Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 38 entries
Sorted by: Best Match Show Resources per page
PL3 Amidase, a Tailor-made Lysin Constructed by Domain Shuffling with Potent Killing Activity against Pneumococci and Related Species.

Frontiers in microbiology

Blázquez B, Fresco-Taboada A, Iglesias-Bexiga M, Menéndez M, García P.
PMID: 27516758
Front Microbiol. 2016 Jul 28;7:1156. doi: 10.3389/fmicb.2016.01156. eCollection 2016.

The emergence and spread of antibiotic-resistant bacteria is pushing the need of alternative treatments. In this context, phage therapy is already a reality to successfully fight certain multiresistant bacteria. Among different phage gene products, murein hydrolases responsible of phage...

Cite
Blázquez B, Fresco-Taboada A, Iglesias-Bexiga M, et al. PL3 Amidase, a Tailor-made Lysin Constructed by Domain Shuffling with Potent Killing Activity against Pneumococci and Related Species. Front Microbiol. 2016;7:1156doi: 10.3389/fmicb.2016.01156.
Blázquez, B., Fresco-Taboada, A., Iglesias-Bexiga, M., Menéndez, M., & García, P. (2016). PL3 Amidase, a Tailor-made Lysin Constructed by Domain Shuffling with Potent Killing Activity against Pneumococci and Related Species. Frontiers in microbiology, 71156. https://doi.org/10.3389/fmicb.2016.01156
Blázquez, Blas, et al. "PL3 Amidase, a Tailor-made Lysin Constructed by Domain Shuffling with Potent Killing Activity against Pneumococci and Related Species." Frontiers in microbiology vol. 7 (2016): 1156. doi: https://doi.org/10.3389/fmicb.2016.01156
Blázquez B, Fresco-Taboada A, Iglesias-Bexiga M, Menéndez M, García P. PL3 Amidase, a Tailor-made Lysin Constructed by Domain Shuffling with Potent Killing Activity against Pneumococci and Related Species. Front Microbiol. 2016 Jul 28;7:1156. doi: 10.3389/fmicb.2016.01156. eCollection 2016. PMID: 27516758; PMCID: PMC4963390.
Copy Download .nbib Format: NLM
Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis .

F1000Research

Atila M, Luo Y.
PMID: 26998233
F1000Res. 2016 Jan 29;5:121. doi: 10.12688/f1000research.7842.1. eCollection 2016.

Cationic modulation of the dominantly negative electrostatic structure of phospholipids plays an important role in bacterial response to changes in the environment. In addition to zwitterionic phosphatidylethanolamine, Gram-positive bacteria are also abundant in positively charged lysyl-phosphatidylglycerol. Increased amounts of...

Cite
Atila M, Luo Y. Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis . F1000Res. 2016;5:121doi: 10.12688/f1000research.7842.1.
Atila, M., & Luo, Y. (2016). Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis . F1000Research, 5121. https://doi.org/10.12688/f1000research.7842.1
Atila, Metin, and Luo, Yu. "Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis ." F1000Research vol. 5 (2016): 121. doi: https://doi.org/10.12688/f1000research.7842.1
Atila M, Luo Y. Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis . F1000Res. 2016 Jan 29;5:121. doi: 10.12688/f1000research.7842.1. eCollection 2016. PMID: 26998233; PMCID: PMC4792211.
Copy Download .nbib Format: NLM
Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.

Frontiers in microbiology

Vermassen A, Leroy S, Talon R, Provot C, Popowska M, Desvaux M.
PMID: 30873139
Front Microbiol. 2019 Feb 28;10:331. doi: 10.3389/fmicb.2019.00331. eCollection 2019.

The cell wall (CW) of bacteria is an intricate arrangement of macromolecules, at least constituted of peptidoglycan (PG) but also of (lipo)teichoic acids, various polysaccharides, polyglutamate and/or proteins. During bacterial growth and division, there is a constant balance between...

