Cargando…

Structurally- and dynamically-driven allostery of the chymotrypsin-like proteases of SARS, Dengue and Zika viruses

Coronavirus 3C-like and Flavivirus NS2B-NS3 proteases utilize the chymotrypsin fold to harbor their catalytic machineries but also contain additional domains/co-factors. Over the past decade, we aimed to decipher how the extra domains/co-factors mediate the catalytic machineries of SARS 3C-like, Den...

Descripción completa

Detalles Bibliográficos
Autores principales:	Lim, Liangzhong, Gupta, Garvita, Roy, Amrita, Kang, Jian, Srivastava, Shagun, Shi, Jiahai, Song, Jianxing
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Elsevier Ltd. 2019
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111307/ https://www.ncbi.nlm.nih.gov/pubmed/30217495 http://dx.doi.org/10.1016/j.pbiomolbio.2018.08.009

Ejemplares similares

NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics
por: Gupta, Garvita, et al.
Publicado: (2015)

Solution conformations of Zika NS2B-NS3pro and its inhibition by natural products from edible plants
por: Roy, Amrita, et al.
Publicado: (2017)

Dynamically-Driven Enhancement of the Catalytic Machinery of the SARS 3C-Like Protease by the S284-T285-I286/A Mutations on the Extra Domain
por: Lim, Liangzhong, et al.
Publicado: (2014)

Myricetin Allosterically Inhibits the Dengue NS2B-NS3 Protease by Disrupting the Active and Locking the Inactive Conformations
por: Dang, Mei, et al.
Publicado: (2022)

Curcumin Allosterically Inhibits the Dengue NS2B-NS3 Protease by Disrupting Its Active Conformation
por: Lim, Liangzhong, et al.
Publicado: (2020)

Dynamically-Driven Inactivation of the Catalytic Machinery of the SARS 3C-Like Protease by the N214A Mutation on the Extra Domain
por: Shi, Jiahai, et al.
Publicado: (2011)

Structural, Stability, Dynamic and Binding Properties of the ALS-Causing T46I Mutant of the hVAPB MSP Domain as Revealed by NMR and MD Simulations
por: Lua, Shixiong, et al.
Publicado: (2011)

Trypsin- and Chymotrypsin-Like Serine Proteases in Schistosoma mansoni – ‘The Undiscovered Country’
por: Horn, Martin, et al.
Publicado: (2014)

Biflavonoid as potential 3-chymotrypsin-like protease (3CLpro) inhibitor of SARS-Coronavirus
por: Hartini, Yustina, et al.
Publicado: (2021)

Loss of chymotrypsin-like protease (CTRL) alters intrapancreatic protease activation but not pancreatitis severity in mice
por: Mosztbacher, Dóra, et al.
Publicado: (2020)

Pharmacoinformatic study of inhibitory potentials of selected flavonoids against papain-like protease and 3-chymotrypsin-like protease of SARS-CoV-2
por: Tijjani, Habibu, et al.
Publicado: (2022)

Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes
por: Qin, Haina, et al.
Publicado: (2014)

Ginkgolic acid and anacardic acid are reversible inhibitors of SARS-CoV-2 3-chymotrypsin-like protease
por: Li, Dongsheng, et al.
Publicado: (2022)

Treponema denticola chymotrypsin-like protease as associated with HPV-negative oropharyngeal squamous cell carcinoma
por: Kylmä, Anna Kaisa, et al.
Publicado: (2018)

Biochemical and biophysical characterization of the main protease, 3-chymotrypsin-like protease (3CLpro) from the novel coronavirus SARS-CoV 2
por: Ferreira, Juliana C., et al.
Publicado: (2020)

Identification of 3-chymotrypsin like protease (3CLPro) inhibitors as potential anti-SARS-CoV-2 agents
por: Mody, Vicky, et al.
Publicado: (2021)

Considerations for the discovery and development of 3-chymotrypsin-like cysteine protease inhibitors targeting SARS-CoV-2 infection
por: Vandyck, Koen, et al.
Publicado: (2021)

Structural comparison strengthens the higher-order classification of proteases related to chymotrypsin
por: Mönttinen, Heli A. M., et al.
Publicado: (2019)

AN ENZYME IN MAST CELLS WITH PROPERTIES LIKE CHYMOTRYPSIN
por: Benditt, Earl P., et al.
Publicado: (1959)

