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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_01652
- pan locus tag?: SAUPAN004133000
- symbol: SAOUHSC_01652
- pan gene symbol?: pbp3
- synonym:
- product: penicillin-binding protein 3
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_01652
- symbol: SAOUHSC_01652
- product: penicillin-binding protein 3
- replicon: chromosome
- strand: -
- coordinates: 1564943..1567018
- length: 2076
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3920104 NCBI
- RefSeq: YP_500164 NCBI
- BioCyc: G1I0R-1536 BioCyc
- MicrobesOnline: 1290078 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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 2041TTGTTAAAAAGACTAAAAGAAAAATCAAATGATGAAATCGTTCAAAATACAATTAACAAG
 AGAATTAACTTTATATTTGGTGTGATTGTATTTATTTTTGCAGTACTAGTACTACGTTTA
 GGTTATTTACAAATCGCACAAGGCTCACATTATAAACAAATTATAAAAAATGATGAAAAC
 ATTACAGTGAATGAGTCTGTGCCAAGAGGTCGTATTTTAGACAGAAATGGGAAAGTTTTA
 GTTGATAATGCTTCTAAAATGGCTATTACATATACTAGGGGTCGAAAAACAACACAATCG
 GAAATGTTGGATACGGCTGAAAAGTTATCAAAGCTAATCAAGATGGATACTAAGAAAATT
 ACAGAACGTGATAAGAAAGATTTCTGGATTCAGTTGCATCCTAAAAAAGCAAAAGCAATG
 ATGACAAAAGAACAAGCTATGTTAGCAGATGGAAGTATTAAACAAGATCAATATGATAAA
 CAACTGTTATCGAAAATCGGAAAATCACAATTAGATGAATTGTCTTCTAAAGATTTACAA
 GTTTTAGCTATTTTTCGAGAGATGAATGCAGGAACAGTTTTAGATCCACAAATGATAAAA
 AATGAAGATGTCAGTGAAAAAGAGTATGCAGCAGTTTCTCAGCAACTTTCCAAATTACCA
 GGTGTTAACACGTCTATGGATTGGGATAGAAAATATCCATATGGCGATACTTTAAGAGGT
 ATATTCGGAGATGTATCGACACCTGCTGAAGGTATTCCAAAAGAATTGACAGAACATTAC
 TTATCCAAAGGATATTCACGCAATGATCGTGTTGGAAAATCTTACCTAGAATATCAATAT
 GAAGATGTATTGCGTGGTAAGAAGAAAGAAATGAAATACACAACGGACAAATCTGGTAAA
 GTTACATCTTCAGAAGTGTTAAATCCTGGCGCTCGCGGTCAAGATTTGAAATTAACGATC
 GATATAGATCTTCAAAAAGAAGTAGAAGCATTATTAGATAAACAAATTAAGAAGCTTCGC
 AGTCAAGGTGCCAAAGATATGGATAATGCAATGATGGTTGTACAAAATCCTAAAAATGGA
 GACATTCTTGCGCTTGCCGGAAAGCAGATTAATAAGAGTGGTAAAATGACTGATTATGAC
 ATTGGTACGTTTACTTCTCAATTTGCGGTTGGATCTTCTGTAAAAGGTGGAACATTATTA
 GCCGGTTATCAGAATAAAGCTATCAAAGTTGGAGAAACAATGGTCGATGAACCATTACAT
 TTCCAAGGTGGTTTGACAAAACGATCATACTTCAATAAAAACGGGCATGTAACTATTAAT
 GATAAGCAAGCTTTGATGCATTCATCAAACGTATATATGTTTAAAACAGCATTAAAATTA
 GCGGGAGACCCTTATTATTCTGGTATGGCTTTACCTTCAGACATAAGTTCACCTGCCCAA
 AAGCTAAGAAGAGGATTAAATCAAGTAGGCTTAGGTGTGAAAACAGGGATAGATTTACCA
 AATGAAACAAGAGGTCAAATCGAACCATTAACAAATAATCCAGGTAATTATCTAGATTTA
 TCAATTGGTCAATATGATACCTATACACCATTACAATTATCACAATATGTTTCAACTATA
 GCGAATGATGGTTATAGAATACAGCCACACATTGGATTAACGATTCATGAATCAACTAAT
 AAAGATGAGGTTGGTCCACTCAAGAAGAAAATTAATGGCACTGTCTTGAACAAGGTTAAT
 AATACTGAAAAGGAAATCAAACAAATTCAAGAAGGATTCAAAATGGCATTTAATGATAAA
 GATGGTACTGGATATGTTAGTTTTAAAGATACAGTAGTACCTACTGCTGGTAAAACGGGT
 ACCGCAGAAGTGTTCCAAAACGGAGAGCCAAGAGTTAACTCTACTTATATAGGATACGCG
 CCAATTGATGATCCAAAATTAGCGTTTTCAATTGTATATACAAATCAGCCTGTACCACCA
 CCATGGTTAACAGGTGGAGACTTAGGTAGAGATGTAATTAACTACTACTTTAAGCAGTTA
 GGTAAAGATGATAAAAATAAAGACAAAGACAAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_01652
- symbol: SAOUHSC_01652
- description: penicillin-binding protein 3
- length: 691
- theoretical pI: 9.73368
- theoretical MW: 77237.6
- GRAVY: -0.603473
⊟Function[edit | edit source]
