about
Human milk sIgA molecules contain various combinations of different antigen-binding sites resulting in a multiple binding specificity of antibodies and enzymatic activities of abzymesBeyond new chemical entities: advancing drug development based on functional versatility of antibodiesSelection of peptides inhibiting a beta-lactamase-like activity.Anti-idiotypic antibodies: a new approach in prion research.Comparison of antibodies hydrolyzing myelin basic protein from the cerebrospinal fluid and serum of patients with multiple sclerosis.Human milk IgGs contain various combinations of different antigen-binding sites resulting in multiple variants of their bispecificity.Survey of the year 2000 commercial optical biosensor literature.Comparison of DNA-hydrolyzing antibodies from the cerebrospinal fluid and serum of patients with multiple sclerosis.Systemic lupus erythematosus: molecular cloning and analysis of recombinant DNase monoclonal κ light chain NGK-1.Catalytic antibodies in healthy humans and patients with autoimmune and viral diseases.Systemic lupus erythematosus: molecular cloning and analysis of 22 individual recombinant monoclonal kappa light chains specifically hydrolyzing human myelin basic protein.Systemic lupus erythematosus: molecular cloning and analysis of recombinant monoclonal kappa light chain NGTA2-Me-pro-ChTr possessing two different activities-trypsin-like and metalloprotease.DNA-hydrolysing activity of IgG antibodies from the sera of patients with schizophreniaComparison of Antibodies with Amylase Activity from Cerebrospinal Fluid and Serum of Patients with Multiple Sclerosis.Systemic lupus erythematosus: molecular cloning and analysis of recombinant monoclonal kappa light chain NGTA1-Me-pro with two metalloprotease active centers.Multitarget selection of catalytic antibodies with β-lactamase activity using phage display.Chemical polysialylation of human recombinant butyrylcholinesterase delivers a long-acting bioscavenger for nerve agents in vivo.Biochemical features of a catalytic antibody light chain, 22F6, prepared from human lymphocytes.Affinity and catalytic heterogeneity of polyclonal myelin basic protein-hydrolyzing IgGs from sera of patients with multiple sclerosisNanobody; an old concept and new vehicle for immunotargeting.How human IgGs against myelin basic protein (MBP) recognize oligopeptides and MBP.Functional mapping of the anti-idiotypic antibody anti-TS1 scFv using site-directed mutagenesis and kinetic analysisCatalytic features and eradication ability of antibody light-chain UA15-L against Helicobacter pylori.Antibodies from the sera of HIV-infected patients efficiently hydrolyze all human histones.Deoxyribonuclease activity of polyclonal IgGs: a putative serological marker in patients with spondyloarthritides.Generation, characterization, and docking studies of DNA-hydrolyzing recombinant F(ab) antibodies.Toward selective covalent inactivation of pathogenic antibodies: a phosphate diester analog of vasoactive intestinal peptide that inactivates catalytic autoantibodies.Ontogeny of proteolytic immunity: IgM serine proteases.Diversity of DNA-hydrolyzing antibodies from the sera of autoimmune-prone MRL/MpJ-lpr mice.Broadly distributed chemical reactivity of natural antibodies expressed in coordination with specific antigen binding activity.Specific degradation of H. pylori urease by a catalytic antibody light chain.Affinity and catalytic heterogeneity and metal-dependence of polyclonal myelin basic protein-hydrolyzing IgGs from sera of patients with systemic lupus erythematosus.Catalytic digestion of human tumor necrosis factor-α by antibody heavy chain.
P2860
Q28484841-BF5D3537-B815-4D79-B5D3-8B26E518095AQ30386064-1A0EF771-D1D5-4917-84AB-33EA1BDDDC26Q33187520-67E772F8-AE15-4CA7-A342-6550F5F9B5C7Q33419724-752A8F3A-7E77-4205-B4C1-0B8AB9B18F79Q34266957-FC362DB4-2C3F-4B48-B119-9FEB19F3E45DQ34389092-838D248B-47B1-40E6-AF2C-0D28155281A8Q34464911-0570EAD2-86EC-44E1-9E99-205F19304277Q35149485-9BC6402B-B5AC-4992-A043-D4BD88D11C73Q35185626-67C03C39-FBB2-4B12-AD49-E23A3DD82498Q35574151-26194EFE-294A-4430-879E-2011D1E27DDCQ35600192-875423EC-F62B-4935-8DCE-21053311D877Q35691336-BEA81FFB-04F2-4C64-B3DB-1B2E09D3028AQ35779904-0FD7F837-ED83-49FC-91FD-1976ABB7391CQ36022441-79871DC9-A564-4FCE-ABC7-67E1722A4CB2Q36174449-468BBE88-5E18-480B-950A-890BA95E15B3Q36246066-66F16F75-1CE0-4150-8B34-053118ABE6B1Q36567954-6414F01E-E71F-4612-8390-2F878CBEC881Q37000547-D5E68E01-9CDD-4280-A546-9AC3A7A25E8DQ37296340-62F2642B-01E0-4305-B764-7793ABC99FF2Q37829737-234F1DBD-2974-4F93-B293-F803F8F153A4Q38805503-6520F360-3E81-45D7-BD71-C7842795FCB7Q39810820-818DB9AB-9038-4EB3-9DE9-2A98AEDAD8A8Q40155856-9465A2DB-6B0F-4C1F-B1AB-1E5AE029B2EBQ40821819-8D0F37FC-9BDF-4AA0-8B9B-99B7C12E4D47Q42266445-5CB2D55F-C1AB-4AAB-BA00-CD678E48DFE2Q42798552-E3B36B56-2608-4FDE-94A9-B4F0CDAA45B2Q44693889-C1C6BF31-612C-4474-A3CB-83ACCC374FF9Q44730627-C7967A7C-00C3-407A-B9C8-F8C355DC5020Q45172471-9288173D-A8EE-4D11-A645-C07D4C4B9677Q48253017-2515DA0F-D1EC-4AE3-B090-7D860BD3A470Q51965368-7DD11CBF-EEF2-414D-82AA-91A250A20F6FQ53209420-E660ACB8-6E9B-417C-9DE2-929FFE0532F3Q53305638-0CB61402-649A-4FF4-B3AB-40CA6F01EF41
P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Enzyme mimicry by the antiidiotypic antibody approach.
@ast
Enzyme mimicry by the antiidiotypic antibody approach.
@en
type
label
Enzyme mimicry by the antiidiotypic antibody approach.
@ast
Enzyme mimicry by the antiidiotypic antibody approach.
@en
prefLabel
Enzyme mimicry by the antiidiotypic antibody approach.
@ast
Enzyme mimicry by the antiidiotypic antibody approach.
@en
P2093
P2860
P356
P1476
Enzyme mimicry by the antiidiotypic antibody approach.
@en
P2093
Alexandrova ES
Friboulet A
Gabibov AG
Kolesnikov AV
Koralewski F
P2860
P304
13526-13531
P356
10.1073/PNAS.200360497
P407
P577
2000-12-01T00:00:00Z