about
The Chemical Biology of Human Metallo-β-Lactamase Fold ProteinsRhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibitionUse of ferrous iron by metallo-β-lactamasesBiochemical characterization of New Delhi metallo-β-lactamase variants reveals differences in protein stability.Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy.Structural Basis of Metallo-β-Lactamase Inhibition by Captopril StereoisomersComparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition ProfilesBisthiazolidines: A Substrate-Mimicking Scaffold as an Inhibitor of the NDM-1 Carbapenemase.Insights into the Mechanistic Basis of Plasmid-Mediated Colistin Resistance from Crystal Structures of the Catalytic Domain of MCR-1NMR-filtered virtual screening leads to non-metal chelating metallo-β-lactamase inhibitorsThe road to avibactam: the first clinically useful non-β-lactam working somewhat like a β-lactam.Structural and Biochemical Characterization of Rm3, a Subclass B3 Metallo-β-Lactamase Identified from a Functional Metagenomic Study.Structural/mechanistic insights into the efficacy of non-classical β-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates.Sideromimic Modification of Lactivicin Dramatically Increases Potency against Extensively Drug-Resistant Stenotrophomonas maltophilia Clinical IsolatesAssay for drug discovery: Synthesis and testing of nitrocefin analogues for use as β-lactamase substrates.Monitoring conformational changes in the NDM-1 metallo-β-lactamase by 19F NMR spectroscopy.Cephalosporins inhibit human metallo β-lactamase fold DNA repair nucleases SNM1A and SNM1B/apollo.19 F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the São Paulo Metallo-β-Lactamase.Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates.Cation-π Interactions Contribute to Substrate Recognition in γ-Butyrobetaine Hydroxylase Catalysis.Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1†Electronic supplementary information (ESI) available: Procedures for protein expression and purification, 19F-labelling, crystallisation, data collection, and structure deStereoselective preparation of lipidated carboxymethyl-proline/pipecolic acid derivatives via coupling of engineered crotonases with an alkylmalonyl-CoA synthetase.Cyclobutanone Mimics of Intermediates in Metallo-β-Lactamase Catalysis.A New Mechanism for β-Lactamases: Class D Enzymes Degrade 1β-Methyl Carbapenems through Lactone Formation.13C-Carbamylation as a mechanistic probe for the inhibition of class D β-lactamases by avibactam and halide ions.New Delhi Metallo-β-Lactamase 1 Catalyzes Avibactam and Aztreonam Hydrolysis.Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition.Chromophore-linked substrate (CLS405): probing metallo-β-lactamase activity and inhibition.Ejection of structural zinc leads to inhibition of γ-butyrobetaine hydroxylaseNon-Hydrolytic β-Lactam Antibiotic Fragmentation by l,d-Transpeptidases and Serine β-Lactamase Cysteine VariantsWill morphing boron-based inhibitors beat the β-lactamases?Mechanistic Insights into β-Lactamase-Catalysed Carbapenem Degradation Through Product Characterisation19 F NMR Monitoring of Reversible Protein Post-Translational Modifications: Class D β-Lactamase Carbamylation and InhibitionBroad Spectrum β-Lactamase Inhibition by a Thioether Substituted Bicyclic BoronateA Fluorescence-Based Assay for Screening β-Lactams Targeting the Mycobacterium tuberculosis Transpeptidase LdtMt2Targeting the Mycobacterium tuberculosis transpeptidase LdtMt2 with cysteine-reactive inhibitors including ebselenMolecular Basis of Class A β-Lactamase Inhibition by RelebactamBicyclic Boronate VNRX-5133 Inhibits Metallo- and Serine-β-LactamasesBicyclic Boronates as Potent Inhibitors of AmpC, the Class C β-Lactamase from Escherichia coli
P50
Q26775167-39504969-9F0A-4FC4-90BF-5617D3195874Q27696197-FA793245-4D96-4D7C-8E3C-CB2459F679ACQ27725877-AE851091-CE0F-41C0-AD04-FB41678BB109Q34443982-E44303F6-2B9D-4601-BE0B-73A376ECFE8DQ34458551-308A2FD8-DD0C-4938-9365-9FAF43076BB2Q34498607-F4ADFF2D-755D-4C53-98A9-8733AE8BD78FQ34505085-48391F74-483A-4ED6-BE19-B0412D11826CQ37340068-DD37E83F-4C4E-4CC5-AF8E-BF52FE63CE43Q37563550-4D0A2EDC-9DD1-463E-AD1B-C4ECC66E9C85Q37725029-410FAA48-ED04-4424-A48A-13B0CCFC6AAFQ38850240-9A203EB2-2E55-4D52-ADAF-F28C3A4A8D01Q39588086-4EAF74BC-1321-4402-ADB0-C4BA0910F5C7Q40064693-25298C00-4460-4E05-B550-1A4A23E5DA24Q40690144-0746D7AC-1A8A-4582-92FC-55C52CB9C81BQ41123464-99C0EADA-DA41-45DF-B079-B52654CB074BQ41125182-73CC5781-20D5-4358-A24E-A185E44B0C39Q41453763-CD9102BA-76CB-4F87-AE00-A95DDC194088Q41775520-F2D4FDF7-9C24-448F-81A5-2ADD9C108694Q41983307-B76C4584-0967-413F-ABEC-93B8D95D9E84Q42012386-E5450D55-BA1F-4323-9775-5E314DD4F2E8Q42103741-1FE6AA8A-B644-4120-B582-22B60EA446D2Q46076921-B264D5CA-E0E7-4A43-8A25-757D45300C04Q46237711-A5E4F432-85E7-42D6-81B8-228B7E34E746Q47757046-DF14CAF1-38D6-477B-A2E8-A66B1304D0C4Q47983005-68E50B0B-9DBD-4149-B1C0-418543E8CB08Q48254391-39C6024F-CB0D-4AFC-82F4-22739E3BAA78Q53314946-5718FE15-9BE1-4A11-9F29-1050873A317FQ54301525-7510CD30-2EFB-4FEF-BC12-BC36424F2311Q57808496-A41B17CA-30EB-425C-A3AA-343F71F6FC7AQ64230466-5B0D5F5F-2741-467B-B8BB-1F78E65A6D3BQ90032232-53E40F30-E48B-4A29-874A-F3F0B054125EQ90197670-D235DDFE-BC2B-4609-9E43-E4E4A12A6EC0Q91921563-0DAE2497-FA20-4676-96C8-4E050BADD901Q92007379-8B4C9B06-CB03-4C44-AB15-91F4CAEF220DQ92019467-2AF3BBD7-0E86-4043-BBDB-46D06669519EQ92410879-D44E04F4-C89C-4AEC-84EC-FD399BEDEA2EQ92430039-9259427D-1172-429A-B52B-FFD534A78614Q92899649-F80EDC4D-0AD4-4FF5-875F-9A08F10A6E72Q96429021-F62E9E41-EEA0-44AA-A0AE-7501C172501E
P50
description
investigador
@es
researcher
@en
name
Jürgen Brem
@en
type
label
Jürgen Brem
@en
prefLabel
Jürgen Brem
@en
P31
P496
0000-0002-0137-3226