- TIGRFAM: Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan penicillin-binding protein 2 (TIGR03423; HMM-score: 277.9)and 5 moreCell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan stage V sporulation protein D (TIGR02214; HMM-score: 139.8)Cellular processes Sporulation and germination stage V sporulation protein D (TIGR02214; HMM-score: 139.8)Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan penicillin-binding protein, 1A family (TIGR02074; HMM-score: 46.9)Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan penicillin-binding protein 1C (TIGR02073; HMM-score: 30.6)Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan penicillin-binding protein 1B (TIGR02071; HMM-score: 28.7)
- TheSEED  : - Cell division protein FtsI [Peptidoglycan synthetase] (EC 2.4.1.129)
- Transpeptidase, Penicillin binding protein transpeptidase domain
 Cell Division and Cell Cycle Cell Division and Cell Cycle - no subcategory Bacterial Cytoskeleton Cell division protein FtsI [Peptidoglycan synthetase] (EC 2.4.1.129)and 1 more
- PFAM: Beta-lactamase (CL0013) Transpeptidase; Penicillin binding protein transpeptidase domain (PF00905; HMM-score: 190)and 3 morePBP_NTD (CL0776) PBP_dimer; Penicillin-binding Protein dimerisation domain (PF03717; HMM-score: 147.3)EF_hand (CL0220) EF-hand_6; EF-hand domain (PF13405; HMM-score: 13.8)EF-hand_1; EF hand domain (PF00036; HMM-score: 11.6)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic Membrane- Cytoplasmic Score: 0.17
- Cytoplasmic Membrane Score: 9.51
- Cellwall Score: 0.16
- Extracellular Score: 0.15
- Internal Helix: 1
 
- DeepLocPro: Cytoplasmic Membrane- Cytoplasmic Score: 0.0001
- Cytoplasmic Membrane Score: 0.9392
- Cell wall & surface Score: 0.0006
- Extracellular Score: 0.0601
 
- LocateP: N-terminally anchored (No CS) - Prediction by SwissProt Classification: Membrane
- Pathway Prediction: Sec-(SPI)
- Intracellular possibility: 0.17
- Signal peptide possibility: -1
- N-terminally Anchored Score: 2
- Predicted Cleavage Site: No CleavageSite
 
- SignalP: no predicted signal peptide- SP(Sec/SPI): 0.063616
- TAT(Tat/SPI): 0.000737
- LIPO(Sec/SPII): 0.001627
 
- predicted transmembrane helices (TMHMM): 1
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MLKRLKEKSNDEIVQNTINKRINFIFGVIVFIFAVLVLRLGYLQIAQGSHYKQIIKNDENITVNESVPRGRILDRNGKVLVDNASKMAITYTRGRKTTQSEMLDTAEKLSKLIKMDTKKITERDKKDFWIQLHPKKAKAMMTKEQAMLADGSIKQDQYDKQLLSKIGKSQLDELSSKDLQVLAIFREMNAGTVLDPQMIKNEDVSEKEYAAVSQQLSKLPGVNTSMDWDRKYPYGDTLRGIFGDVSTPAEGIPKELTEHYLSKGYSRNDRVGKSYLEYQYEDVLRGKKKEMKYTTDKSGKVTSSEVLNPGARGQDLKLTIDIDLQKEVEALLDKQIKKLRSQGAKDMDNAMMVVQNPKNGDILALAGKQINKSGKMTDYDIGTFTSQFAVGSSVKGGTLLAGYQNKAIKVGETMVDEPLHFQGGLTKRSYFNKNGHVTINDKQALMHSSNVYMFKTALKLAGDPYYSGMALPSDISSPAQKLRRGLNQVGLGVKTGIDLPNETRGQIEPLTNNPGNYLDLSIGQYDTYTPLQLSQYVSTIANDGYRIQPHIGLTIHESTNKDEVGPLKKKINGTVLNKVNNTEKEIKQIQEGFKMAFNDKDGTGYVSFKDTVVPTAGKTGTAEVFQNGEPRVNSTYIGYAPIDDPKLAFSIVYTNQPVPPPWLTGGDLGRDVINYYFKQLGKDDKNKDKDK
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell:
