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The diversity of H3 loops determines the antigen-binding tendencies of antibody CDR loops.
Not available
S-EPMC4941225
|
biostudies-literature
Cite
Comparative Analysis of the CDR Loops of Antigen Receptors.
Not available
S-EPMC6803477
|
biostudies-literature
Cite
Accurate Structure Prediction of CDR H3 Loops Enabled by a Novel Structure-Based C-Terminal Constraint.
Not available
S-EPMC5173470
|
biostudies-literature
Cite
Antibody CDR loops as ensembles in solution vs. canonical clusters from X-ray structures.
Not available
S-EPMC7153821
|
biostudies-literature
Cite
Distance-Guided Forward and Backward Chain-Growth Monte Carlo Method for Conformational Sampling and Structural Prediction of Antibody CDR-H3 Loops.
Not available
S-EPMC5565776
|
biostudies-literature
Cite
Repertoire Analysis of Antibody CDR-H3 Loops Suggests Affinity Maturation Does Not Typically Result in Rigidification.
Not available
S-EPMC5840193
|
biostudies-literature
Cite
The origin of CDR H3 structural diversity.
Not available
S-EPMC4318709
|
biostudies-literature
Cite
Revisiting antibody modeling assessment for CDR-H3 loop.
Not available
S-EPMC5081041
|
biostudies-literature
Cite
VHH CDR-H3 conformation is determined by VH germline usage.
Not available
S-EPMC10439903
|
biostudies-literature
Cite
Canonical structures of short CDR-L3 in antibodies.
Not available
S-EPMC4260120
|
biostudies-literature
Cite
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