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Article: Beyond comparison--antibiotics from genome data?

Alekshun, M N

2001 Volume 19, Issue 12, Page(s) 1124–1125

MeSH term(s)	Anti-Bacterial Agents/pharmacology ; Drug Design ; Drug Resistance/genetics ; Genome, Bacterial
Chemical Substances	Anti-Bacterial Agents
Language	English
Publishing date	2001-12
Publishing country	United States
Document type	News
ZDB-ID	1311932-1
ISSN	1546-1696 ; 1087-0156
ISSN (online)	1546-1696
ISSN	1087-0156
DOI	10.1038/nbt1201-1124
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Article: Commensals upon us.

Alekshun, M N / Levy, S B

Biochemical pharmacology

2006 Volume 71, Issue 7, Page(s) 893–900

Abstract: A battle to control and curtail bacterial infectious diseases is being waged in our hospitals and communities through antibiotic therapies and vaccines targeting specific species. But what effects do these interventions have on the epidemiology of ... ...

Abstract	A battle to control and curtail bacterial infectious diseases is being waged in our hospitals and communities through antibiotic therapies and vaccines targeting specific species. But what effects do these interventions have on the epidemiology of infections caused by the organisms that are part of our natural microbial flora? Gram-positive and gram-negative bacteria appear as new disease agents from among commensal flora. These include vancomycin resistant enterococci (VRE), community-associated methicillin resistant Staphylococcus aureus (CA-MRSA), non-vaccine invasive serotypes of Streptococcus pneumoniae, new strains of non-type b Haemophilus influenzae and multi-drug resistant Escherichia coli. These examples illustrate how clinical improvements and widespread use and misuse of antibiotics have pushed evolution, allowing normally non-pathogenic strains to become infectious disease threats to human health.
MeSH term(s)	Anti-Bacterial Agents/therapeutic use ; Bacterial Infections/immunology ; Bacterial Infections/microbiology ; Community-Acquired Infections/microbiology ; Drug Resistance, Microbial ; Host-Parasite Interactions/physiology ; Humans ; Infection Control/methods ; Public Health ; Symbiosis/physiology
Chemical Substances	Anti-Bacterial Agents
Language	English
Publishing date	2006-03-30
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	208787-x
ISSN	1873-2968 ; 0006-2952
ISSN (online)	1873-2968
ISSN	0006-2952
DOI	10.1016/j.bcp.2005.12.040
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Article: The mar regulon: multiple resistance to antibiotics and other toxic chemicals.

Alekshun, M N / Levy, S B

Trends in microbiology

1999 Volume 7, Issue 10, Page(s) 410–413

Abstract: The chromosomal multiple antibiotic resistance (mar) locus of Escherichia coli and other members of the Enterobacteriaceae controls resistance to multiple, structurally unrelated compounds including antibiotics, household disinfectants, organic solvents ... ...

Abstract	The chromosomal multiple antibiotic resistance (mar) locus of Escherichia coli and other members of the Enterobacteriaceae controls resistance to multiple, structurally unrelated compounds including antibiotics, household disinfectants, organic solvents and other toxic chemicals. The Mar phenotype is induced following exposure to a variety of chemicals with aromatic rings.
MeSH term(s)	Anti-Bacterial Agents/pharmacology ; Disinfectants/pharmacology ; Drug Resistance, Microbial/genetics ; Drug Resistance, Multiple/genetics ; Escherichia coli/drug effects ; Escherichia coli/genetics ; Humans ; Regulon ; Solvents/pharmacology
Chemical Substances	Anti-Bacterial Agents ; Disinfectants ; Solvents
Language	English
Publishing date	1999-10
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	1158963-2
ISSN	1878-4380 ; 0966-842X
ISSN (online)	1878-4380
ISSN	0966-842X
DOI	10.1016/s0966-842x(99)01589-9
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Article: Alteration of the repressor activity of MarR, the negative regulator of the Escherichia coli marRAB locus, by multiple chemicals in vitro.

Alekshun, M N / Levy, S B

Journal of bacteriology

1999 Volume 181, Issue 15, Page(s) 4669–4672

Abstract: MarR negatively regulates expression of the multiple antibiotic resistance operon (marRAB) in Escherichia coli. In this study, it was demonstrated that sodium salicylate, plumbagin, 2, 4-dinitrophenol, and menadione-inducers of the marRAB operon in whole ...