Cite
Vermassen A, Leroy S, Talon R, et al. Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan. Front Microbiol. 2019;10:331doi: 10.3389/fmicb.2019.00331.
Vermassen, A., Leroy, S., Talon, R., Provot, C., Popowska, M., & Desvaux, M. (2019). Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan. Frontiers in microbiology, 10331. https://doi.org/10.3389/fmicb.2019.00331
Vermassen, Aurore, et al. "Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan." Frontiers in microbiology vol. 10 (2019): 331. doi: https://doi.org/10.3389/fmicb.2019.00331
Vermassen A, Leroy S, Talon R, Provot C, Popowska M, Desvaux M. Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan. Front Microbiol. 2019 Feb 28;10:331. doi: 10.3389/fmicb.2019.00331. eCollection 2019. PMID: 30873139; PMCID: PMC6403190.
Copy Download .nbib Format: NLM
Pneumococcal LytR Protein Is Required for the Surface Attachment of Both Capsular Polysaccharide and Teichoic Acids: Essential for Pneumococcal Virulence.

Frontiers in microbiology

Ye W, Zhang J, Shu Z, Yin Y, Zhang X, Wu K.
PMID: 29951042
Front Microbiol. 2018 Jun 13;9:1199. doi: 10.3389/fmicb.2018.01199. eCollection 2018.

The LytR-Cps-Psr family proteins are commonly present in Gram-positive bacteria, which have been shown to implicate in anchoring cell wall-related glycopolymers to the peptidoglycan. Here, we report the cellular function of SPD_1741 (LytR) in

Cite
Ye W, Zhang J, Shu Z, et al. Pneumococcal LytR Protein Is Required for the Surface Attachment of Both Capsular Polysaccharide and Teichoic Acids: Essential for Pneumococcal Virulence. Front Microbiol. 2018;9:1199doi: 10.3389/fmicb.2018.01199.
Ye, W., Zhang, J., Shu, Z., Yin, Y., Zhang, X., & Wu, K. (2018). Pneumococcal LytR Protein Is Required for the Surface Attachment of Both Capsular Polysaccharide and Teichoic Acids: Essential for Pneumococcal Virulence. Frontiers in microbiology, 91199. https://doi.org/10.3389/fmicb.2018.01199
Ye, Weijie, et al. "Pneumococcal LytR Protein Is Required for the Surface Attachment of Both Capsular Polysaccharide and Teichoic Acids: Essential for Pneumococcal Virulence." Frontiers in microbiology vol. 9 (2018): 1199. doi: https://doi.org/10.3389/fmicb.2018.01199
Ye W, Zhang J, Shu Z, Yin Y, Zhang X, Wu K. Pneumococcal LytR Protein Is Required for the Surface Attachment of Both Capsular Polysaccharide and Teichoic Acids: Essential for Pneumococcal Virulence. Front Microbiol. 2018 Jun 13;9:1199. doi: 10.3389/fmicb.2018.01199. eCollection 2018. PMID: 29951042; PMCID: PMC6008509.
Copy Download .nbib Format: NLM
Biosynthetic Mechanisms and Biological Significance of Glycerol Phosphate-Containing Glycan in Mammals.

Molecules (Basel, Switzerland)

Imae R, Manya H, Endo T.
PMID: 34771084
Molecules. 2021 Nov 04;26(21). doi: 10.3390/molecules26216675.

Bacteria contain glycerol phosphate (GroP)-containing glycans, which are important constituents of cell-surface glycopolymers such as the teichoic acids of Gram-positive bacterial cell walls. These glycopolymers comprising GroP play crucial roles in bacterial physiology and virulence. Recently, the first identification...

Cite
Imae R, Manya H, Endo T. Biosynthetic Mechanisms and Biological Significance of Glycerol Phosphate-Containing Glycan in Mammals. Molecules. 2021;26(21)doi: 10.3390/molecules26216675.
Imae, R., Manya, H., & Endo, T. (2021). Biosynthetic Mechanisms and Biological Significance of Glycerol Phosphate-Containing Glycan in Mammals. Molecules (Basel, Switzerland), 26(21), . https://doi.org/10.3390/molecules26216675
Imae, Rieko, et al. "Biosynthetic Mechanisms and Biological Significance of Glycerol Phosphate-Containing Glycan in Mammals." Molecules (Basel, Switzerland) vol. 26,21 (2021). doi: https://doi.org/10.3390/molecules26216675
Imae R, Manya H, Endo T. Biosynthetic Mechanisms and Biological Significance of Glycerol Phosphate-Containing Glycan in Mammals. Molecules. 2021 Nov 04;26(21). doi: 10.3390/molecules26216675. PMID: 34771084; PMCID: PMC8587909.
Copy Download .nbib Format: NLM
Wall teichoic acids govern cationic gold nanoparticle interaction with Gram-positive bacterial cell walls.

