Folding domains within the ricin toxin A subunit as targets of protective antibodies
about
Monoclonal Antibody Combinations that Present Synergistic Neutralizing Activity: A Platform for Next-Generation Anti-Toxin DrugsSub-domains of ricin's B subunit as targets of toxin neutralizing and non-neutralizing monoclonal antibodiesCrystal Structures of Ricin Toxin's Enzymatic Subunit (RTA) in Complex with Neutralizing and Non-Neutralizing Single-Chain AntibodiesStructure of RiVax: a recombinant ricin vaccineNovel Ricin Subunit Antigens With Enhanced Capacity to Elicit Toxin-Neutralizing Antibody Responses in Mice.Chimeric plantibody passively protects mice against aerosolized ricin challenge.Differential neutralizing activities of a single domain camelid antibody (VHH) specific for ricin toxin's binding subunit (RTB).Localization of non-linear neutralizing B cell epitopes on ricin toxin's enzymatic subunit (RTA)Functional divergence between the two P1-P2 stalk dimers on the ribosome in their interaction with ricin A chainNeutralising antibodies against ricin toxin.Resolution of two overlapping neutralizing B cell epitopes within a solvent exposed, immunodominant α-helix in ricin toxin's enzymatic subunitHumanization and characterization of an anti-ricin neutralization monoclonal antibodyMechanistic insights into the neutralization of cytotoxic abrin by the monoclonal antibody D6F10.Thermostable ricin vaccine protects rhesus macaques against aerosolized ricin: Epitope-specific neutralizing antibodies correlate with protection.Characterization and epitope mapping of the polyclonal antibody repertoire elicited by ricin holotoxin-based vaccinationProtective immunity to ricin toxin conferred by antibodies against the toxin's binding subunit (RTB).Passive and active vaccination strategies to prevent ricin poisoning.Immunity to ricin: fundamental insights into toxin-antibody interactions.Plant-based expression of a partially humanized neutralizing monoclonal IgG directed against an immunodominant epitope on the ricin toxin A subunit.Strong protection against ricin challenge induced by a novel modified ricin A-chain protein in mouse model.Isolation of Anti-Ricin Protective Antibodies Exhibiting High Affinity from Immunized Non-Human Primates.Monoclonal antibodies and toxins--a perspective on function and isotype.Neutralizing Monoclonal Antibodies against Disparate Epitopes on Ricin Toxin's Enzymatic Subunit Interfere with Intracellular Toxin Transport.Comparative efficacy of two leading candidate ricin toxin a subunit vaccines in mice.LT-IIb(T13I), a non-toxic type II heat-labile enterotoxin, augments the capacity of a ricin toxin subunit vaccine to evoke neutralizing antibodies and protective immunityNeutralizing monoclonal antibodies against ricin's enzymatic subunit interfere with protein disulfide isomerase-mediated reduction of ricin holotoxin in vitro.Recent advances in the development of vaccines against ricin.Structural insights into the neutralization mechanism of monoclonal antibody 6C2 against ricin.Neutralizing activity and protective immunity to ricin toxin conferred by B subunit (RTB)-specific Fab fragmentsArginine residues on the opposite side of the active site stimulate the catalysis of ribosome depurination by ricin A chain by interacting with the P-protein stalkHumanized Monoclonal Antibody That Passively Protects Mice against Systemic and Intranasal Ricin Toxin Challenge.Stepwise engineering of heterodimeric single domain camelid VHH antibodies that passively protect mice from ricin toxin.Active immunity induced by passive IgG post-exposure protection against ricin.Ricin uses arginine 235 as an anchor residue to bind to P-proteins of the ribosomal stalk.Antibody-mediated inhibition of ricin toxin retrograde transport.Progress and challenges associated with the development of ricin toxin subunit vaccines.Evaluation of lumazine synthase from Bacillus anthracis as a presentation platform for polyvalent antigen display.Using homology modeling to interrogate binding affinity in neutralization of ricin toxin by a family of single domain antibodies.Structural Analysis of Single Domain Antibodies Bound to a Second Neutralizing Hot Spot on Ricin Toxin's Enzymatic Subunit.Structural analysis of nested neutralizing and non-neutralizing B cell epitopes on ricin toxin's enzymatic subunit.
