All-D peptides recognized by an anti-carbohydrate antibody identified from a positional scanning library.
about
Evolutionary transition pathways for changing peptide ligand specificity and structureDirecting the immune response to carbohydrate antigens.Reversible inhibitors of lambda integrase-mediated recombination efficiently trap Holliday junction intermediates and form the basis of a novel assay for junction resolution.Plasticity in structure and interactions is critical for the action of indolicidin, an antibacterial peptide of innate immune origin.A molecular basis for functional peptide mimicry of a carbohydrate antigen.
P2860
All-D peptides recognized by an anti-carbohydrate antibody identified from a positional scanning library.
description
1998 nî lūn-bûn
@nan
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
All-D peptides recognized by a ...... a positional scanning library.
@ast
All-D peptides recognized by a ...... a positional scanning library.
@en
type
label
All-D peptides recognized by a ...... a positional scanning library.
@ast
All-D peptides recognized by a ...... a positional scanning library.
@en
prefLabel
All-D peptides recognized by a ...... a positional scanning library.
@ast
All-D peptides recognized by a ...... a positional scanning library.
@en
P2093
P356
P1476
All-D peptides recognized by a ...... a positional scanning library
@en
P2093
Buencamino J
Campbell GD
Greenspan NS
P304
P356
10.1006/JMBI.1998.2137
P577
1998-11-01T00:00:00Z