Philip Hinchliffe
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Explore the profile of Philip Hinchliffe including associated specialties, affiliations and a list of published articles.
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43
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1539
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Recent Articles
1.
Hinchliffe P, Calvopina K, Rabe P, Mojica M, Schofield C, Dmitrienko G, et al.
J Biol Chem
. 2024 Oct;
300(10):107819.
PMID: 39383701
No abstract available.
2.
Dynamical responses predict a distal site that modulates activity in an antibiotic resistance enzyme
Beer M, Oliveira A, Tooke C, Hinchliffe P, Tsz Yan Li A, Balega B, et al.
Chem Sci
. 2024 Oct;
PMID: 39364073
β-Lactamases, which hydrolyse β-lactam antibiotics, are key determinants of antibiotic resistance. Predicting the sites and effects of distal mutations in enzymes is challenging. For β-lactamases, the ability to make such...
3.
Villamil V, Rossi M, Mojica M, Hinchliffe P, Martinez V, Castillo V, et al.
J Med Chem
. 2024 Feb;
67(5):3795-3812.
PMID: 38373290
Antimicrobial resistance is a global public health threat. Metallo-β-lactamases (MBLs) inactivate β-lactam antibiotics, including carbapenems, are disseminating among Gram-negative bacteria, and lack clinically useful inhibitors. The evolving bisthiazolidine (BTZ) scaffold...
4.
Rossi M, Martinez V, Hinchliffe P, Mojica M, Castillo V, Moreno D, et al.
Chem Sci
. 2023 Sep;
14(34):9226.
PMID: 37655038
[This corrects the article DOI: 10.1039/D0SC05172A.].
5.
Tooke C, Hinchliffe P, Beer M, Zinovjev K, Colenso C, Schofield C, et al.
J Am Chem Soc
. 2023 Mar;
145(13):7166-7180.
PMID: 36972204
KPC-2 ( carbapenemase-2) is a globally disseminated serine-β-lactamase (SBL) responsible for extensive β-lactam antibiotic resistance in Gram-negative pathogens. SBLs inactivate β-lactams via a mechanism involving a hydrolytically labile covalent acyl-enzyme...
6.
Hinchliffe P, Calvopina K, Rabe P, Mojica M, Schofield C, Dmitrienko G, et al.
J Biol Chem
. 2023 Mar;
299(5):104606.
PMID: 36924941
L1 is a dizinc subclass B3 metallo-β-lactamase (MBL) that hydrolyzes most β-lactam antibiotics and is a key resistance determinant in the Gram-negative pathogen Stenotrophomonas maltophilia, an important cause of nosocomial...
7.
Hinchliffe P, Tooke C, Bethel C, Wang B, Arthur C, Heesom K, et al.
mBio
. 2022 May;
13(3):e0179321.
PMID: 35612361
β-Lactamases hydrolyze β-lactam antibiotics and are major determinants of antibiotic resistance in Gram-negative pathogens. Enmetazobactam (formerly AAI101) and tazobactam are penicillanic acid sulfone (PAS) β-lactamase inhibitors that differ by an...
8.
Brem J, Panduwawala T, Ulf Hansen J, Hewitt J, Liepins E, Donets P, et al.
Nat Chem
. 2021 Dec;
14(1):15-24.
PMID: 34903857
Carbapenems are vital antibiotics, but their efficacy is increasingly compromised by metallo-β-lactamases (MBLs). Here we report the discovery and optimization of potent broad-spectrum MBL inhibitors. A high-throughput screen for NDM-1...
9.
Twidale R, Hinchliffe P, Spencer J, Mulholland A
J Chem Inf Model
. 2021 Oct;
61(12):5988-5999.
PMID: 34637298
Widespread bacterial resistance to carbapenem antibiotics is an increasing global health concern. Resistance has emerged due to carbapenem-hydrolyzing enzymes, including metallo-β-lactamases (MβLs), but despite their prevalence and clinical importance, MβL...
10.
Gervasoni S, Spencer J, Hinchliffe P, Pedretti A, Vairoletti F, Mahler G, et al.
Proteins
. 2021 Aug;
90(2):372-384.
PMID: 34455628
Antibiotic resistance is a major threat to global public health. β-lactamases, which catalyze breakdown of β-lactam antibiotics, are a principal cause. Metallo β-lactamases (MBLs) represent a particular challenge because they...