Abstract	MarR negatively regulates expression of the multiple antibiotic resistance operon (marRAB) in Escherichia coli. In this study, it was demonstrated that sodium salicylate, plumbagin, 2, 4-dinitrophenol, and menadione-inducers of the marRAB operon in whole cells-all interfered with the repressor activity of MarR in vitro. It is proposed that these compounds can interact directly with MarR to affect its repressor activity.
MeSH term(s)	2,4-Dinitrophenol/pharmacology ; Antineoplastic Agents, Phytogenic/pharmacology ; Bacterial Proteins/metabolism ; Drug Resistance, Microbial/genetics ; Escherichia coli/drug effects ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins ; Naphthoquinones/pharmacology ; Operon/drug effects ; Plasmids ; Repressor Proteins/metabolism ; Restriction Mapping ; Sodium Salicylate/pharmacology ; Vitamin K/pharmacology
Chemical Substances	Antineoplastic Agents, Phytogenic ; Bacterial Proteins ; Escherichia coli Proteins ; MarR protein, E coli ; Naphthoquinones ; Repressor Proteins ; Vitamin K (12001-79-5) ; 2,4-Dinitrophenol (Q13SKS21MN) ; Sodium Salicylate (WIQ1H85SYP) ; plumbagin (YAS4TBQ4OQ)
Language	English
Publishing date	1999-08
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.181.15.4669-4672.1999
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Article: Characterization of MarR superrepressor mutants.

Alekshun, M N / Levy, S B

Journal of bacteriology

1999 Volume 181, Issue 10, Page(s) 3303–3306

Abstract: MarR negatively regulates expression of the multiple antibiotic resistance (mar) locus in Escherichia coli. Superrepressor mutants, generated in order to study regions of MarR required for function, exhibited altered inducer recognition properties in ... ...

Abstract	MarR negatively regulates expression of the multiple antibiotic resistance (mar) locus in Escherichia coli. Superrepressor mutants, generated in order to study regions of MarR required for function, exhibited altered inducer recognition properties in whole cells and increased DNA binding to marO in vitro. Mutations occurred in three areas of the relatively small MarR protein (144 amino acids). It is surmised that superrepression results from increased DNA binding activities of these mutant proteins.
MeSH term(s)	Bacterial Proteins/biosynthesis ; Bacterial Proteins/genetics ; Bacterial Proteins/isolation & purification ; Bacterial Proteins/metabolism ; Base Sequence ; DNA Footprinting ; DNA, Bacterial/genetics ; DNA, Bacterial/metabolism ; DNA-Binding Proteins/biosynthesis ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/isolation & purification ; DNA-Binding Proteins/metabolism ; Deoxyribonucleases, Type II Site-Specific/metabolism ; Escherichia coli/genetics ; Escherichia coli Proteins ; Gene Expression Regulation, Bacterial ; Genes, Bacterial/genetics ; Genes, Reporter ; Molecular Sequence Data ; Phenotype ; Protein Binding ; Repressor Proteins/biosynthesis ; Repressor Proteins/genetics ; Repressor Proteins/isolation & purification ; Repressor Proteins/metabolism ; Selection, Genetic ; Suppression, Genetic ; beta-Galactosidase/metabolism
Chemical Substances	Bacterial Proteins ; DNA, Bacterial ; DNA-Binding Proteins ; Escherichia coli Proteins ; MarR protein, E coli ; Repressor Proteins ; endodeoxyribonuclease SspI (EC 3.1.21.-) ; Deoxyribonucleases, Type II Site-Specific (EC 3.1.21.4) ; beta-Galactosidase (EC 3.2.1.23)
Language	English
Publishing date	1999-05
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.181.10.3303-3306.1999
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Article: Regulation of chromosomally mediated multiple antibiotic resistance: the mar regulon.

Alekshun, M N / Levy, S B

Antimicrobial agents and chemotherapy

1997 Volume 41, Issue 10, Page(s) 2067–2075

MeSH term(s)	Animals ; Chromosomes, Bacterial/genetics ; Chromosomes, Bacterial/physiology ; Drug Resistance, Microbial/genetics ; Genes, Bacterial/genetics ; Genes, Bacterial/physiology ; Humans ; Regulon/genetics ; Regulon/physiology ; Transcription, Genetic/genetics
Language	English
Publishing date	1997-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	217602-6
ISSN	1098-6596 ; 0066-4804
ISSN (online)	1098-6596
ISSN	0066-4804
DOI	10.1128/AAC.41.10.2067
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Zs.A 809: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Einzelsignatur: Show issues

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Article: Mutational analysis of MarR, the negative regulator of marRAB expression in Escherichia coli, suggests the presence of two regions required for DNA binding.

