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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_01251
- pan locus tag?: SAUPAN003575000
- symbol: SAOUHSC_01251
- pan gene symbol?: pnpA
- synonym:
- product: polynucleotide phosphorylase/polyadenylase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_01251
- symbol: SAOUHSC_01251
- product: polynucleotide phosphorylase/polyadenylase
- replicon: chromosome
- strand: +
- coordinates: 1202091..1204187
- length: 2097
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3919982 NCBI
- RefSeq: YP_499784 NCBI
- BioCyc: G1I0R-1169 BioCyc
- MicrobesOnline: 1289698 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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2041ATGTCTCAAGAAAAGAAAGTTTTTAAAACTGAATGGGCAGGAAGATCTTTAACGATTGAA
ACAGGGCAATTAGCTAAACAAGCAAATGGCGCTGTATTGGTTCGTTATGGAGATACAGTC
GTGTTATCGACGGCAACTGCATCAAAAGAACCTCGTGATGGAGATTTCTTCCCATTAACA
GTGAACTATGAAGAAAAAATGTACGCTGCGGGTAAAATTCCTGGTGGATTTAAAAAGAGA
GAAGGACGTCCTGGTGACGATGCAACATTAACTGCGCGATTAATTGATAGACCAATTAGA
CCTTTATTCCCTAAAGGATATAAGCATGATGTTCAAATTATGAACATGGTATTAAGTGCA
GATCCTGATTGTTCACCACAAATGGCTGCAATGATTGGTTCATCTATGGCGCTTAGTGTG
TCGGATATTCCATTCCAAGGGCCAATCGCCGGTGTAAATGTGGGTTATATTGACGGTAAA
TATATCATTAACCCAACAGTAGAAGAAAAAGAAGTTTCTCGTTTAGACCTTGAAGTAGCT
GGTCATAAAGATGCGGTAAACATGGTAGAGGCAGGCGCTAGTGAGATTACTGAACAAGAA
ATGTTAGAGGCGATTTTCTTTGGTCATGAAGAGATTCAACGTTTAGTTGATTTCCAACAA
CAAATCGTCGACCACATTCAACCTGTTAAACAAGAATTTATTCCAGCAGAGCGTGATGAA
GCGCTAGTTGAACGTGTAAAATCTTTAACCGAAGAAAAAGGACTTAAAGAAACAGTTTTA
ACATTTGATAAACAACAACGAGATGAAAATCTTGATAACTTAAAAGAAGAAATCGTCAAT
GAATTTATCGATGAAGAAGATCCAGAGAATGAATTACTTATTAAAGAAGTTTATGCAATT
TTAAATGAATTAGTGAAAGAAGAAGTTCGACGTTTAATTGCAGATGAAAAAATTAGACCA
GACGGCCGTAAACCTGATGAAATCCGTCCATTAGATTCTGAAGTTGGTATTTTACCTAGA
ACGCATGGTTCAGGTCTATTTACACGTGGTCAGACTCAAGCACTTTCAGTTTTAACATTA
GGTGCTTTAGGCGATTATCAATTAATTGATGGTTTAGGACCTGAAGAAGAAAAAAGATTC
ATGCATCATTACAACTTCCCGAATTTTTCAGTAGGTGAAACTGGTCCAGTACGTGCGCCA
GGTCGTCGTGAAATTGGACATGGTGCGTTAGGTGAAAGAGCATTAAAATATATTATTCCT
GATACTGCTGATTTCCCATATACAATTCGTATTGTAAGTGAGGTACTTGAATCAAATGGT
TCATCATCTCAAGCGTCAATTTGTGGATCAACATTAGCATTAATGGATGCGGGCGTACCG
ATTAAAGCACCAGTTGCTGGTATTGCTATGGGCCTTGTTACACGTGAAGATAGCTATACG
ATTTTAACTGATATCCAAGGTATGGAAGATGCATTAGGTGATATGGACTTTAAAGTCGCT
GGTACTAAAGAAGGTATTACAGCAATCCAAATGGATATTAAAATTGACGGTTTAACGCGT
GAAATTATCGAAGAGGCTCTAGAACAAGCGAGACGTGGTCGTTTAGAAATAATGAATCAT
ATGTTACAAACAATTGATCAACCACGTACTGAATTAAGTGCTTACGCGCCAAAAGTTGTA
ACTATGACAATTAAACCAGATAAGATTAGAGATGTTATCGGACCTGGTGGTAAAAAAATT
AACGAAATTATTGATGAAACAGGTGTTAAATTAGATATTGAACAAGATGGTACTATCTTT
ATTGGTGCTGTTGATCAAGCTATGATAAATCGTGCTCGTGAAATCATTGAGGAAATTACA
CGTGAAGCGGAAGTAGGTCAAACTTATCAAGCCACTGTTAAACGTATTGAAAAATACGGT
GCGTTTGTAGGCCTATTCCCAGGTAAAGATGCGTTGCTTCACATTTCACAAATTTCAAAA
AATAGAATTGAAAAAGTGGAAGATGTATTAAAAATCGGTGACACAATTGAAGTTAAGATT
ACTGAAATTGATAAACAAGGTCGAGTAAATGCTTCACATAGAGCATTAGAAGAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_01251
- symbol: SAOUHSC_01251
- description: polynucleotide phosphorylase/polyadenylase
- length: 698
- theoretical pI: 4.60512
- theoretical MW: 77361.5
- GRAVY: -0.336103
⊟Function[edit | edit source]
- reaction: EC 2.7.7.8? ExPASyPolyribonucleotide nucleotidyltransferase RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate
- TIGRFAM: Transcription Degradation of RNA polyribonucleotide nucleotidyltransferase (TIGR03591; EC 2.7.7.8; HMM-score: 1049)and 7 moreguanosine pentaphosphate synthetase I/polyribonucleotide nucleotidyltransferase (TIGR02696; EC 2.7.-.-,2.7.7.8; HMM-score: 683.3)Transcription Degradation of RNA exosome complex exonuclease 1 (TIGR02065; EC 3.1.13.-; HMM-score: 121.5)Transcription RNA processing ribonuclease PH (TIGR01966; EC 2.7.7.56; HMM-score: 57.3)Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein bS1 (TIGR00717; HMM-score: 40.5)arCOG04150 universal archaeal KH domain protein (TIGR03665; HMM-score: 21.4)Transcription Degradation of RNA VacB and RNase II family 3'-5' exoribonucleases (TIGR00358; EC 3.1.13.1; HMM-score: 16.6)ATP synthase archaeal, H subunit (TIGR02926; EC 3.6.3.14; HMM-score: 6.1)
