about
A computational study of the glycine-rich loop of mitochondrial processing peptidaseStructure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestisExpression and kinetic characterization of methylmalonyl-CoA mutase from patients with the mut- phenotype: evidence for naturally occurring interallelic complementationReductive evolution of the mitochondrial processing peptidases of the unicellular parasites trichomonas vaginalis and giardia intestinalisAdaptation of an L-proline adenylation domain to use 4-propyl-L-proline in the evolution of lincosamide biosynthesisCleavage site selection within a folded substrate by the ATP-dependent lon protease.Elucidation of salicylate attachment in celesticetin biosynthesis opens the door to create a library of more efficient hybrid lincosamide antibioticsPrevalence of resistance mechanisms against macrolides and lincosamides in methicillin-resistant coagulase-negative staphylococci in the Czech Republic and occurrence of an undefined mechanism of resistance to lincosamides.Lincomycin biosynthesis involves a tyrosine hydroxylating heme protein of an unusual enzyme family.Lincosamide synthetase--a unique condensation system combining elements of nonribosomal peptide synthetase and mycothiol metabolism.Spore-specific modification of DNA-dependent RNA polymerase alpha subunit in streptomycetes--a new model of transcription regulation.ClpP-independent function of ClpX interferes with telithromycin resistance conferred by Msr(A) in Staphylococcus aureus.A new evolutionary variant of the streptogramin A resistance protein, Vga(A)LC, from Staphylococcus haemolyticus with shifted substrate specificity towards lincosamides.Deacetylation of mycothiol-derived 'waste product' triggers the last biosynthetic steps of lincosamide antibiotics.An Advanced System of the Mitochondrial Processing Peptidase and Core Protein Family in Trypanosoma brucei and Multiple Origins of the Core I Subunit in Eukaryotes.Sequence analysis of porothramycin biosynthetic gene cluster.Mutasynthesis of lincomycin derivatives with activity against drug-resistant staphylococci.Detailed mutational analysis of Vga(A) interdomain linker: implication for antibiotic resistance specificity and mechanism.Putative lmbI and lmbH genes form a single lmbIH ORF in Streptomyces lincolnensis type strain ATCC 25466.Subunit-subunit interactions are weakened in mutant forms of acetohydroxy acid synthase insensitive to valine inhibition.Glycine-rich loop of mitochondrial processing peptidase alpha-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20.Characterization of N-demethyllincosamide methyltransferases LmbJ and CcbJ.Changes in the incidence of periodontal pathogens during long-term monitoring and after application of antibacterial drugs.Substrate evokes translocation of both domains in the mitochondrial processing peptidase alpha-subunit during which the C-terminus acts as a stabilizing element.l-3,4-Dihydroxyphenyl alanine-extradiol cleavage is followed by intramolecular cyclization in lincomycin biosynthesis.In vitro activity of telithromycin and quinupristin/dalfopristin against methicillin-resistant coagulase-negative staphylococci with defined resistance genotypes.Hybridization analysis and mapping of the celesticetin gene cluster revealed genes shared with lincomycin biosynthesis.Diversity of Alkylproline Moieties in Pyrrolobenzodiazepines Arises from Postcondensation Modifications of a Unified Building Block.Biosynthesis and incorporation of an alkylproline-derivative (APD) precursor into complex natural products.Translation initiation factors of a tetracycline-producing strain of Streptomyces aureofaciens.Structure of the CcbJ Methyltransferase from Streptomyces caelestisStructure of the CcbJ Methyltransferase from Streptomyces caelestisHigh-throughput quantification of lincomycin traces in fermentation broth of genetically modified Streptomyces sppLmbJ and LmbIH protein levels correlate with lincomycin production in Streptomyces lincolnensisDifferent Reaction Specificities of F420H2-Dependent Reductases Facilitate Pyrrolobenzodiazepines and Lincomycin To Fit Their Biological Targets
P50
Q27306794-202BA320-78AD-4A57-88CD-02E6317A1F53Q27689753-1D25DABA-91DB-489B-8E44-7BB97A69E32FQ28248139-D4A96E82-3E58-4C0E-A3C7-C9CFB0FB3C48Q28474319-EB155731-C980-429A-988C-E6EA42525AB5Q28538073-88B21057-AE6F-4E52-96F1-C93705ABF0C1Q33214663-50418158-6756-4F66-BFDD-D6068F879874Q33636153-47AA6DE7-B93D-49FF-84BF-9122C7A43F26Q33938215-3B7ACF0D-199A-4039-B1FE-1378AB740D40Q35063699-26377B4A-491F-488E-A0CE-961299E0D15AQ35571970-6DC1C174-86E7-4311-8402-D3A2D648E7DFQ35672246-11EC3689-0413-4E4D-A0CB-0ACC63465D33Q40675976-BE3C5E51-1789-46BC-A216-906669EA99EEQ40902773-34955DD6-A141-4DF4-B762-8E6DFA0B0598Q41068742-38C98C3E-9D3B-4D9A-A501-9C4D738DFB69Q41581700-E2DADC55-4AB3-47C6-9181-9285990E1205Q41773669-B9B409CE-7026-4C04-86A2-C83C29D2B347Q41812922-76965BE3-3FC0-465C-927C-310E888CA2B0Q42076814-2A513348-AA36-4070-B018-184B62644266Q42668719-6563E5B7-0AC0-45B5-9697-22B1A7C8702FQ43182361-7D8C9AFC-1E80-46C2-9490-7B138E4A344EQ43201368-384451C0-A65B-4269-A039-2441A0DF110BQ44387963-6CDF315E-421D-42FD-B45B-82FB17F4F5B2Q44523021-561B7B40-4974-405D-90BF-E6A23D972B07Q44788177-32C6FE33-1F87-4EB3-8286-A07C23E5C6D0Q45049948-F7A576F5-8D42-4445-AAAE-892E846F37F2Q46616859-40E67658-3F6D-404F-AE5D-54D4E5DA54EBQ46735393-A0E7D127-209F-49F5-A849-202397686590Q48139868-3142AAFF-F29A-4C5D-AA9C-FF3145C91AB3Q52667248-254CCB25-6442-4DBA-A1DC-AC04A23596E1Q54615465-EE2CC399-8CA5-4D2B-8EBF-5C751EAA945AQ63648146-E28249A2-4973-4A38-8F7E-B185DCE0B493Q63648148-02A49D4A-F29F-4C11-A5FB-0C08A8875C9EQ63648154-8FB5A1D5-E702-4A28-8E65-6518E6454BE8Q63648158-A42848FA-B7EC-4851-8C76-893A5FDCF6B8Q92687021-A8176111-0246-44B2-B3A1-02D0D468AA8A
P50
description
mikrobiolog
@cs
onderzoeker
@nl
researcher, ORCID id # 0000-0002-4582-2062
@en
name
Jirí Janata
@ast
Jirí Janata
@es
Jirí Janata
@nl
Jiří Janata
@cs
Jiří Janata
@en
type
label
Jirí Janata
@ast
Jirí Janata
@es
Jirí Janata
@nl
Jiří Janata
@cs
Jiří Janata
@en
prefLabel
Jirí Janata
@ast
Jirí Janata
@es
Jirí Janata
@nl
Jiří Janata
@cs
Jiří Janata
@en
P214
P21
P214
P31
P496
0000-0002-4582-2062
P691
P7859
lccn-n00097211