Investigation of griffithsin's interactions with human cells confirms its outstanding safety and efficacy profile as a microbicide candidate
about
Rapid and scalable plant-based production of a cholera toxin B subunit variant to aid in mass vaccination against cholera outbreaksActivity of and effect of subcutaneous treatment with the broad-spectrum antiviral lectin griffithsin in two laboratory rodent modelsBulk production of the antiviral lectin griffithsinGriffithsin: An Antiviral Lectin with Outstanding Therapeutic PotentialPharmacokinetics of the Antiviral Lectin Griffithsin Administered by Different Routes Indicates Multiple Potential UsesAntiviral lectins from red and blue-green algae show potent in vitro and in vivo activity against hepatitis C virusThe root extract of the medicinal plant Pelargonium sidoides is a potent HIV-1 attachment inhibitorAqueous extracts of the marine brown alga Lobophora variegata inhibit HIV-1 infection at the level of virus entry into cellsAnti-Retroviral Lectins Have Modest Effects on Adherence of Trichomonas vaginalis to Epithelial Cells In Vitro and on Recovery of Tritrichomonas foetus in a Mouse Vaginal ModelDevelopment of an HIV-1 Microbicide Based on Caulobacter crescentus: Blocking Infection by High-Density Display of Virus Entry Inhibitors.Entry Inhibition of Influenza Viruses with High Mannose Binding Lectin ESA-2 from the Red Alga Eucheuma serra through the Recognition of Viral HemagglutininBroad anti-HIV activity of the Oscillatoria agardhii agglutinin homologue lectin family.Algal lectins as potential HIV microbicide candidatesRole of the carbohydrate-binding sites of griffithsin in the prevention of DC-SIGN-mediated capture and transmission of HIV-1.Griffithsin has antiviral activity against hepatitis C virusGriffithsin tandemers: flexible and potent lectin inhibitors of the human immunodeficiency virusImproving the large scale purification of the HIV microbicide, griffithsin.The lectins griffithsin, cyanovirin-N and scytovirin inhibit HIV-1 binding to the DC-SIGN receptor and transfer to CD4(+) cells.Engineering soya bean seeds as a scalable platform to produce cyanovirin-N, a non-ARV microbicide against HIVGriffithsin and Carrageenan Combination To Target Herpes Simplex Virus 2 and Human Papillomavirus.The role of individual carbohydrate-binding sites in the function of the potent anti-HIV lectin griffithsin.Combinations of griffithsin with other carbohydrate-binding agents demonstrate superior activity against HIV Type 1, HIV Type 2, and selected carbohydrate-binding agent-resistant HIV Type 1 strainsM48U1 CD4 mimetic has a sustained inhibitory effect on cell-associated HIV-1 by attenuating virion infectivity through gp120 shedding.Efficient single tobamoviral vector-based bioproduction of broadly neutralizing anti-HIV-1 monoclonal antibody VRC01 in Nicotiana benthamiana plants and utility of VRC01 in combination microbicidesGriffithsin protects mice from genital herpes by preventing cell-to-cell spreadRice endosperm is cost-effective for the production of recombinant griffithsin with potent activity against HIV.The griffithsin dimer is required for high-potency inhibition of HIV-1: evidence for manipulation of the structure of gp120 as part of the griffithsin dimer mechanism.Non-Antiretroviral Microbicides for HIV Prevention.Griffithsin-Modified Electrospun Fibers as a Delivery Scaffold To Prevent HIV Infection.The lectin-like protein 1 in Lactobacillus rhamnosus GR-1 mediates tissue-specific adherence to vaginal epithelium and inhibits urogenital pathogens.Studies in a Murine Model Confirm the Safety of Griffithsin and Advocate Its Further Development as a Microbicide Targeting HIV-1 and Other Enveloped Viruses.Inhibition of hepatitis C virus by the cyanobacterial protein Microcystis viridis lectin: mechanistic differences between the high-mannose specific lectins MVL, CV-N, and GNA.Antibody-based concepts for multipurpose prevention technologies.Microbial lectins and their prospective mitogenic potential.Effects of N-glycan precursor length diversity on quality control of protein folding and on protein glycosylation.HIV-1 and its resistance to peptidic carbohydrate-binding agents (CBAs): an overview.Lectins with anti-HIV activity: a review.Marine lectins and their medicinal applications.Antiviral lectins: Selective inhibitors of viral entry.Multipurpose tenofovir disoproxil fumarate electrospun fibers for the prevention of HIV-1 and HSV-2 infections in vitro.