Alekshun, M N / Kim, Y S / Levy, S B

Molecular microbiology

2000 Volume 35, Issue 6, Page(s) 1394–1404

Abstract: MarR, the negative regulator of the Escherichia coli multiple antibiotic resistance (marRAB) operon, is a member of a newly recognized family of regulatory proteins. The amino acid sequences of these proteins do not display any apparent homologies to the ...

Abstract	MarR, the negative regulator of the Escherichia coli multiple antibiotic resistance (marRAB) operon, is a member of a newly recognized family of regulatory proteins. The amino acid sequences of these proteins do not display any apparent homologies to the DNA binding domains of prokaryotic transcription regulators and a DNA binding motif for any one of the MarR homologues is currently unknown. In order to define regions of MarR required for DNA binding, mutant repressors, selected based on their ability to interfere with (negatively complement) the activity of wild-type MarR, were isolated. As determined using gel mobility shift assays, 13 out of 14 negative complementing mutants tested were unable to bind DNA in vitro. Three negative complementing alleles presumably specify truncated repressors and one of these proteins, a 120 residue MarR, can bind DNA in vitro. Most of the negative complementing mutations were clustered within two areas of MarR with features related to a helix-turn-helix DNA binding motif. These regions are presumed to be required for the DNA binding activity of the repressor.
MeSH term(s)	Amino Acid Motifs ; Amino Acid Sequence ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; DNA, Bacterial/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Escherichia coli/genetics ; Escherichia coli Proteins ; Gene Expression Regulation, Bacterial ; Genetic Complementation Test ; Molecular Sequence Data ; Mutation ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Sequence Homology, Amino Acid
Chemical Substances	Bacterial Proteins ; DNA, Bacterial ; DNA-Binding Proteins ; Escherichia coli Proteins ; MarA protein, E coli ; MarR protein, E coli ; Repressor Proteins ; multiple antibiotic resistance protein B
Language	English
Publishing date	2000-03
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1046/j.1365-2958.2000.01802.x
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Article: The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution.

Alekshun, M N / Levy, S B / Mealy, T R / Seaton, B A / Head, J F

Nature structural biology

2001 Volume 8, Issue 8, Page(s) 710–714

Abstract: MarR is a regulator of multiple antibiotic resistance in Escherichia coli. It is the prototypical member of the MarR family of regulatory proteins found in bacteria and archaea that play important roles in the development of antibiotic resistance, a ... ...

Abstract	MarR is a regulator of multiple antibiotic resistance in Escherichia coli. It is the prototypical member of the MarR family of regulatory proteins found in bacteria and archaea that play important roles in the development of antibiotic resistance, a global health problem. Here we describe the crystal structure of the MarR protein, determined at a resolution of 2.3 A. This is the first reported crystal structure of a member of this newly-described protein family. The structure shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.
MeSH term(s)	Amino Acid Motifs ; Amino Acid Sequence ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Binding Sites ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Dimerization ; Drug Resistance, Microbial ; Drug Resistance, Multiple ; Escherichia coli/chemistry ; Escherichia coli Proteins ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; Repressor Proteins/chemistry ; Repressor Proteins/metabolism ; Salicylates/metabolism ; Sequence Alignment
Chemical Substances	Bacterial Proteins ; DNA-Binding Proteins ; Escherichia coli Proteins ; MarR protein, E coli ; Protein Subunits ; Repressor Proteins ; Salicylates
Language	English
Publishing date	2001-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1192623-5
ISSN	1072-8368
ISSN	1072-8368
DOI	10.1038/90429
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Article: Multidrug resistance following expression of the Escherichia coli marA gene in Mycobacterium smegmatis.

McDermott, P F / White, D G / Podglajen, I / Alekshun, M N / Levy, S B

Journal of bacteriology

1998 Volume 180, Issue 11, Page(s) 2995–2998

Abstract: ... turn-helix domain, failed to produce the multiresistance phenotype in E. coli and M. smegmatis ... functions in M. smegmatis and that a mar-like regulatory system exists in this organism. ...

