@article{MTMT:3378998,
	title = {Antibiotic-resistant bacteria show widespread collateral sensitivity to antimicrobial peptides},
	url = {https://m2.mtmt.hu/api/publication/3378998},
	author = {Lázár, Viktória and Martins, Ana and Spohn, Réka and Daruka, Lejla and Grézal, Gábor and Fekete, Gergely and Számel, Mónika and Jangir, Pramod Kumar and Kintses, Bálint and Csörgő, Bálint and Nyerges, Ákos and Györkei, Ádám and Kincses, András and Dér, András and Walter, Fruzsina and Deli, Mária Anna and Zsoldiné Urbán, Edit and Hegedüs, Zsófia and Olajos, Gábor and Méhi, Orsolya Katinka and Bálint, Balázs and Nagy, István and Martinek, Tamás and Papp, Balázs and Pál, Csaba},
	doi = {10.1038/s41564-018-0164-0},
	journal-iso = {NAT MICROBIOL},
	journal = {NATURE MICROBIOLOGY},
	volume = {3},
	unique-id = {3378998},
	issn = {2058-5276},
	abstract = {Antimicrobial peptides are promising alternative antimicrobial agents. However, little is known about whether resistance to small-molecule antibiotics leads to cross-resistance (decreased sensitivity) or collateral sensitivity (increased sensitivity) to antimicrobial peptides. We systematically addressed this question by studying the susceptibilities of a comprehensive set of 60 antibiotic-resistant Escherichia coli strains towards 24 antimicrobial peptides. Strikingly, antibiotic-resistant bacteria show a high frequency of collateral sensitivity to antimicrobial peptides, whereas cross-resistance is relatively rare. We identify clinically relevant multidrug-resistance mutations that increase bacterial sensitivity to antimicrobial peptides. Collateral sensitivity in multidrug-resistant bacteria arises partly through regulatory changes shaping the lipopolysaccharide composition of the bacterial outer membrane. These advances allow the identification of antimicrobial peptide-antibiotic combinations that enhance antibiotic activity against multidrug-resistant bacteria and slow down de novo evolution of resistance. In particular, when co-administered as an adjuvant, the antimicrobial peptide glycine-leucine-amide caused up to 30-fold decrease in the antibiotic resistance level of resistant bacteria. Our work provides guidelines for the development of efficient peptide-based therapies of antibiotic-resistant infections.},
	year = {2018},
	eissn = {2058-5276},
	pages = {718-731},
	orcid-numbers = {Grézal, Gábor/0000-0003-1685-4791; Jangir, Pramod Kumar/0000-0001-8330-0655; Csörgő, Bálint/0000-0003-0397-6845; Nyerges, Ákos/0000-0002-1581-490X; Walter, Fruzsina/0000-0001-8145-2823; Deli, Mária Anna/0000-0001-6084-6524; Zsoldiné Urbán, Edit/0000-0002-9602-7552; Hegedüs, Zsófia/0000-0002-5546-8167; Olajos, Gábor/0000-0002-2479-4891; Méhi, Orsolya Katinka/0009-0004-7918-913X; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:1920999,
	title = {Proline: a multifunctional amino acid},
	url = {https://m2.mtmt.hu/api/publication/1920999},
	author = {Szabados, László and Savoure, A},
	doi = {10.1016/j.tplants.2009.11.009},
	journal-iso = {TRENDS PLANT SCI},
	journal = {TRENDS IN PLANT SCIENCE},
	volume = {15},
	unique-id = {1920999},
	issn = {1360-1385},
	abstract = {Proline accumulates in many plant species in response to environmental stress. Although much is now known about proline metabolism, some aspects of its biological functions are still unclear. Here, we discuss the compartmentalization of proline biosynthesis, accumulation and degradation in the cytosol, chloroplast and mitochondria. We also describe the role of proline in cellular homeostasis, including redox balance and energy status. Proline can act as a signaling molecule to modulate mitochondrial functions, influence cell proliferation or cell death and trigger specific gene expression, which can be essential for plant recovery from stress. Although the regulation and function of proline accumulation are not yet completely understood, the engineering of proline metabolism could lead to new opportunities to improve plant tolerance of environmental stresses.},
	year = {2010},
	eissn = {1878-4372},
	pages = {89-97}
}