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C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates.
Loessner MJ, Kramer K, Ebel F, Scherer S. Loessner MJ, et al. Mol Microbiol. 2002 Apr;44(2):335-49. doi: 10.1046/j.1365-2958.2002.02889.x. Mol Microbiol. 2002. PMID: 11972774
A new procedure for efficient recovery of DNA, RNA, and proteins from Listeria cells by rapid lysis with a recombinant bacteriophage endolysin.
Loessner MJ, Schneider A, Scherer S. Loessner MJ, et al. Appl Environ Microbiol. 1995 Mar;61(3):1150-2. doi: 10.1128/AEM.61.3.1150-1152.1995. Appl Environ Microbiol. 1995. PMID: 7540820 Free PMC article.
Organization and transcriptional analysis of the Listeria phage A511 late gene region comprising the major capsid and tail sheath protein genes cps and tsh.
Loessner MJ, Scherer S. Loessner MJ, et al. J Bacteriol. 1995 Nov;177(22):6601-9. doi: 10.1128/jb.177.22.6601-6609.1995. J Bacteriol. 1995. PMID: 7592439 Free PMC article.
Supplementary Listeria-typing with defective Listeria phage particles (monocins).
Zink R, Loessner MJ, Glas I, Scherer S. Zink R, et al. Lett Appl Microbiol. 1994 Aug;19(2):99-101. doi: 10.1111/j.1472-765x.1994.tb00915.x. Lett Appl Microbiol. 1994. PMID: 7765224
Structural proteins and DNA characteristics of 14 Listeria typing bacteriophages.
Loessner MJ, Krause IB, Henle T, Scherer S. Loessner MJ, et al. J Gen Virol. 1994 Apr;75 ( Pt 4):701-10. doi: 10.1099/0022-1317-75-4-701. J Gen Virol. 1994. PMID: 8151288
Heterogeneous endolysins in Listeria monocytogenes bacteriophages: a new class of enzymes and evidence for conserved holin genes within the siphoviral lysis cassettes.
Loessner MJ, Wendlinger G, Scherer S. Loessner MJ, et al. Mol Microbiol. 1995 Jun;16(6):1231-41. doi: 10.1111/j.1365-2958.1995.tb02345.x. Mol Microbiol. 1995. PMID: 8577256
They encode proteins of structural similarity to the product of phage lambda gene S, and are predicted to be membrane proteins which form pores to allow access of the lysins to their peptidoglycan substrates. ...
They encode proteins of structural similarity to the product of phage lambda gene S, and are predicted to be membrane proteins which …
Modified Listeria bacteriophage lysin genes (ply) allow efficient overexpression and one-step purification of biochemically active fusion proteins.
Loessner MJ, Schneider A, Scherer S. Loessner MJ, et al. Appl Environ Microbiol. 1996 Aug;62(8):3057-60. doi: 10.1128/AEM.62.8.3057-3060.1996. Appl Environ Microbiol. 1996. PMID: 8702301 Free PMC article.
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