- TheSEED :
- Polyribonucleotide nucleotidyltransferase (EC 2.7.7.8)
- PFAM: S5 (CL0329) RNase_PH; 3' exoribonuclease family, domain 1 (PF01138; HMM-score: 143.7)and 10 moreno clan defined RNase_PH_C; 3' exoribonuclease family, domain 2 (PF03725; HMM-score: 90.7)OB (CL0021) S1; S1 RNA binding domain (PF00575; HMM-score: 72)no clan defined PNPase; Polyribonucleotide nucleotidyltransferase, RNA binding domain (PF03726; HMM-score: 50.2)KH (CL0007) KH_1; KH domain (PF00013; HMM-score: 38.7)OB (CL0021) S1_2; S1 domain (PF13509; HMM-score: 18)TRAM; TRAM domain (PF01938; HMM-score: 14.2)no clan defined SPATA25; Spermatogenesis-associated protein 25 (PF15218; HMM-score: 13.7)DUF3921; Protein of unknown function (DUF3921) (PF13060; HMM-score: 12.4)DUF416; Protein of unknown function (DUF416) (PF04222; HMM-score: 9.9)KH (CL0007) KH_2; KH domain (PF07650; HMM-score: 7.4)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors: Mg2+
- 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
- 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): 0.014325
- TAT(Tat/SPI): 0.007821
- LIPO(Sec/SPII): 0.002457
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MSQEKKVFKTEWAGRSLTIETGQLAKQANGAVLVRYGDTVVLSTATASKEPRDGDFFPLTVNYEEKMYAAGKIPGGFKKREGRPGDDATLTARLIDRPIRPLFPKGYKHDVQIMNMVLSADPDCSPQMAAMIGSSMALSVSDIPFQGPIAGVNVGYIDGKYIINPTVEEKEVSRLDLEVAGHKDAVNMVEAGASEITEQEMLEAIFFGHEEIQRLVDFQQQIVDHIQPVKQEFIPAERDEALVERVKSLTEEKGLKETVLTFDKQQRDENLDNLKEEIVNEFIDEEDPENELLIKEVYAILNELVKEEVRRLIADEKIRPDGRKPDEIRPLDSEVGILPRTHGSGLFTRGQTQALSVLTLGALGDYQLIDGLGPEEEKRFMHHYNFPNFSVGETGPVRAPGRREIGHGALGERALKYIIPDTADFPYTIRIVSEVLESNGSSSQASICGSTLALMDAGVPIKAPVAGIAMGLVTREDSYTILTDIQGMEDALGDMDFKVAGTKEGITAIQMDIKIDGLTREIIEEALEQARRGRLEIMNHMLQTIDQPRTELSAYAPKVVTMTIKPDKIRDVIGPGGKKINEIIDETGVKLDIEQDGTIFIGAVDQAMINRAREIIEEITREAEVGQTYQATVKRIEKYGAFVGLFPGKDALLHISQISKNRIEKVEDVLKIGDTIEVKITEIDKQGRVNASHRALEE
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
SAOUHSC_01471 (asnC) asparaginyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_00790 (clpP) ATP-dependent Clp protease proteolytic subunit [3] (data from MRSA252) SAOUHSC_01683 (dnaK) molecular chaperone DnaK [3] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [3] (data from MRSA252) SAOUHSC_02117 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [3] (data from MRSA252) SAOUHSC_01276 (glpK) glycerol kinase [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_01246 (infB) translation initiation factor IF-2 [3] (data from MRSA252) SAOUHSC_01786 (infC) translation initiation factor IF-3 [3] (data from MRSA252) SAOUHSC_00900 (pgi) glucose-6-phosphate isomerase [3] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [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_00520 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [3] (data from MRSA252) SAOUHSC_02478 (rplM) 50S ribosomal protein L13 [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_01211 (rplS) 50S ribosomal protein L19 [3] (data from MRSA252) SAOUHSC_01784 (rplT) 50S ribosomal protein L20 [3] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [3] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [3] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [3] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [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_00348 (rpsF) 30S ribosomal protein S6 [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_02487 (rpsM) 30S ribosomal protein S13 [3] (data from MRSA252) SAOUHSC_02503 (rpsQ) 30S ribosomal protein S17 [3] (data from MRSA252) SAOUHSC_00350 (rpsR) 30S ribosomal protein S18 [3] (data from MRSA252) SAOUHSC_02508 (rpsS) 30S ribosomal protein S19 [3] (data from MRSA252) SAOUHSC_01418 (sucA) 2-oxoglutarate dehydrogenase E1 component [3] (data from MRSA252) SAOUHSC_01216 (sucC) succinyl-CoA synthetase subunit beta [3] (data from MRSA252) SAOUHSC_01788 (thrS) threonyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_01779 (tig) trigger factor [3] (data from MRSA252) SAOUHSC_01234 (tsf) elongation factor Ts [3] (data from MRSA252) SAOUHSC_00069 protein A [3] (data from MRSA252) SAOUHSC_00100 2-deoxyribose-5-phosphate aldolase [3] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [3] (data from MRSA252) SAOUHSC_00206 L-lactate dehydrogenase [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_00426 ABC transporter substrate-binding protein [3] (data from MRSA252) SAOUHSC_00474 50S ribosomal protein L25/general stress protein Ctc [3] (data from MRSA252) SAOUHSC_00483 hypothetical protein [3] (data from MRSA252) SAOUHSC_00488 hypothetical protein [3] (data from MRSA252) SAOUHSC_00499 pyridoxal biosynthesis lyase PdxS [3] (data from MRSA252) SAOUHSC_00525 DNA-directed RNA polymerase subunit beta' [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_00608 alcohol dehydrogenase [3] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_00845 hypothetical protein [3] (data from MRSA252) SAOUHSC_00878 hypothetical protein [3] (data from MRSA252) SAOUHSC_00895 glutamate dehydrogenase [3] (data from MRSA252) SAOUHSC_00951 hypothetical protein [3] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [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_01218 succinyl-CoA synthetase subunit alpha [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_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01605 6-phosphogluconate dehydrogenase [3] (data from MRSA252) SAOUHSC_01666 glycyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01807 6-phosphofructokinase [3] (data from MRSA252) SAOUHSC_01814 hypothetical protein [3] (data from MRSA252) SAOUHSC_01819 hypothetical protein [3] (data from MRSA252) SAOUHSC_01820 acetate kinase [3] (data from MRSA252) SAOUHSC_01845 formate--tetrahydrofolate ligase [3] (data from MRSA252) SAOUHSC_01901 putative translaldolase [3] (data from MRSA252) SAOUHSC_02108 ferritin [3] (data from MRSA252) SAOUHSC_02363 aldehyde dehydrogenase [3] (data from MRSA252) SAOUHSC_02366 fructose-bisphosphate aldolase [3] (data from MRSA252) SAOUHSC_02399 glucosamine--fructose-6-phosphate aminotransferase [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_02486 30S ribosomal protein S11 [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]
- predicted SigA promoter [4] : S517 > rbfA > S518 > SAOUHSC_01248 > SAOUHSC_01249 > S519 > rpsO > S520 > SAOUHSC_01251predicted SigB promoter [4] : S518 > SAOUHSC_01248 > SAOUHSC_01249 > S519 > rpsO > S520 > SAOUHSC_01251
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [4] Multi-gene expression profiles
⊟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]
- ↑ 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) - ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 3.14 3.15 3.16 3.17 3.18 3.19 3.20 3.21 3.22 3.23 3.24 3.25 3.26 3.27 3.28 3.29 3.30 3.31 3.32 3.33 3.34 3.35 3.36 3.37 3.38 3.39 3.40 3.41 3.42 3.43 3.44 3.45 3.46 3.47 3.48 3.49 3.50 3.51 3.52 3.53 3.54 3.55 3.56 3.57 3.58 3.59 3.60 3.61 3.62 3.63 3.64 3.65 3.66 3.67 3.68 3.69 3.70 3.71 3.72 3.73 3.74 3.75 3.76 3.77 3.78 3.79 3.80 3.81 3.82 3.83 3.84 3.85 3.86 3.87 3.88 3.89 3.90 3.91 3.92 3.93 3.94 3.95 3.96 3.97 3.98 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 4.2 4.3 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)