Chemical science

Caudill ER, Hernandez RT, Johnson KP, O'Rourke JT, Zhu L, Haynes CL, Feng ZV, Pedersen JA.
PMID: 34122876
Chem Sci. 2020 Mar 23;11(16):4106-4118. doi: 10.1039/c9sc05436g.

Molecular-level understanding of nanomaterial interactions with bacterial cell surfaces can facilitate design of antimicrobial and antifouling surfaces and inform assessment of potential consequences of nanomaterial release into the environment. Here, we investigate the interaction of cationic nanoparticles with the...

Cite
Caudill ER, Hernandez RT, Johnson KP, et al. Wall teichoic acids govern cationic gold nanoparticle interaction with Gram-positive bacterial cell walls. Chem Sci. 2020;11(16):4106-4118doi: 10.1039/c9sc05436g.
Caudill, E. R., Hernandez, R. T., Johnson, K. P., O'Rourke, J. T., Zhu, L., Haynes, C. L., Feng, Z. V., & Pedersen, J. A. (2020). Wall teichoic acids govern cationic gold nanoparticle interaction with Gram-positive bacterial cell walls. Chemical science, 11(16), 4106-4118. https://doi.org/10.1039/c9sc05436g
Caudill, Emily R, et al. "Wall teichoic acids govern cationic gold nanoparticle interaction with Gram-positive bacterial cell walls." Chemical science vol. 11,16 (2020): 4106-4118. doi: https://doi.org/10.1039/c9sc05436g
Caudill ER, Hernandez RT, Johnson KP, O'Rourke JT, Zhu L, Haynes CL, Feng ZV, Pedersen JA. Wall teichoic acids govern cationic gold nanoparticle interaction with Gram-positive bacterial cell walls. Chem Sci. 2020 Mar 23;11(16):4106-4118. doi: 10.1039/c9sc05436g. PMID: 34122876; PMCID: PMC8152635.
Copy Download .nbib Format: NLM
Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display.

Frontiers in microbiology

Desvaux M, Candela T, Serror P.
PMID: 29491848
Front Microbiol. 2018 Feb 14;9:100. doi: 10.3389/fmicb.2018.00100. eCollection 2018.

The cell envelope of parietal monoderm bacteria (archetypal Gram-positive bacteria) is formed of a cytoplasmic membrane (CM) and a cell wall (CW). While the CM is composed of phospholipids, the CW is composed at least of peptidoglycan (PG) covalently...

Cite
Desvaux M, Candela T, Serror P. Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display. Front Microbiol. 2018;9:100doi: 10.3389/fmicb.2018.00100.
Desvaux, M., Candela, T., & Serror, P. (2018). Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display. Frontiers in microbiology, 9100. https://doi.org/10.3389/fmicb.2018.00100
Desvaux, Mickaël, et al. "Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display." Frontiers in microbiology vol. 9 (2018): 100. doi: https://doi.org/10.3389/fmicb.2018.00100
Desvaux M, Candela T, Serror P. Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display. Front Microbiol. 2018 Feb 14;9:100. doi: 10.3389/fmicb.2018.00100. eCollection 2018. PMID: 29491848; PMCID: PMC5817068.
Copy Download .nbib Format: NLM
Teichoic acids: synthesis and applications.

Chemical Society reviews

van der Es D, Hogendorf WF, Overkleeft HS, van der Marel GA, Codée JD.
PMID: 27990523
Chem Soc Rev. 2017 Mar 06;46(5):1464-1482. doi: 10.1039/c6cs00270f.

This review describes the developments in the synthesis of teichoic acids (TA) - glycosylated poly(alditolphosphates) - and the application of these fragments in immunological studies. These structurally diverse biopolymers are omnipresent constituents of the Gram-positive bacterial cell wall where...