Dissection Study on the Severe Acute Respiratory Syndrome 3C-like Protease Reveals the Critical Role of the Extra Domain in Dimerization of the Enzyme: DEFINING THE EXTRA DOMAIN AS A NEW TARGET FOR DESIGN OF HIGHLY SPECIFIC PROTEASE INHIBITORS
por: Shi, Jiahai, et al.
Publicado: (2004)

Cloning a Chymotrypsin-Like 1 (CTRL-1) Protease cDNA from the Jellyfish Nemopilema nomurai
por: Heo, Yunwi, et al.
Publicado: (2016)

Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis
por: Clark, Elizabeth A., et al.
Publicado: (2011)

Identification of novel drug scaffolds for inhibition of SARS-CoV 3-Chymotrypsin-like protease using virtual and high-throughput screenings
por: Lee, Hyun, et al.
Publicado: (2014)

Exploration of chalcones as 3-chymotrypsin-like protease (3CL(pro)) inhibitors of SARS-CoV-2 using computational approaches
por: Lam, Thua-Phong, et al.
Publicado: (2022)

Computational analysis of dynamic allostery and control in the SARS-CoV-2 main protease
por: Dubanevics, Igors, et al.
Publicado: (2021)

FORMATION OF NEW CRYSTALLINE ENZYMES FROM CHYMOTRYPSIN : ISOLATION OF BETA AND GAMMA CHYMOTRYPSIN
por: Kunitz, M.
Publicado: (1938)

Assessment of activity of chalcone compounds as inhibitors of 3-chymotrypsin like protease (3CL(Pro)) of SARS-CoV-2: in silico study
por: Mathpal, Shalini, et al.
Publicado: (2022)

In silico analysis and identification of antiviral coumarin derivatives against 3-chymotrypsin-like main protease of the novel coronavirus SARS-CoV-2
por: Abdizadeh, Rahman, et al.
Publicado: (2021)

Catalytic Dyad Residues His41 and Cys145 Impact the Catalytic Activity and Overall Conformational Fold of the Main SARS-CoV-2 Protease 3-Chymotrypsin-Like Protease
por: Ferreira, Juliana C., et al.
Publicado: (2021)

Structure-based virtual screening suggests inhibitors of 3-Chymotrypsin-Like Protease of SARS-CoV-2 from Vernonia amygdalina and Occinum gratissimum
por: Gyebi, Gideon A., et al.
Publicado: (2021)

Structure and Cleavage Specificity of the Chymotrypsin-Like Serine Protease (3CLSP/nsp4) of Porcine Reproductive and Respiratory Syndrome Virus (PRRSV)
por: Tian, Xinsheng, et al.
Publicado: (2009)

The Nuclear Pore Complex: A Target for NS3 Protease of Dengue and Zika Viruses
por: De Jesús-González, Luis Adrián, et al.
Publicado: (2020)

In silico testing of flavonoids as potential inhibitors of protease and helicase domains of dengue and Zika viruses
por: Cruz-Arreola, Omar, et al.
Publicado: (2022)

Intracellular localization of Treponema denticola chymotrypsin-like proteinase in chronic periodontitis
por: Marttila, Emilia, et al.
Publicado: (2014)

Impact of bound ssRNA length on allostery in the Dengue Virus NS3 helicase
por: Amrein, Fernando, et al.
Publicado: (2023)

ALG-097111, a potent and selective SARS-CoV-2 3-chymotrypsin-like cysteine protease inhibitor exhibits in vivo efficacy in a Syrian Hamster model
por: Vandyck, Koen, et al.
Publicado: (2021)

ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43
por: Lim, Liangzhong, et al.
Publicado: (2016)

A new chymotrypsin-like serine protease involved in dietary protein digestion in a primitive animal, Scorpio maurus: purification and biochemical characterization
por: Louati, Hanen, et al.
Publicado: (2011)

Response of Midgut Trypsin- and Chymotrypsin-Like Proteases of Helicoverpa armigera Larvae Upon Feeding With Peanut BBI: Biochemical and Biophysical Characterization of PnBBI
por: Lokya, Vadthya, et al.
Publicado: (2020)

Molecular Docking Analysis of Anti-Severe Acute Respiratory Syndrome-Coronavirus 2 Ligands against Spike Glycoprotein and the 3-Chymotrypsin-Like Protease
por: Janabi, Ali Hassan Daghir
Publicado: (2021)

Cannot write session to /tmp/vufind_sessions/sess_015n39eldg40oagru0uiljchte