- interaction partners: SAOUHSC_02490 (adk) adenylate kinase [3] (data from MRSA252) SAOUHSC_02380 (deoD) purine nucleoside phosphorylase [3] (data from MRSA252) SAOUHSC_01683 (dnaK) molecular chaperone DnaK [3] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [3] (data from MRSA252) SAOUHSC_00574 (eutD) phosphotransacetylase [3] (data from MRSA252) SAOUHSC_02117 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [3] (data from MRSA252) SAOUHSC_00509 (gltX) glutamyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_02703 (gpmA) 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [3] (data from MRSA252) SAOUHSC_02254 (groEL) chaperonin GroEL [3] (data from MRSA252) SAOUHSC_00375 (guaA) GMP synthase [3] (data from MRSA252) SAOUHSC_01786 (infC) translation initiation factor IF-3 [3] (data from MRSA252) SAOUHSC_00225 (ispD) 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [3] (data from MRSA252) SAOUHSC_01875 (leuS) leucyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_00493 (lysS) lysyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_00900 (pgi) glucose-6-phosphate isomerase [3] (data from MRSA252) SAOUHSC_00796 (pgk) phosphoglycerate kinase [3] (data from MRSA252) SAOUHSC_01168 (pyrC) dihydroorotase [3] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [3] (data from MRSA252) SAOUHSC_02512 (rplC) 50S ribosomal protein L3 [3] (data from MRSA252) SAOUHSC_02511 (rplD) 50S ribosomal protein L4 [3] (data from MRSA252) SAOUHSC_02500 (rplE) 50S ribosomal protein L5 [3] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [3] (data from MRSA252) SAOUHSC_00518 (rplK) 50S ribosomal protein L11 [3] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [3] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [3] (data from MRSA252) SAOUHSC_02484 (rplQ) 50S ribosomal protein L17 [3] (data from MRSA252) SAOUHSC_02495 (rplR) 50S ribosomal protein L18 [3] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [3] (data from MRSA252) SAOUHSC_02501 (rplX) 50S ribosomal protein L24 [3] (data from MRSA252) SAOUHSC_02493 (rpmD) 50S ribosomal protein L30 [3] (data from MRSA252) SAOUHSC_01785 (rpmI) 50S ribosomal protein L35 [3] (data from MRSA252) SAOUHSC_00524 (rpoB) DNA-directed RNA polymerase subunit beta [3] (data from MRSA252) SAOUHSC_01493 (rpsA) 30S ribosomal protein S1 [3] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [3] (data from MRSA252) SAOUHSC_01829 (rpsD) 30S ribosomal protein S4 [3] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [3] (data from MRSA252) SAOUHSC_02498 (rpsH) 30S ribosomal protein S8 [3] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [3] (data from MRSA252) SAOUHSC_01250 (rpsO) 30S ribosomal protein S15 [3] (data from MRSA252) SAOUHSC_02503 (rpsQ) 30S ribosomal protein S17 [3] (data from MRSA252) SAOUHSC_01689 (rpsT) 30S ribosomal protein S20 [3] (data from MRSA252) SAOUHSC_01216 (sucC) succinyl-CoA synthetase subunit beta [3] (data from MRSA252) SAOUHSC_00797 (tpiA) triosephosphate isomerase [3] (data from MRSA252) SAOUHSC_01822 (tpx) 2-Cys peroxiredoxin [3] (data from MRSA252) SAOUHSC_01234 (tsf) elongation factor Ts [3] (data from MRSA252) SAOUHSC_00009 seryl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_00069 