Protease enzyme virus

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Elongated and shortened peptidomimetic inhibitors of the proprotein convertase furin. Van Lam van T. Ivanova, K. Hardes, M. Heindl, R. Morty, E. Lindberg, M. Than, S. Dahms, T. Steinmetzer, Design, synthesis, and characterization of macrocyclic inhibitors of the proprotein convertase Furin, CheMedChem 14 —, doi: Lucas J.

The androgen-regulated protease TMPRSS2 activates a proteolytic cascade involving components of the tumor microenvironment and promotes prostate cancer metastasis. Cancer Dis. Mikkonen L. Androgen receptor and androgen- dependent gene expression in lung. Shen L. Madjid M. Potential effects of coronaviruses on the cardiovascular system: a review. JAMA Cardiol. Strope J. Pan X. Identification of a potential mechanism of acute kidney injury during the COVID outbreak: a study based on single-cell transcriptome analysis.

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Membrane-anchored serine proteases in health and disease. Mushtaq H. Herter S. Hepatocyte growth factor is a preferred in vitro substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancers. Structural comparison strengthens the higher order classification of proteases related to chymotrypsin. Fastrez J. Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by chymotrypsin. Bottcher E. Bottcher-Friebertshauser E.

Chaipan, D. Kobasa, S. Bertram, I. Glowacka, I. Steffen, T. Tsegaye, M. Takeda, T. Bugge, S. Kim, Y. Park, A. Marzi, S. Matsuyama S. Kawase M. Simultaneous treatment of human bronchial epithelial cells with serine and cysteine protease inhibitors prevents severe acute respiratory syndrome coronavirus entry. Hatesuer B. PLoS Pathogen. Tarnow C. Sakai K. Iwata-Yoshikawa N. TMPRSS2 contributes to virus spread and immunopathology in the airways of murine models after coronavirus infection.

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The interaction of human tryptase- beta with small molecule inhibitors provides new insights into the unusual functional instability and quaternary structure of the protease. Burkard, M. Verheije, O. Wicht, S. Haagmans, L. Pelkmans, P. Rottier, B. Bosch, C. PLoS Pathol.

Nishizawa M. Zhang C. Huang B. Roebroek A. Failure of ventral closure and axial rotation in embryos lacking the proprotein convertase Furin. Neumann G. Reverse genetics demonstrates that proteolytic processing of the Ebola virus glycoprotein is not essential for replication in cell culture.

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A review on the phytochemistry, pharmacology, pharmacokinetics and toxicology of geniposide, a natural product. Yamaya M. Protease inhibitors: candidate drugs to inhibit severe acute respiratory syndrome Coronavirus 2 replication.

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Yang H. The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor. Zhang L. Lee C. Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and peptidomimetic compounds.

The SARS-coronavirus papain-like protease: structure, function and inhibition by designed antiviral compounds. Ziebuhr J. Virus-encoded proteinases and proteolytic processing in the Nidovirales.

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Hegyi A. Mutational analysis of the active centre of coronavirus 3C-like proteases. Komatsu T. Liu W. Rut W. Hayashi H. Dimerization of HIV-1 protease occurs through two steps relating to the mechanism of protease dimerization inhibition by darunavir. Jin Z. Dai W. Tsai K. Hagar M. Liang J. Islam R. Fischer A. Potential inhibitors for novel Coronavirus protease identified by virtual screening of million compounds. Gupta S. Identification of potential natural inhibitors of SARS-CoV2 main protease by molecular docking and simulation studies.

Gurung A. Life Sci. Kumar A. Identification of phytochemical inhibitors against main protease of COVID using molecular modeling approaches. Kumar V. Bhardwaj V. Umesh D. Enmozhi S. Serseg, K. Benarous, M. Aided Drug Des. Khan M. Gentile D. Putative inhibitors of SARS-CoV-2 main protease from a library of marine natural products: a virtual screening and molecular modeling study.

Gimeno A. A Shamsi, T. Mohammad, S. Anwar, M. Al Ajmi, A. Hussain, M. Rehman, A. Islam, M. Calligari P. Al-Khafaji K. Das S. An investigation into the identification of potential inhibitors of SARS-CoV-2 main protease using molecular docking study. Shahab S. Mahanta S. Potential anti-viral activity of approved repurposed drug against main protease of SARS-CoV an in silico based approach.

Mittal L. Identification of potential molecules against COVID main protease through structure-guided virtual screening approach. Tsuji M. Elmezayen A. Huynh T. In silico exploration of the molecular mechanism of clinically oriented drugs for possibly inhibiting SARS-CoV-2's main protease.

Acta Pharmacol. Liu J. Cell Discov. Cell Res. Hung H. Yang Q. Design and synthesis of cinanserin analogs as severe acute respiratory syndrome coronavirus 3CL protease inhibitors. Tokyo ; 56 — Chen L. Cinanserin is an inhibitor of the 3C-like proteinase of severe acute respiratory syndrome coronavirus and strongly reduces virus replication in vitro. Choy K. Yao, F. Ye, M Zhang, C. Cui, B. Huang, P. Niu, X. Liu, L. Zhao, E. Dong, C. Song, S. Zhan, R. Lu, H. Li, W. Freitas B.

ACS Infect. X-ray structural and biological evaluation of a series of potent and highly selective inhibitors of human coronavirus papain-like proteases. Guzik T. COVID and the cardiovascular system: implications for risk assessment, diagnosis, and treatment options.

Liu X. Potential inhibitors against nCoV coronavirus M protease from clinically approved medicines. Cao B. A trial of Lopinavir-Ritonavir in adults hospitalized with severe Covid Sankar J. COVID in children: clinical approach and management. Indian J. Vincent M. Chloroquine is a potent inhibitor of SARS coronavirus infection and spread.

Zou L. Hydroxychloroquine and chloroquine: a potential and controversial treatment for COVI Arch Pharm Res. The role of these enzymes is to catalyze the cleavage of specific peptide bonds in viral polyprotein precursors or in cellular proteins. In most cases these proteolytic events are essential for the completion of the viral infectious cycle. Viral proteases may use different catalytic mechanisms involving either serine, cysteine or aspartic acid residues to attack the scissile peptide bond.

This bond is often located within conserved sequence motifs extending for up to ten residues. Selective recognition of these sequence patterns by a complementary substrate binding site of the enzyme ensures a high degree of specific recognition and cleavage Fig. Open image in new window. SARS main protease top and papain-like protease bottom , with inhibitor in turquoise.

The two proteases from SARS are shown here. The papain-like protease PDB entry 4ow0 has single subunit and also uses a cysteine in the reaction. It makes three specific cuts in the SARS polyproteins, and also clips several proteins in the infected cell, including removing ubiquitin from ubiquitinated proteins.

One of the consequences of this deubiquitination is that it interferes with production of interferons in the innate immune system, short-circuiting some of our defenses against the virus. Topics for Further Discussion An unusual octameric form of the main protease may be involved in its maturation. You can see it in PDB entry 3iwm. Try using trypsinogen PDB entry 1tgs , so that the whole enzyme is one chain for the alignment. References Cui, J.

FEBS J. New York Times, July 30, section C, page 2. About Molecule of the Month. Each installment includes an introduction to the structure and function of the molecule, a discussion of the relevance of the molecule to human health and welfare, and suggestions for how visitors might view these structures and access further details.