(Q30935094)

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Acyl sulfonamides as potent protease inhibitors of the hepatitis C virus full-Length NS3 (protease-helicase/NTPase): a comparative study of different C-terminals

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Europe PubMed Central

PubMed publication ID

27 June 2017

Acyl sulfonamides as potent protease inhibitors of the hepatitis C virus full-Length NS3 (protease-helicase/NTPase): a comparative study of different C-terminals (English)

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

Hepatitis C virus

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Anders Hallberg

9

object named as

Anders Hallberg

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

author name string

Anja Johansson

1

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Europe PubMed Central

PubMed publication ID

27 June 2017

Anton Poliakov

2

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

Eva Akerblom

3

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

Karin Wiklund

4

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

Gunnar Lindeberg

5

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

Susanne Winiwarter

6

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

U Helena Danielson

7

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

Bertil Samuelsson

8

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Europe PubMed Central

PubMed publication ID

27 June 2017

language of work or name

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publication date

1 June 2003

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Europe PubMed Central

PubMed publication ID

27 June 2017

Bioorganic & Medicinal Chemistry

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Europe PubMed Central

PubMed publication ID

27 June 2017

11

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

12

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

2551-2568

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Europe PubMed Central

PubMed publication ID

27 June 2017

Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome

1 reference

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Global surveillance and control of hepatitis C. Report of a WHO Consultation organized in collaboration with the Viral Hepatitis Prevention Board, Antwerp, Belgium

1 reference

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The scientific challenge of hepatitis C.

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Hepatitis C therapeutics: current status and emerging strategies

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Emerging therapies for hepatitis C virus infection

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The NS3/4A proteinase of the hepatitis C virus: unravelling structure and function of an unusual enzyme and a prime target for antiviral therapy

1 reference

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Recent advances in the molecular biology of hepatitis C virus

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Hepatitis C: molecular virology and antiviral targets

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Inhibiting viral proteases: challenges and opportunities

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Hepatitis C virus protease inhibitors: current progress and future challenges

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Solution and solid-phase synthesis of potent inhibitors of hepatitis C virus NS3 proteinase

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1-Aminocyclopropaneboronic acid: synthesis and incorporation into an inhibitor of hepatitis C virus NS3 protease

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P1 Phenethyl peptide boronic acid inhibitors of HCV NS3 protease

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Capped dipeptide alpha-ketoacid inhibitors of the HCV NS3 protease

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Evolution, synthesis and SAR of tripeptide alpha-ketoacid inhibitors of the hepatitis C virus NS3/NS4A serine protease

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Alpha-ketoacids are potent slow binding inhibitors of the hepatitis C virus NS3 protease

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A designed P1 cysteine mimetic for covalent and non-covalent inhibitors of HCV NS3 protease.

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The identification of alpha-ketoamides as potent inhibitors of hepatitis C virus NS3-4A proteinase

1 reference

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Solid phase synthesis of aminoboronic acids: potent inhibitors of the hepatitis C virus NS3 proteinase

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Alpha-ketoamides, alpha-ketoesters and alpha-diketones as HCV NS3 protease inhibitors

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The design and synthesis of potent inhibitors of hepatitis C virus NS3-4A proteinase

1 reference

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Studies on the C-terminal of hexapeptide inhibitors of the hepatitis C virus serine protease.

1 reference

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Solid phase synthesis of peptide aldehyde protease inhibitors. Probing the proteolytic sites of hepatitis C virus polyprotein

1 reference

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7 January 2021

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Azapeptides as inhibitors of the hepatitis C virus NS3 serine protease

1 reference

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7 January 2021

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Peptide-based inhibitors of the hepatitis C virus serine protease

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7 January 2021

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Product inhibition of the hepatitis C virus NS3 protease

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7 January 2021

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Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase

1 reference

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Potent peptide inhibitors of human hepatitis C virus NS3 protease are obtained by optimizing the cleavage products

1 reference

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Highly potent and selective peptide-based inhibitors of the hepatitis C virus serine protease: towards smaller inhibitors.

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Solid-phase synthesis of peptidomimetic inhibitors for the hepatitis C virus NS3 protease

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Optimization of the P'-region of peptide inhibitors of hepatitis C virus NS3/4A protease

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Prime site binding inhibitors of a serine protease: NS3/4A of hepatitis C virus

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Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain

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Tetrapeptides as potent protease inhibitors of Hepatitis C Virus full-length NS3 (protease-helicase/NTPase).

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An improved procedure for N- to C-directed (Inverse) solid-phase peptide synthesis

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Solid Phase Peptide Synthesis. I. The Synthesis of a Tetrapeptide

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Inhibition of human neutrophil elastase with peptidyl electrophilic ketones. 2. Orally active PG-Val-Pro-Val pentafluoroethyl ketones

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Identifiers

10.1016/S0968-0896(03)00179-2

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

27 June 2017

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