About: Role of the Hydrophobic Bridge in the Carbapenemase Activity of Class D β-Lactamases

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Role of the Hydrophobic Bridge in the Carbapenemase Activity of Class D β-Lactamases Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article published on 29 January 2019

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) artículu científicu espublizáu en xineru de 2019 (ast) scientific article published on 29 January 2019 (en) наукова стаття, опублікована 29 січня 2019 (uk)
publication date	wds:Q90364704-51058C6A-DD8D-4D84-9259-DFBEC2575474
publication date	2019-01-29 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q90364704-A7A10154-C430-48A3-8BD7-77A477C2C805
language of work or name	English
cites work	wds:Q90364704-0F95B1C5-4D65-455C-B9FA-A101E1340276 wds:Q90364704-0FF3A707-2133-45E7-BA59-23614053D0CF wds:Q90364704-2AFBA04B-9A60-46C3-851A-631B920B480C wds:Q90364704-2D34EB73-DD73-4076-A151-39F54D93CBB2 wds:Q90364704-37BC5B73-45C5-446A-9A53-E892B6774411 wds:Q90364704-51D5BCEA-0963-4234-817F-699EDEC35E45 wds:Q90364704-53333628-0328-49B0-8BB4-8B851ACBDC88 wds:Q90364704-58084A09-D4FC-42B6-9793-14D96B7BD975 wds:Q90364704-645B61FC-EC4C-4FFB-A507-03C7FF02F00B wds:Q90364704-6928AB86-DE50-4022-BCB9-8DB4FB05F8A2 wds:Q90364704-9F4E5CA8-3D0E-4648-9B88-18BC5C7EF9BF wds:Q90364704-BE4AB496-E402-42D2-99B9-8BC340EB2C1D wds:Q90364704-C6DFCA38-E450-44F7-A8C6-20B1ACF4AC77 wds:Q90364704-CA7A5C7F-CC0A-4B00-8491-77C6E09D6A8A wds:Q90364704-D21EDF5A-68FF-4ACB-AB82-11EFF98EC1CF wds:Q90364704-D5816CD9-BE9A-4311-A2CB-CFC365D317FA wds:Q90364704-EA8DA7EF-0E25-4AF1-88B5-1A14CAE56CEB
cites work	Clinical relevance of the ESKAPE pathogens PHENIX: a comprehensive Python-based system for macromolecular structure solution The 1.4 Å Crystal Structure of the Class D β-Lactamase OXA-1 Complexed with Doripenem Structures of the Class D Carbapenemase OXA-24 from Acinetobacter baumannii in Complex with Doripenem Structural Basis for Carbapenemase Activity of the OXA-23 β-Lactamase from Acinetobacter baumannii Class D β-lactamases: a reappraisal after five decades The determination of enzyme inhibitor constants Coot: model-building tools for molecular graphics Crystal structure of the OXA-48 beta-lactamase reveals mechanistic diversity among class D carbapenemases OXA β-lactamases Class D β-lactamases: are they all carbapenemases? Bacterial resistance to beta-lactam antibiotics: compelling opportunism, compelling opportunity Crystal structure of the carbapenemase OXA-24 reveals insights into the mechanism of carbapenem hydrolysis Design, Synthesis, and Crystal Structures of 6-Alkylidene-2′-Substituted Penicillanic Acid Sulfones as Potent Inhibitors of Acinetobacter baumannii OXA-24 Carbapenemase Acquired Class D β-Lactamases Structure-Function Relationships of Class D Carbapenemases. Active-Site Plasticity Is Essential to Carbapenem Hydrolysis by OXA-58 Class D β-Lactamase of Acinetobacter baumannii
author name string	wds:Q90364704-391B6E67-C7D8-40C6-B6BA-215A1F2B28C0 wds:Q90364704-7A01320B-9B6E-4CFA-99CC-F6D21361B7A0 wds:Q90364704-8E3FCFB5-5495-4167-8E92-56CB7519D8A9 wds:Q90364704-B49146B7-E701-48A4-8515-CFF8D78012DC wds:Q90364704-E5AD2073-6D3C-46B0-B511-C9837F7875E5
author name string	Clyde A Smith Marta Toth Sergei B Vakulenko Nuno T Antunes Nichole K Stewart
rdfs:label	Role of the Hydrophobic Bridge in the Carbapenemase Activity of Class D β-Lactamases (en) Role of the Hydrophobic Bridge in the Carbapenemase Activity of Class D β-Lactamases (nl)
skos:prefLabel	Role of the Hydrophobic Bridge in the Carbapenemase Activity of Class D β-Lactamases (en) Role of the Hydrophobic Bridge in the Carbapenemase Activity of Class D β-Lactamases (nl)
name	Role of the Hydrophobic Bridge in the Carbapenemase Activity of Class D β-Lactamases (en) Role of the Hydrophobic Bridge in the Carbapenemase Activity of Class D β-Lactamases (nl)
title	wds:Q90364704-6749F644-796D-4BD5-9F8A-F956C0E3FAF3
title	Role of the Hydrophobic Bridge in the Carbapenemase Activity of Class D β-Lactamases (en)
instance of	wds:Q90364704-6BA8F3F3-737C-4C85-A783-5B68C0CC59BE
instance of	scholarly article
PubMed ID	wds:Q90364704-A651FBF2-8D5D-4ADD-A3C7-1988C9BB7920
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30530607
PubMed ID	30530607
published in	wds:Q90364704-4740F931-1EDE-4122-81FC-4EA5A0381FB4
published in	Antimicrobial Agents and Chemotherapy
issue	wds:Q90364704-290E094F-A7E1-4A5A-AEEE-01BFCCD9C3CB
volume	wds:Q90364704-B93FB7C6-20F4-4590-ACF8-23375173D4A8
issue	2
volume	63
DOI	wds:Q90364704-0B957B1F-2B07-4ED6-A1E2-F608EECDDD40
DOI	http://dx.doi.org/10.1128/AAC.02191-18
DOI	10.1128/AAC.02191-18
PMCID	wds:Q90364704-9B92DCD8-E17F-4C99-BDEE-8E3407F110D4
PMCID	6355612
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q90364704
is cites work of	Mechanistic Insights into β-Lactamase-Catalysed Carbapenem Degradation Through Product Characterisation β-Lactamases and β-Lactamase Inhibitors in the 21st Century Structural Analysis of The OXA-48 Carbapenemase Bound to A "Poor" Carbapenem Substrate, Doripenem Structural Insights into the Mechanism of Carbapenemase Activity of the OXA-48 β-Lactamase Identifying Oxacillinase-48 Carbapenemase Inhibitors Using DNA-Encoded Chemical Libraries
is cites work of	wds:Q90197670-EEECED4F-F836-4DC1-BF1D-8E9E5ADA3444 wds:Q90079407-F9506CEF-B388-4FF4-8511-D1324871F174 wds:Q92930337-446CE977-676B-41FC-B83B-D511DE938754 wds:Q92264471-F1575514-F620-4D80-AA9A-88A7F80DDAEA wds:Q90391781-CB699D4B-F332-42EA-9190-A4EA2BFEFB98

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 188 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software