Results 131 to 140 of about 81,932 (256)

Precision Chemistry for Protein Lysine Modification

Chemistry – A European Journal, EarlyView.
Selective modification of lysine residues is challenging due to their similar intrinsic reactivity. Inspired by enzymatic recognition, ligand‐guided electrophiles enable site‐selective labeling and functionalization, while ligand‐guided catalyses achieve regioselective installation of bio‐relevant post‐translational modifications.
Mayu Onoda, Motomu Kanai
wiley   +1 more source

De Novo Design of Multivalent α/β‐Peptides Mimicking Transcription Factors Targeting the CBP KIX Domain

Chemistry – A European Journal, EarlyView.
A modular, de novo α/β‐peptide design strategy allows fine‐tuning of ligand properties, resulting in multivalent ligands that simultaneously target separate binding sites on the protein surface. ABSTRACT Protein‐protein interactions that regulate gene expression in the nucleus are increasingly recognized as potential therapeutic targets but present ...
Márk V. Tresztián, Vencel L. Petrovicz, Edit Wéber, Tamás A. Martinek, Zsófia Hegedüs   +4 more
wiley   +1 more source

A single allosteric site merges activation, modulation and inhibition in TRPM5. [PDF]

Nat Chem Biol
Ruan Z, Lee J, Li Y, Orozco IJ, Du J, Lü W.   +5 more
europepmc   +1 more source

Allosteric Site of ACE-2 as a Drug Target for COVID-19. [PDF]

ACS Pharmacol Transl Sci, 2022
Dutta K.
europepmc   +1 more source

Substrate‐Selective Inhibition of the SARS‐CoV‐2 Papain‐Like Protease: Inhibition of Hydrolysis of Human Over Viral Substrates

Chemistry – A European Journal, EarlyView.
The SARS‐CoV‐2 papain‐like protease (PLpro) is a medicinal chemistry target. Here we report mass spectrometry assays employing oligopeptide substrates based on the sequences of the viral polyproteins 1a/1ab and on an ISG15‐modified human protein, which enabled the identification of substrate‐selective PLpro inhibitors.
Sakshi Sharma, Peter A. C. Wing, Wojtek Trede, Shyam Basak, Simeon D. Draganov, Taylah Andrews‐Clark, Eidarus Salah, Petra Lukacik, Claire Strain‐Damerell, Adán Pinto‐Fernández, Martin A. Walsh, Fernanda Duarte, Christopher J. Schofield, Lennart Brewitz   +13 more
wiley   +1 more source

Galectin-3 Binds to the Allosteric Site and Activates Integrins αvβ3, αIIbβ3, and α5β1, and Lactose Inhibits This Activation. [PDF]

Biomolecules
Takada YK, Wan YY, Takada Y.
europepmc   +1 more source

Illumination of serotonin transporter mechanism and role of the allosteric site. [PDF]

Sci Adv, 2021
Yang D, Gouaux E.
europepmc   +1 more source

Characterisation of an allosteric site in PLCγ enzymes and implications for development of their specific inhibitors. [PDF]

Biochem J
Bunney TD, Nyvall HG, Macrae C, Lalović D, Gregory A, Le Huray KIP, Harvey N, Pinotsis N, Kalli AC, Waudby CA, Burke JE, Katan M.   +11 more
europepmc   +1 more source

CD40L Activates Platelet Integrin αIIbβ3 by Binding to the Allosteric Site (Site 2) in a KGD-Independent Manner and HIGM1 Mutations Are Clustered in the Integrin-Binding Sites of CD40L. [PDF]

Cells, 2023
Takada YK, Shimoda M, Takada Y.
europepmc   +1 more source

A Systematic Review on Disease‐Modifying Therapies in Parkinsonian Disorders

Clinical Pharmacology &Therapeutics, EarlyView.
Parkinsonian disorders, including Parkinson's disease, Lewy body dementia, multiple system atrophy, and progressive supranuclear palsy, are progressive neurodegenerative conditions with no treatment options to slow disease progression. This systematic review provides an overview of evidence of disease‐modifying therapies that have been evaluated in ...
Pepijn P.N.M. Eijsvogel, Lars M.G. Smits, Philip H.C. Kremer, Geert Jan Groeneveld   +3 more
wiley   +1 more source