Cite
van der Es D, Hogendorf WF, Overkleeft HS, et al. Teichoic acids: synthesis and applications. Chem Soc Rev. 2017;46(5):1464-1482doi: 10.1039/c6cs00270f.
van der Es, D., Hogendorf, W. F., Overkleeft, H. S., van der Marel, G. A., & Codée, J. D. (2017). Teichoic acids: synthesis and applications. Chemical Society reviews, 46(5), 1464-1482. https://doi.org/10.1039/c6cs00270f
van der Es, Daan, et al. "Teichoic acids: synthesis and applications." Chemical Society reviews vol. 46,5 (2017): 1464-1482. doi: https://doi.org/10.1039/c6cs00270f
van der Es D, Hogendorf WF, Overkleeft HS, van der Marel GA, Codée JD. Teichoic acids: synthesis and applications. Chem Soc Rev. 2017 Mar 06;46(5):1464-1482. doi: 10.1039/c6cs00270f. PMID: 27990523.
Copy Download .nbib Format: NLM
Ultrastructural changes in methicillin-resistant Staphylococcus aureus induced by positively charged silver nanoparticles.

Beilstein journal of nanotechnology

Romero-Urbina DG, Lara HH, Velázquez-Salazar JJ, Arellano-Jiménez MJ, Larios E, Srinivasan A, Lopez-Ribot JL, Yacamán MJ.
PMID: 26734530
Beilstein J Nanotechnol. 2015 Dec 15;6:2396-405. doi: 10.3762/bjnano.6.246. eCollection 2015.

Silver nanoparticles offer a possible means of fighting antibacterial resistance. Most of their antibacterial properties are attributed to their silver ions. In the present work, we study the actions of positively charged silver nanoparticles against both methicillin-sensitive Staphylococcus aureus...

Cite
Romero-Urbina DG, Lara HH, Velázquez-Salazar JJ, et al. Ultrastructural changes in methicillin-resistant Staphylococcus aureus induced by positively charged silver nanoparticles. Beilstein J Nanotechnol. 2015;6:2396-405doi: 10.3762/bjnano.6.246.
Romero-Urbina, D. G., Lara, H. H., Velázquez-Salazar, J. J., Arellano-Jiménez, M. J., Larios, E., Srinivasan, A., Lopez-Ribot, J. L., & Yacamán, M. J. (2015). Ultrastructural changes in methicillin-resistant Staphylococcus aureus induced by positively charged silver nanoparticles. Beilstein journal of nanotechnology, 62396-405. https://doi.org/10.3762/bjnano.6.246
Romero-Urbina, Dulce G, et al. "Ultrastructural changes in methicillin-resistant Staphylococcus aureus induced by positively charged silver nanoparticles." Beilstein journal of nanotechnology vol. 6 (2015): 2396-405. doi: https://doi.org/10.3762/bjnano.6.246
Romero-Urbina DG, Lara HH, Velázquez-Salazar JJ, Arellano-Jiménez MJ, Larios E, Srinivasan A, Lopez-Ribot JL, Yacamán MJ. Ultrastructural changes in methicillin-resistant Staphylococcus aureus induced by positively charged silver nanoparticles. Beilstein J Nanotechnol. 2015 Dec 15;6:2396-405. doi: 10.3762/bjnano.6.246. eCollection 2015. PMID: 26734530; PMCID: PMC4685924.
Copy Download .nbib Format: NLM
Antimicrobial Peptides Targeting Gram-Positive Bacteria.

Pharmaceuticals (Basel, Switzerland)

Malanovic N, Lohner K.
PMID: 27657092
Pharmaceuticals (Basel). 2016 Sep 20;9(3). doi: 10.3390/ph9030059.

Antimicrobial peptides (AMPs) have remarkably different structures as well as biological activity profiles, whereupon most of these peptides are supposed to kill bacteria via membrane damage. In order to understand their molecular mechanism and target cell specificity for Gram-positive...

Cite
Malanovic N, Lohner K. Antimicrobial Peptides Targeting Gram-Positive Bacteria. Pharmaceuticals (Basel). 2016;9(3)doi: 10.3390/ph9030059.
Malanovic, N., & Lohner, K. (2016). Antimicrobial Peptides Targeting Gram-Positive Bacteria. Pharmaceuticals (Basel, Switzerland), 9(3), . https://doi.org/10.3390/ph9030059
Malanovic, Nermina, and Lohner, Karl. "Antimicrobial Peptides Targeting Gram-Positive Bacteria." Pharmaceuticals (Basel, Switzerland) vol. 9,3 (2016). doi: https://doi.org/10.3390/ph9030059
Malanovic N, Lohner K. Antimicrobial Peptides Targeting Gram-Positive Bacteria. Pharmaceuticals (Basel). 2016 Sep 20;9(3). doi: 10.3390/ph9030059. PMID: 27657092; PMCID: PMC5039512.
Copy Download .nbib Format: NLM
How Teichoic Acids Could Support a Periplasm in Gram-Positive Bacteria, and Let Cell Division Cheat Turgor Pressure.