P2860
Q26863621-C9598697-2BF5-457E-8F62-49349DAADB1DQ27320750-72CEF211-2BD8-46E9-93EA-0CDEFA6E88BEQ27644583-91712ECA-343E-46C3-953B-99FDC4BF5B39Q27673488-B51982AE-7DAB-4828-9E04-66344F079885Q30385759-9772B34E-D22A-403C-BAAF-C4FA35DC5CE6Q33601893-5144455A-6F03-43BD-87A7-EED7F581EF49Q33740485-419820DA-1B96-4756-821B-544ECA7933D6Q33805876-C044FF2A-7FAB-48E5-BDE9-0FF27D53D0E8Q33909090-B9737D88-027E-43E8-9538-596CBFD6A0D2Q33919740-5DF92D5A-B2D1-467E-9CFB-9B7D3901CD64Q34323267-2344197A-DAB1-4205-B430-197F303D9ABFQ34438229-11620DD8-D8BE-41DC-AF9F-CE55E3DEDC27Q34906649-A271EE3F-70DE-41A7-B6B8-FDD67A506396Q35229553-70D8C42C-47AA-4F6B-A94D-531B7DBB76ECQ35246883-15EDF267-6C2E-4872-B470-30B440ABB339Q35317286-D37E005A-1171-4FF9-BA0E-ACE4B6646CC6Q35459324-513C5773-F96B-4BBC-B6B9-32B0380A0F1CQ35612017-7E681F20-8AA0-436B-A647-FFF52F1F3DC7Q35742640-01EAE13E-7EAA-47AC-A365-BF19D7AFB61EQ35887201-E65ED992-9DA3-4343-A2D1-600F7F7F4463Q35947693-0A10B589-4CF9-41BC-827E-80CA5E6ADEDCQ36099489-47F179E2-38EE-48B9-8162-E47C05FDC056Q36656806-033BFAD3-2817-477D-96EB-2F6F23009089Q36911310-075F9AC9-FF0C-43B6-A222-B42D94BA6A5BQ37066634-6F2CE63B-B64E-4DE0-8011-B862B74359A7Q37120906-48212DEA-C060-47F5-A11A-D0D3522441F6Q37130978-7B136552-04A7-4FE4-A19C-A47FDD9DF33DQ37132077-9F78178F-0811-4D45-A4D3-61EF38E57197Q37175688-59BA9A00-DC01-4A88-A5AA-CEEDDE9349A7Q37234010-B4D1FDC1-9D7C-41D7-9DF4-58139A5CA169Q37239558-E106E841-0447-4F88-86DE-B65C26718DB3Q37405037-9D40E44E-4F06-4F32-A480-D5D2CF89BBB4Q37576203-74154C08-E1C7-4D30-A255-80251442CA2FQ37660963-20C4EBD6-9F6A-4643-A8D9-F85F94266A55Q37714072-908EFE4F-0A86-4FA8-ADC4-D042DAE5A02AQ38783059-68597D3A-55BE-4AB3-93FC-516706E1A617Q40122953-C41CB8E5-97DD-4D31-864A-0CE80B917AECQ40130441-9DE6E027-8C74-4DA3-8337-6414A5441D8AQ40428974-20EA6523-8DBD-47ED-B1F8-444C4C813380Q40682149-D01F5B5D-5DC6-421F-9157-198FAA4C9BAC
P2860
Folding domains within the ricin toxin A subunit as targets of protective antibodies
description
2010 nî lūn-bûn
@nan
2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Folding domains within the ricin toxin A subunit as targets of protective antibodies
@ast
Folding domains within the ricin toxin A subunit as targets of protective antibodies
@en
Folding domains within the ricin toxin A subunit as targets of protective antibodies
@nl
type
label
Folding domains within the ricin toxin A subunit as targets of protective antibodies
@ast
Folding domains within the ricin toxin A subunit as targets of protective antibodies
@en
Folding domains within the ricin toxin A subunit as targets of protective antibodies
@nl
prefLabel
Folding domains within the ricin toxin A subunit as targets of protective antibodies
@ast
Folding domains within the ricin toxin A subunit as targets of protective antibodies
@en
Folding domains within the ricin toxin A subunit as targets of protective antibodies
@nl
P2093
P2860
P1433
P1476
Folding domains within the ricin toxin A subunit as targets of protective antibodies
@en
P2093
Elizabeth A McCarthy
Jane A Kasten-Jolly
Joanne M O'Hara
Robert N Brey
P2860
P304
P356
10.1016/J.VACCINE.2010.08.020
P407
P577
2010-08-18T00:00:00Z