Abstract	Expression of the Escherichia coli multiple antibiotic resistance marA gene cloned in Mycobacterium smegmatis produced increased resistance to multiple antimicrobial agents, including rifampin, isoniazid, ethambutol, tetracycline, and chloramphenicol. Cloned marR or marA cloned in the antisense direction had no effect. Resistance changes were lost with spontaneous loss of the plasmid bearing marA. A MarA mutant protein, having an insertional mutation within either of its two alpha-helices of the first putative helix-turn-helix domain, failed to produce the multiresistance phenotype in E. coli and M. smegmatis, indicating that this region is critical for MarA function. These results strongly suggest that E. coli marA functions in M. smegmatis and that a mar-like regulatory system exists in this organism.
MeSH term(s)	Bacterial Proteins/genetics ; Chaperonin 60/genetics ; DNA-Binding Proteins/genetics ; Drug Resistance, Microbial/genetics ; Drug Resistance, Multiple/genetics ; Escherichia coli/drug effects ; Escherichia coli/genetics ; Escherichia coli Proteins ; Gene Expression ; Helix-Turn-Helix Motifs ; Mycobacterium/drug effects ; Mycobacterium/genetics ; Promoter Regions, Genetic/genetics ; Recombinant Fusion Proteins
Chemical Substances	Bacterial Proteins ; Chaperonin 60 ; DNA-Binding Proteins ; Escherichia coli Proteins ; MarA protein, E coli ; Recombinant Fusion Proteins
Language	English
Publishing date	1998-06
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.180.11.2995-2998.1998
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Article ; Online: Bortezomib salvage followed by a Phase I/II study of bortezomib plus high-dose melphalan and tandem autologous transplantation for patients with primary resistant myeloma.

British journal of haematology

2012 Volume 157, Issue 5, Page(s) 553–563

Abstract: ... with granulocyte colony-stimulating factor and harvest. Melphalan 100 mg/m(2) per day on two consecutive days was administered, immediately ... noted in 45% of patients. The maximum planned dose of bortezomib at 1·3 mg/m(2) was well tolerated and ...

Abstract	We conducted a Phase 1/2 study of bortezomib administered in combination with high-dose melphalan followed by tandem autologous transplants in patients with primary resistant multiple myeloma. Thirty patients received two cycles of salvage bortezomib followed by stem cell mobilization with granulocyte colony-stimulating factor and harvest. Melphalan 100 mg/m(2) per day on two consecutive days was administered, immediately followed by one dose of bortezomib (dose escalation) and stem cell infusion. The median beta 2-microglobulin was 4·35 mg/l (range: 1·8-11·4); albumin was 37 g/l (range: 3·1-4·9); high-risk karyotypes were noted in 45% of patients. The maximum planned dose of bortezomib at 1·3 mg/m(2) was well tolerated and a formal maximum tolerated dose was not determined. The peak of best overall response (≥partial response) and complete response rates after tandem transplants were 84% and 36%, respectively. With a median follow-up of 48 months, the median progression-free survival was 15 [95% confidence interval (CI): 11-21] months and the median overall survival was 35 (95% CI: 22-43) months. Correlative studies demonstrated decreased expression of BRCA2 (P = 0·0072) and FANCF (P = 0·0458) mRNA following bortezomib treatment. Bortezomib combined with high-dose melphalan is a well-tolerated conditioning with some activity in patients with resistant myeloma.
MeSH term(s)	Adult ; Aged ; Antineoplastic Combined Chemotherapy Protocols/adverse effects ; Antineoplastic Combined Chemotherapy Protocols/therapeutic use ; Boronic Acids/administration & dosage ; Bortezomib ; Disease Progression ; Fanconi Anemia Complementation Group Proteins/metabolism ; Female ; Hematopoietic Stem Cell Transplantation ; Humans ; Male ; Melphalan/administration & dosage ; Middle Aged ; Multiple Myeloma/metabolism ; Multiple Myeloma/mortality ; Multiple Myeloma/therapy ; Pyrazines/administration & dosage ; Salvage Therapy ; Signal Transduction ; Survival Analysis ; Transplantation Conditioning ; Transplantation, Autologous ; Treatment Outcome
Chemical Substances	Boronic Acids ; Fanconi Anemia Complementation Group Proteins ; Pyrazines ; Bortezomib (69G8BD63PP) ; Melphalan (Q41OR9510P)
Language	English
Publishing date	2012-03-26
Publishing country	England
Document type	Clinical Trial, Phase I ; Clinical Trial, Phase II ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80077-6
ISSN	1365-2141 ; 0007-1048
ISSN (online)	1365-2141
ISSN	0007-1048
DOI	10.1111/j.1365-2141.2012.09099.x
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