Frontiers in microbiology

Erickson HP.
PMID: 34040598
Front Microbiol. 2021 May 10;12:664704. doi: 10.3389/fmicb.2021.664704. eCollection 2021.

The cytoplasm of bacteria is maintained at a higher osmolality than the growth medium, which generates a turgor pressure. The cell membrane (CM) cannot support a large turgor, so there are two possibilities for transferring the pressure to the...

Cite
Erickson HP. How Teichoic Acids Could Support a Periplasm in Gram-Positive Bacteria, and Let Cell Division Cheat Turgor Pressure. Front Microbiol. 2021;12:664704doi: 10.3389/fmicb.2021.664704.
Erickson, H. P. (2021). How Teichoic Acids Could Support a Periplasm in Gram-Positive Bacteria, and Let Cell Division Cheat Turgor Pressure. Frontiers in microbiology, 12664704. https://doi.org/10.3389/fmicb.2021.664704
Erickson, Harold P. "How Teichoic Acids Could Support a Periplasm in Gram-Positive Bacteria, and Let Cell Division Cheat Turgor Pressure." Frontiers in microbiology vol. 12 (2021): 664704. doi: https://doi.org/10.3389/fmicb.2021.664704
Erickson HP. How Teichoic Acids Could Support a Periplasm in Gram-Positive Bacteria, and Let Cell Division Cheat Turgor Pressure. Front Microbiol. 2021 May 10;12:664704. doi: 10.3389/fmicb.2021.664704. eCollection 2021. PMID: 34040598; PMCID: PMC8141598.
Copy Download .nbib Format: NLM
The Role of β-Glycosylated Wall Teichoic Acids in the Reduction of Vancomycin Susceptibility in Vancomycin-Intermediate Staphylococcus aureus.

Microbiology spectrum

Hort M, Bertsche U, Nozinovic S, Dietrich A, Schrötter AS, Mildenberger L, Axtmann K, Berscheid A, Bierbaum G.
PMID: 34668723
Microbiol Spectr. 2021 Oct 31;9(2):e0052821. doi: 10.1128/Spectrum.00528-21. Epub 2021 Oct 20.

Staphylococcus aureus is an opportunistic pathogen that causes a wide range of infections. Due to the rapid evolution of antibiotic resistance that leads to treatment failure, it is important to understand the underlying mechanisms. Here, the cell wall structures...

Cite
Hort M, Bertsche U, Nozinovic S, et al. The Role of β-Glycosylated Wall Teichoic Acids in the Reduction of Vancomycin Susceptibility in Vancomycin-Intermediate Staphylococcus aureus. Microbiol Spectr. 2021;9(2):e0052821doi: 10.1128/Spectrum.00528-21.
Hort, M., Bertsche, U., Nozinovic, S., Dietrich, A., Schrötter, A. S., Mildenberger, L., Axtmann, K., Berscheid, A., & Bierbaum, G. (2021). The Role of β-Glycosylated Wall Teichoic Acids in the Reduction of Vancomycin Susceptibility in Vancomycin-Intermediate Staphylococcus aureus. Microbiology spectrum, 9(2), e0052821. https://doi.org/10.1128/Spectrum.00528-21
Hort, Michael, et al. "The Role of β-Glycosylated Wall Teichoic Acids in the Reduction of Vancomycin Susceptibility in Vancomycin-Intermediate Staphylococcus aureus." Microbiology spectrum vol. 9,2 (2021): e0052821. doi: https://doi.org/10.1128/Spectrum.00528-21
Hort M, Bertsche U, Nozinovic S, Dietrich A, Schrötter AS, Mildenberger L, Axtmann K, Berscheid A, Bierbaum G. The Role of β-Glycosylated Wall Teichoic Acids in the Reduction of Vancomycin Susceptibility in Vancomycin-Intermediate Staphylococcus aureus. Microbiol Spectr. 2021 Oct 31;9(2):e0052821. doi: 10.1128/Spectrum.00528-21. Epub 2021 Oct 20. PMID: 34668723; PMCID: PMC8528128.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 38 entries