protein A [3] (data from MRSA252) SAOUHSC_00100 2-deoxyribose-5-phosphate aldolase [3] (data from MRSA252) SAOUHSC_00132 aldehyde dehydrogenase [3] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [3] (data from MRSA252) SAOUHSC_00336 acetyl-CoA acyltransferase [3] (data from MRSA252) SAOUHSC_00365 alkyl hydroperoxide reductase subunit C [3] (data from MRSA252) SAOUHSC_00374 inosine-5'-monophosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_00444 hypothetical protein [3] (data from MRSA252) SAOUHSC_00461 methionyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_00469 regulatory protein SpoVG [3] (data from MRSA252) SAOUHSC_00474 50S ribosomal protein L25/general stress protein Ctc [3] (data from MRSA252) SAOUHSC_00488 hypothetical protein [3] (data from MRSA252) SAOUHSC_00499 pyridoxal biosynthesis lyase PdxS [3] (data from MRSA252) SAOUHSC_00505 endopeptidase [3] (data from MRSA252) SAOUHSC_00517 transcription antitermination protein [3] (data from MRSA252) SAOUHSC_00525 DNA-directed RNA polymerase subunit beta' [3] (data from MRSA252) SAOUHSC_00528 30S ribosomal protein S7 [3] (data from MRSA252) SAOUHSC_00529 elongation factor G [3] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [3] (data from MRSA252) SAOUHSC_00532 2-amino-3-ketobutyrate coenzyme A ligase [3] (data from MRSA252) SAOUHSC_00536 branched-chain amino acid aminotransferase [3] (data from MRSA252) SAOUHSC_00608 alcohol dehydrogenase [3] (data from MRSA252) SAOUHSC_00634 ABC transporter substrate-binding protein [3] (data from MRSA252) SAOUHSC_00675 hypothetical protein [3] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_00834 thioredoxin [3] (data from MRSA252) SAOUHSC_00835 hypothetical protein [3] (data from MRSA252) SAOUHSC_00891 cyclophilin-type peptidyl-prolyl cis-trans isomerase [3] (data from MRSA252) SAOUHSC_00895 glutamate dehydrogenase [3] (data from MRSA252) SAOUHSC_00906 hypothetical protein [3] (data from MRSA252) SAOUHSC_00937 oligoendopeptidase F [3] (data from MRSA252) SAOUHSC_00951 hypothetical protein [3] (data from MRSA252) SAOUHSC_01007 bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase [3] (data from MRSA252) SAOUHSC_01028 phosphocarrier protein HPr [3] (data from MRSA252) SAOUHSC_01029 phosphoenolpyruvate-protein phosphotransferase [3] (data from MRSA252) SAOUHSC_01036 hypothetical protein [3] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [3] (data from MRSA252) SAOUHSC_01041 pyruvate dehydrogenase complex, E1 component subunit beta [3] (data from MRSA252) SAOUHSC_01042 branched-chain alpha-keto acid dehydrogenase subunit E2 [3] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [3] (data from MRSA252) SAOUHSC_01100 thioredoxin [3] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [3] (data from MRSA252) SAOUHSC_01199 3-oxoacyl-(acyl-carrier-protein) reductase [3] (data from MRSA252) SAOUHSC_01228 transcriptional repressor CodY [3] (data from MRSA252) SAOUHSC_01251 polynucleotide phosphorylase/polyadenylase [3] (data from MRSA252) SAOUHSC_01287 glutamine synthetase [3] (data from MRSA252) SAOUHSC_01337 