Domain-swapped structure of the potent antiviral protein griffithsin and its mode of carbohydrate binding.
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Activity of and effect of subcutaneous treatment with the broad-spectrum antiviral lectin griffithsin in two laboratory rodent modelsA lectin isolated from bananas is a potent inhibitor of HIV replicationBroad-spectrum in vitro activity and in vivo efficacy of the antiviral protein griffithsin against emerging viruses of the family CoronaviridaeScaleable manufacture of HIV-1 entry inhibitor griffithsin and validation of its safety and efficacy as a topical microbicide componentPlant-produced candidate countermeasures against emerging and reemerging infections and bioterror agentsProteins and Carbohydrates from Red Seaweeds: Evidence for Beneficial Effects on Gut Function and MicrobiotaBulk production of the antiviral lectin griffithsinCrystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamineConformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 Å resolutionMonomerization of Viral Entry Inhibitor Griffithsin Elucidates the Relationship between Multivalent Binding to Carbohydrates and anti-HIV ActivityNovel Fold and Carbohydrate Specificity of the Potent Anti-HIV Cyanobacterial Lectin from Oscillatoria agardhiiIpomoelin, a Jacalin-Related Lectin with a Compact Tetrameric Association and Versatile Carbohydrate Binding Properties Regulated by Its N TerminusStructural Insights into the Anti-HIV Activity of the Oscillatoria agardhii Agglutinin Homolog Lectin FamilyStructural Basis of the Anti-HIV Activity of the Cyanobacterial Oscillatoria Agardhii AgglutininVibrio cholerae Cytolysin Recognizes the Heptasaccharide Core of Complex N-Glycans with Nanomolar AffinityStructural Basis for Multiple Sugar Recognition of Jacalin-related Human ZG16p LectinThe characteristic structure of anti-HIV actinohivin in complex with three HMTG D1 chains of HIV-gp120Griffithsin: 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 virusInvestigation of griffithsin's interactions with human cells confirms its outstanding safety and efficacy profile as a microbicide candidateGrifonin-1: a small HIV-1 entry inhibitor derived from the algal lectin, GriffithsinAlgal lectins as potential HIV microbicide candidatesPotent strategy to inhibit HIV-1 by binding both gp120 and gp41.Role of the carbohydrate-binding sites of griffithsin in the prevention of DC-SIGN-mediated capture and transmission of HIV-1.Inhibition of severe acute respiratory syndrome coronavirus replication in a lethal SARS-CoV BALB/c mouse model by stinging nettle lectin, Urtica dioica agglutinin.Binding of the mannose-specific lectin, griffithsin, to HIV-1 gp120 exposes the CD4-binding siteGriffithsin has antiviral activity against hepatitis C virusGriffithsin tandemers: flexible and potent lectin inhibitors of the human immunodeficiency virusPurification, characterization, and biological activities of broccolini lectin.The lectins griffithsin, cyanovirin-N and scytovirin inhibit HIV-1 binding to the DC-SIGN receptor and transfer to CD4(+) cells.Mannose-rich glycosylation patterns on HIV-1 subtype C gp120 and sensitivity to the lectins, Griffithsin, Cyanovirin-N and Scytovirin.The role of individual carbohydrate-binding sites in the function of the potent anti-HIV lectin griffithsin.Rice 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.A Designed "Nested" Dimer of Cyanovirin-N Increases Antiviral Activity.Protein acrobatics in pairs--dimerization via domain swapping.Mechanisms of HIV-1 subtype C resistance to GRFT, CV-N and SVN.Griffithsin-Modified Electrospun Fibers as a Delivery Scaffold To Prevent HIV Infection.Differential inhibitory effects of cyanovirin-N, griffithsin, and scytovirin on entry mediated by envelopes of gammaretroviruses and deltaretroviruses.
P2860
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P2860
Domain-swapped structure of the potent antiviral protein griffithsin and its mode of carbohydrate binding.
description
2006 nî lūn-bûn
@nan
2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Domain-swapped structure of th ...... mode of carbohydrate binding.
@ast
Domain-swapped structure of th ...... mode of carbohydrate binding.
@en
Domain-swapped structure of th ...... mode of carbohydrate binding.
@nl
type
label
Domain-swapped structure of th ...... mode of carbohydrate binding.
@ast
Domain-swapped structure of th ...... mode of carbohydrate binding.
@en
Domain-swapped structure of th ...... mode of carbohydrate binding.
@nl
prefLabel
Domain-swapped structure of th ...... mode of carbohydrate binding.
@ast
Domain-swapped structure of th ...... mode of carbohydrate binding.
@en
Domain-swapped structure of th ...... mode of carbohydrate binding.
@nl
P2093
P1433
P1476
Domain-swapped structure of th ...... s mode of carbohydrate binding
@en
P2093
Alexander Wlodawer
Barbara Giomarelli
Barry R O'Keefe
Charles Zhu
Fakhrieh Vojdani
James B McMahon
Natasza E Ziółkowska
Toshiyuki Mori
P304
P356
10.1016/J.STR.2006.05.017
P577
2006-07-01T00:00:00Z