P2860
Q21090119-DEBC05D0-006D-4D24-91B0-5058E3BACF3EQ24610025-3B7F98BC-252F-4C60-A773-5857AA0423BAQ26801491-61347939-E231-4849-B3E2-0D1FC63074D2Q27928014-D2C8F89D-6632-4115-9F35-FB4229B1BDB7Q28354743-36DA47A1-E3DC-4BFA-BB36-7DEAAB695BB0Q28488338-0A0DD776-4585-48B4-B1E1-4C543BF97640Q28539308-1D7314FE-D407-4824-B6E3-72683F3E6518Q28542473-BF8AE38C-A7B2-4834-8A8F-7207EF89519EQ28547132-C414C51C-F778-4CD3-AD68-8975DB7B6F02Q30351993-B9A93C8C-0A1D-403E-9D39-35382F924879Q30375215-10075974-B9A8-49EF-AA8E-44392CE94183Q34181482-B017AC1A-123A-4F8B-AF6D-BB6ED4EDA75EQ34291727-2C874B39-B0B2-4D97-941C-843677E5D248Q34760408-9B6595F7-92D9-4A40-8E8B-B4D31B746409Q35363633-765748A9-6592-4578-950D-50C0B2A6E0AEQ35568986-49A7D0F5-B924-4BCD-9915-919B15A3866CQ35607915-57EDB62C-2AEA-416B-BA56-B052135FD162Q35743210-7C14CEE5-40B9-4F09-9EF0-FDD4D5DEC997Q35929104-46A852E2-41DB-4FCB-8385-45516A4FE659Q36290533-811B7BFA-7F0A-4CC6-98BE-439681EB327FQ36327928-EE35C3C8-7FA3-492A-9529-6CDE9C11A8C0Q36358780-3D39BA7D-0BC4-42F6-A84D-7BDA5D064302Q36608485-47F183B1-A5E2-46D3-A2F8-2542906360B3Q36785795-E63586B9-E0E4-488A-B7FE-947E3A6002E4Q36827173-F0CB31DB-045F-440A-8109-B78CAE31E7EBQ36896705-03858CE0-0283-44D2-9F13-4BC2914B1A37Q37036454-AE29D005-F194-47A6-921C-A1B13381CA3FQ37317845-788E39B7-1301-4E58-8965-BF7A4A486C3EQ37358616-C05C0F6D-8267-4FEF-970C-106B6CC192EAQ37424913-4A028F6B-90E0-43D2-88DB-C76CBDA55CEDQ37450191-5804EB33-636B-4762-BE4E-E8D6AF8900FEQ37533386-E77C40DB-E236-41E1-B071-A4C281BF0C51Q37601003-B59D9462-D3C1-424C-ADAD-24C73C7F8E1DQ38065207-21B64F8B-5B72-42AC-9866-7E1E061A1C29Q38283133-A78B90CE-19A6-4344-974C-63754EFFB0E1Q38291704-BCC30EA7-E8F9-4AB4-8F25-57D6DFAD7094Q38311332-A4900D37-EC3A-48A5-8546-B281C0E17DC2Q38385723-F6E47DF1-1E45-43CE-9824-3E7D0591A867Q38891044-562E7CF1-FA62-4B74-A10D-1221C4426F8FQ40086722-38D9A772-15BC-42C6-B526-ED0B16D12191
P2860
Investigation of griffithsin's interactions with human cells confirms its outstanding safety and efficacy profile as a microbicide candidate
description
2011 nî lūn-bûn
@nan
2011 թուականին հրատարակուած գիտական յօդուած
@hyw
2011 թվականին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Investigation of griffithsin's ...... ile as a microbicide candidate
@ast
Investigation of griffithsin's ...... ile as a microbicide candidate
@en
Investigation of griffithsin's ...... ile as a microbicide candidate
@nl
type
label
Investigation of griffithsin's ...... ile as a microbicide candidate
@ast
Investigation of griffithsin's ...... ile as a microbicide candidate
@en
Investigation of griffithsin's ...... ile as a microbicide candidate
@nl
prefLabel
Investigation of griffithsin's ...... ile as a microbicide candidate
@ast
Investigation of griffithsin's ...... ile as a microbicide candidate
@en
Investigation of griffithsin's ...... ile as a microbicide candidate
@nl
P2093
P2860
P50
P3181
P1433
P1476
Investigation of griffithsin's ...... ile as a microbicide candidate
@en
P2093
Andrew Johannemann
Barry R O'Keefe
Dana Huskens
Janice M Walker
Joseph Calvin Kouokam
Shonna K Riedell
Wendye Walter
P2860
P304
P3181
P356
10.1371/JOURNAL.PONE.0022635
P407
P577
2011-01-01T00:00:00Z