transketolase [3] (data from MRSA252) SAOUHSC_01347 aconitate hydratase [3] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [3] (data from MRSA252) SAOUHSC_01431 methionine sulfoxide reductase B [3] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01666 glycyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_01794 glyceraldehyde 3-phosphate dehydrogenase 2 [3] (data from MRSA252) SAOUHSC_01802 hypothetical protein [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01810 NADP-dependent malic enzyme [3] (data from MRSA252) SAOUHSC_01820 acetate kinase [3] (data from MRSA252) SAOUHSC_01868 dipeptidase PepV [3] (data from MRSA252) SAOUHSC_01869 hypothetical protein [3] (data from MRSA252) SAOUHSC_01901 putative translaldolase [3] (data from MRSA252) SAOUHSC_02108 ferritin [3] (data from MRSA252) SAOUHSC_02300 STAS domain-containing protein [3] (data from MRSA252) SAOUHSC_02365 UDP-N-acetylglucosamine 1-carboxyvinyltransferase [3] (data from MRSA252) SAOUHSC_02366 fructose-bisphosphate aldolase [3] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [3] (data from MRSA252) SAOUHSC_02425 hypothetical protein [3] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [3] (data from MRSA252) SAOUHSC_02485 DNA-directed RNA polymerase subunit alpha [3] (data from MRSA252) SAOUHSC_02830 D-lactate dehydrogenase [3] (data from MRSA252) SAOUHSC_02869 1-pyrroline-5-carboxylate dehydrogenase [3] (data from MRSA252) SAOUHSC_02922 L-lactate dehydrogenase [3] (data from MRSA252) SAOUHSC_02926 fructose-1,6-bisphosphate aldolase [3] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [3] (data from MRSA252) SAOUHSC_02968 ornithine carbamoyltransferase [3] (data from MRSA252) SAOUHSC_02969 arginine deiminase [3] (data from MRSA252) 
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser:  [4]  Multi-gene expression profiles Multi-gene expression profiles
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
- Aureolib: no data available
⊟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 can add further information about the gene and protein here. [edit]
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ 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)
- ↑ 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)
- ↑ 3.000 3.001 3.002 3.003 3.004 3.005 3.006 3.007 3.008 3.009 3.010 3.011 3.012 3.013 3.014 3.015 3.016 3.017 3.018 3.019 3.020 3.021 3.022 3.023 3.024 3.025 3.026 3.027 3.028 3.029 3.030 3.031 3.032 3.033 3.034 3.035 3.036 3.037 3.038 3.039 3.040 3.041 3.042 3.043 3.044 3.045 3.046 3.047 3.048 3.049 3.050 3.051 3.052 3.053 3.054 3.055 3.056 3.057 3.058 3.059 3.060 3.061 3.062 3.063 3.064 3.065 3.066 3.067 3.068 3.069 3.070 3.071 3.072 3.073 3.074 3.075 3.076 3.077 3.078 3.079 3.080 3.081 3.082 3.083 3.084 3.085 3.086 3.087 3.088 3.089 3.090 3.091 3.092 3.093 3.094 3.095 3.096 3.097 3.098 3.099 3.100 3.101 3.102 3.103 3.104 3.105 3.106 3.107 3.108 3.109 3.110 3.111 3.112 3.113 3.114 3.115 3.116 3.117 3.118 3.119 3.120 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)
- ↑ 4.0 4.1 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)
