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The liposoluble proteome of Mycoplasma agalactiae: an insight into the minimal protein complement of a bacterial membrane.

Cacciotto C, Addis MF, Pagnozzi D, Chessa B, Coradduzza E, Carcangiu L, Uzzau S, Alberti A, Pittau M.

BMC Microbiol. 2010 Aug 25;10:225. doi: 10.1186/1471-2180-10-225.


Genome-scale analysis of Mycoplasma agalactiae loci involved in interaction with host cells.

Skapski A, Hygonenq MC, Sagné E, Guiral S, Citti C, Baranowski E.

PLoS One. 2011;6(9):e25291. doi: 10.1371/journal.pone.0025291.


Critical role of dispensable genes in Mycoplasma agalactiae interaction with mammalian cells.

Baranowski E, Guiral S, Sagné E, Skapski A, Citti C.

Infect Immun. 2010 Apr;78(4):1542-51. doi: 10.1128/IAI.01195-09.


Proteomics and pathway analyses of the milk fat globule in sheep naturally infected by Mycoplasma agalactiae provide indications of the in vivo response of the mammary epithelium to bacterial infection.

Addis MF, Pisanu S, Ghisaura S, Pagnozzi D, Marogna G, Tanca A, Biosa G, Cacciotto C, Alberti A, Pittau M, Roggio T, Uzzau S.

Infect Immun. 2011 Sep;79(9):3833-45. doi: 10.1128/IAI.00040-11.


Proteomics characterization of cytoplasmic and lipid-associated membrane proteins of human pathogen Mycoplasma fermentans M64.

Liu YC, Lin IH, Chung WJ, Hu WS, Ng WV, Lu CY, Huang TY, Shu HW, Hsiao KJ, Tsai SF, Chang CH, Lin CH.

PLoS One. 2012;7(4):e35304. doi: 10.1371/journal.pone.0035304.


Comparative genomic and proteomic analyses of two Mycoplasma agalactiae strains: clues to the macro- and micro-events that are shaping mycoplasma diversity.

Nouvel LX, Sirand-Pugnet P, Marenda MS, Sagné E, Barbe V, Mangenot S, Schenowitz C, Jacob D, Barré A, Claverol S, Blanchard A, Citti C.

BMC Genomics. 2010 Feb 2;11:86. doi: 10.1186/1471-2164-11-86.


Occurrence, plasticity, and evolution of the vpma gene family, a genetic system devoted to high-frequency surface variation in Mycoplasma agalactiae.

Nouvel LX, Marenda M, Sirand-Pugnet P, Sagné E, Glew M, Mangenot S, Barbe V, Barré A, Claverol S, Citti C.

J Bacteriol. 2009 Jul;191(13):4111-21. doi: 10.1128/JB.00251-09.


Phase-locked mutants of Mycoplasma agalactiae: defining the molecular switch of high-frequency Vpma antigenic variation.

Chopra-Dewasthaly R, Citti C, Glew MD, Zimmermann M, Rosengarten R, Jechlinger W.

Mol Microbiol. 2008 Mar;67(6):1196-210. doi: 10.1111/j.1365-2958.2007.06103.x.


Characterization and analysis of a stable serotype-associated membrane protein (P30) of Mycoplasma agalactiae.

Fleury B, Bergonier D, Berthelot X, Schlatter Y, Frey J, Vilei EM.

J Clin Microbiol. 2001 Aug;39(8):2814-22.


Disruption of the pdhB pyruvate dehydrogenase [corrected] gene affects colony morphology, in vitro growth and cell invasiveness of Mycoplasma agalactiae.

Hegde S, Rosengarten R, Chopra-Dewasthaly R.

PLoS One. 2015 Mar 23;10(3):e0119706. doi: 10.1371/journal.pone.0119706. Erratum in: PLoS One. 2015;10(6):e0131134.


Rapid differential diagnosis of Mycoplasma agalactiae and Mycoplasma bovis based on a multiplex-PCR and a PCR-RFLP.

Foddai A, Idini G, Fusco M, Rosa N, de la Fe C, Zinellu S, Corona L, Tola S.

Mol Cell Probes. 2005 Jun;19(3):207-12.


The proteome of Mycoplasma pneumoniae, a supposedly "simple" cell.

Catrein I, Herrmann R.

Proteomics. 2011 Sep;11(18):3614-32. doi: 10.1002/pmic.201100076. Review.


Molecular characterization of the Mycoplasma bovis p68 gene, encoding a basic membrane protein with homology to P48 of Mycoplasma agalactiae.

Lysnyansky I, Yogev D, Levisohn S.

FEMS Microbiol Lett. 2008 Feb;279(2):234-42. doi: 10.1111/j.1574-6968.2007.01040.x.


[The adaptation of mycoplasmas to stress conditions: features of proteome shift in Mycoplasma hominis PG37 under starvation and low temperature].

Chernov VM, Chernova OA, Baranova NB, Gorshkov OV, Medvedeva ES, Shaĭmardanova GF.

Mol Biol (Mosk). 2011 Sep-Oct;45(5):914-23. Russian.


A real-time PCR assay for detection and quantification of Mycoplasma agalactiae DNA.

Lorusso A, Decaro N, Greco G, Corrente M, Fasanella A, Buonavoglia D.

J Appl Microbiol. 2007 Oct;103(4):918-23.


Xer1-mediated site-specific DNA inversions and excisions in Mycoplasma agalactiae.

Czurda S, Jechlinger W, Rosengarten R, Chopra-Dewasthaly R.

J Bacteriol. 2010 Sep;192(17):4462-73. doi: 10.1128/JB.01537-09.


Core proteome of the minimal cell: comparative proteomics of three mollicute species.

Fisunov GY, Alexeev DG, Bazaleev NA, Ladygina VG, Galyamina MA, Kondratov IG, Zhukova NA, Serebryakova MV, Demina IA, Govorun VM.

PLoS One. 2011;6(7):e21964. doi: 10.1371/journal.pone.0021964.


The cell-envelope proteome of Bifidobacterium longum in an in vitro bile environment.

Ruiz L, Couté Y, Sánchez B, de los Reyes-Gavilán CG, Sanchez JC, Margolles A.

Microbiology. 2009 Mar;155(Pt 3):957-67. doi: 10.1099/mic.0.024273-0.

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