5] (data from MRSA252)
    SAOUHSC_01150cell division protein FtsZ  [5] (data from MRSA252)
    SAOUHSC_01218succinyl-CoA synthetase subunit alpha  [5] (data from MRSA252)
    SAOUHSC_01287glutamine synthetase  [5] (data from MRSA252)
    SAOUHSC_01337transketolase  [5] (data from MRSA252)
    SAOUHSC_01347aconitate hydratase  [5] (data from MRSA252)
    SAOUHSC_01416dihydrolipoamide succinyltransferase  [5] (data from MRSA252)
    SAOUHSC_01431methionine sulfoxide reductase B  [5] (data from MRSA252)
    SAOUHSC_01451threonine dehydratase  [5] (data from MRSA252)
    SAOUHSC_01490DNA-binding protein HU  [5] (data from MRSA252)
    SAOUHSC_016056-phosphogluconate dehydrogenase  [5] (data from MRSA252)
    SAOUHSC_01653superoxide dismutase  [5] (data from MRSA252)
    SAOUHSC_01666glycyl-tRNA synthetase  [5] (data from MRSA252)
    SAOUHSC_01684heat shock protein GrpE  [5] (data from MRSA252)
    SAOUHSC_01794glyceraldehyde 3-phosphate dehydrogenase 2  [5] (data from MRSA252)
    SAOUHSC_01801isocitrate dehydrogenase  [5] (data from MRSA252)
    SAOUHSC_01806pyruvate kinase  [5] (data from MRSA252)
    SAOUHSC_018076-phosphofructokinase  [5] (data from MRSA252)
    SAOUHSC_01819hypothetical protein  [5] (data from MRSA252)
    SAOUHSC_01820acetate kinase  [5] (data from MRSA252)
    SAOUHSC_02108ferritin  [5] (data from MRSA252)
    SAOUHSC_02366fructose-bisphosphate aldolase  [5] (data from MRSA252)
    SAOUHSC_02377pyrimidine-nucleoside phosphorylase  [5] (data from MRSA252)
    SAOUHSC_02399glucosamine--fructose-6-phosphate aminotransferase  [5] (data from MRSA252)
    SAOUHSC_02425hypothetical protein  [5] (data from MRSA252)
    SAOUHSC_02441alkaline shock protein 23  [5] (data from MRSA252)
    SAOUHSC_02485DNA-directed RNA polymerase subunit alpha  [5] (data from MRSA252)
    SAOUHSC_0248630S ribosomal protein S11  [5] (data from MRSA252)
    SAOUHSC_02830D-lactate dehydrogenase  [5] (data from MRSA252)
    SAOUHSC_02860HMG-CoA synthase  [5] (data from MRSA252)
    SAOUHSC_028691-pyrroline-5-carboxylate dehydrogenase  [5] (data from MRSA252)
    SAOUHSC_02922L-lactate dehydrogenase  [5] (data from MRSA252)
    SAOUHSC_02926fructose-1,6-bisphosphate aldolase  [5] (data from MRSA252)
    SAOUHSC_02927malate:quinone oxidoreductase  [5] (data from MRSA252)
    SAOUHSC_02968ornithine carbamoyltransferase  [5] (data from MRSA252)
    SAOUHSC_02969arginine deiminase  [5] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

  • predicted SigA promoter [6] : SAOUHSC_01222 > S504 > SAOUHSC_01223 > S505 > SAOUHSC_01224 > SAOUHSC_01225 > hslU > SAOUHSC_01228 > S506 > SAOUHSC_01230 > S507 > S508 > rpsB > SAOUHSC_01233 > tsf > S509 > pyrH > frr > S510 > S511 > SAOUHSC_01237 > SAOUHSC_01238 > S512 > SAOUHSC_01239 > SAOUHSC_01240
    predicted SigA promoter [6] : S508 > rpsB > SAOUHSC_01233 > tsf > S509 > pyrH > frr > S510 > S511 > SAOUHSC_01237 > SAOUHSC_01238 > S512 > SAOUHSC_01239 > SAOUHSC_01240 > S513 > polC > S514 > S515 > SAOUHSC_01242 > nusA > SAOUHSC_01244 > SAOUHSC_01245 > infB

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

  • S.aureus Expression Data Browser:  [6] 
    Expression Data Browser
    ⊟Multi-gene expression profiles



    Click on any data point to display a description of the corresponding condition!

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

  • Aureolib: data available for COL

⊟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. ↑ Roy R Chaudhuri, Andrew G Allen, Paul J Owen, Gil Shalom, Karl Stone, Marcus Harrison, Timothy A Burgis, Michael Lockyer, Jorge Garcia-Lara, Simon J Foster, Stephen J Pleasance, Sarah E Peters, Duncan J Maskell, Ian G Charles
    Comprehensive identification of essential Staphylococcus aureus genes using Transposon-Mediated Differential Hybridisation (TMDH).
    BMC Genomics: 2009, 10;291
    [PubMed:19570206] [WorldCat.org] [DOI] (I e)
  2. ↑ Anne Berscheid, Peter Sass, Konstantin Weber-Lassalle, Ambrose L Cheung, Gabriele Bierbaum
    Revisiting the genomes of the Staphylococcus aureus strains NCTC 8325 and RN4220.
    Int J Med Microbiol: 2012, 302(2);84-7
    [PubMed:22417616] [WorldCat.org] [DOI] (I p)
  3. ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
    A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
    Proteomics: 2015, 15(21);3648-61
    [PubMed:26224020] [WorldCat.org] [DOI] (I p)
  4. ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
    A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
    Sci Rep: 2017, 7(1);9718
    [PubMed:28887440] [WorldCat.org] [DOI] (I e)
  5. ↑ Jump up to: 5.000 5.001 5.002 5.003 5.004 5.005 5.006 5.007 5.008 5.009 5.010 5.011 5.012 5.013 5.014 5.015 5.016 5.017 5.018 5.019 5.020 5.021 5.022 5.023 5.024 5.025 5.026 5.027 5.028 5.029 5.030 5.031 5.032 5.033 5.034 5.035 5.036 5.037 5.038 5.039 5.040 5.041 5.042 5.043 5.044 5.045 5.046 5.047 5.048 5.049 5.050 5.051 5.052 5.053 5.054 5.055 5.056 5.057 5.058 5.059 5.060 5.061 5.062 5.063 5.064 5.065 5.066 5.067 5.068 5.069 5.070 5.071 5.072 5.073 5.074 5.075 5.076 5.077 5.078 5.079 5.080 5.081 5.082 5.083 5.084 5.085 5.086 5.087 5.088 5.089 5.090 5.091 5.092 5.093 5.094 5.095 5.096 5.097 5.098 5.099 5.100 5.101 5.102 5.103 5.104 5.105 5.106 5.107 5.108 5.109 5.110 5.111 5.112 5.113 5.114 5.115 5.116 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)
  6. ↑ Jump up to: 6.0 6.1 6.2 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
    Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
    PLoS Genet: 2016, 12(4);e1005962
    [PubMed:27035918] [WorldCat.org] [DOI] (I e)

⊟Relevant publications[edit | edit source]

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  • This page was last edited on 11 March 2016, at 05:46.
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