Feglymycin, a unique natural bacterial antibiotic peptide, inhibits HIV entry by targeting the viral envelope protein gp120. (Q39283283)

10 September 2017

Feglymycin, a unique natural bacterial antibiotic peptide, inhibits HIV entry by targeting the viral envelope protein gp120. (English)

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10 September 2017

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Roderich D Süssmuth

7

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Dominique Schols

object named as

Dominique Schols

8

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author name string

Geoffrey Férir

1

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10 September 2017

Anne Hänchen

2

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10 September 2017

Katrien O François

3

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10 September 2017

Bart Hoorelbeke

4

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10 September 2017

Dana Huskens

5

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10 September 2017

Frank Dettner

6

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10 September 2017

language of work or name

English

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publication date

7 September 2012

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10 September 2017

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10 September 2017

433

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10 September 2017

2

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10 September 2017

308-319

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Entry of hepatitis C virus and human immunodeficiency virus is selectively inhibited by carbohydrate-binding agents but not by polyanions

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Large-scale manufacture of peptide therapeutics by chemical synthesis

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The antiviral antibiotic feglymycin: first direct-methods solution of a 1000+ equal-atom structure

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High-resolution solution structure of siamycin II: novel amphipathic character of a 21-residue peptide that inhibits HIV fusion

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Siamycins I and II, new anti-HIV-1 peptides: II. Sequence analysis and structure determination of siamycin I.

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1 reference

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Total synthesis of the antiviral peptide antibiotic feglymycin

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Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus

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Resistance of human immunodeficiency virus type 1 to a third-generation fusion inhibitor requires multiple mutations in gp41 and is accompanied by a dramatic loss of gp41 function

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Setting the stage: host invasion by HIV.

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Microvirin, a novel alpha(1,2)-mannose-specific lectin isolated from Microcystis aeruginosa, has anti-HIV-1 activity comparable with that of cyanovirin-N but a much higher safety profile

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Enfuvirtide: from basic investigations to current clinical use.

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Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody

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Microbicides and other topical strategies to prevent vaginal transmission of HIV.

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A small molecule HIV-1 inhibitor that targets the HIV-1 envelope and inhibits CD4 receptor binding

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Characterization of siamycin I, a human immunodeficiency virus fusion inhibitor

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Chloropeptins, new anti-HIV antibiotics inhibiting gp120-CD4 binding from Streptomyces sp. II. Structure elucidation of chloropeptin I

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Enfuvirtide: the first therapy to inhibit the entry of HIV-1 into host CD4 lymphocytes

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Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide

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Potent and selective inhibition of HIV-1 replication in vitro by a novel series of TIBO derivatives

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Candidate sulfonated and sulfated topical microbicides: comparison of anti-human immunodeficiency virus activities and mechanisms of action.

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Cell-to-cell spread of HIV permits ongoing replication despite antiretroviral therapy

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Feglymycin, a novel inhibitor of the replication of the human immunodeficiency virus. Fermentation, isolation and structure elucidation

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Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development

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inferred from DOI database lookup

7 January 2021

based on heuristic

The molecular target of bicyclams, potent inhibitors of human immunodeficiency virus replication

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/J.VIROL.2012.08.007

1 reference

release_wgqstbxxmzd23ikkn55qoygdpe

10 September 2017

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1 reference