about
Understanding the structural basis for substrate and inhibitor recognition in eukaryotic GH11 xylanasesCrystal structure of a cellulosomal family 3 carbohydrate esterase from Clostridium thermocellum provides insights into the mechanism of substrate recognitionEvidence that family 35 carbohydrate binding modules display conserved specificity but divergent functionUnderstanding how diverse beta-mannanases recognize heterogeneous substratesSignature active site architectures illuminate the molecular basis for ligand specificity in family 35 carbohydrate binding moduleCircular Permutation Provides an Evolutionary Link between Two Families of Calcium-dependent Carbohydrate Binding ModulesSubstrate and Metal Ion Promiscuity in Mannosylglycerate SynthaseA Novel, Noncatalytic Carbohydrate-binding Module Displays Specificity for Galactose-containing Polysaccharides through Calcium-mediated OligomerizationHow nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificityProbing the mechanism of ligand recognition in family 29 carbohydrate-binding modules.Affinity maturation generates greatly improved xyloglucan-specific carbohydrate binding modulesStructural dissection and high-throughput screening of mannosylglycerate synthase.Differential recognition of plant cell walls by microbial xylan-specific carbohydrate-binding modules.Two common single nucleotide polymorphisms in the gene encoding beta-carotene 15,15'-monoxygenase alter beta-carotene metabolism in female volunteers.Ligand-mediated dimerization of a carbohydrate-binding molecule reveals a novel mechanism for protein-carbohydrate recognition.Probing the structural basis for the difference in thermostability displayed by family 10 xylanases.Understanding the biological rationale for the diversity of cellulose-directed carbohydrate-binding modules in prokaryotic enzymes.
P50
Q27649314-2442F874-6A02-4CD5-B3D2-D1E3EDDBF724Q27650452-87BA61AC-A915-43D0-92D9-B8081A73F42CQ27653810-982A634B-768D-4F4E-A7FF-246B58BFF75AQ27655475-C895364D-2E6C-4946-9B06-AE22581A05C6Q27661859-FF1E57E7-A045-4E81-AD4E-6FAC1C489D53Q27663603-13A10D83-D69C-4B06-9D29-9BC8617B2D51Q27666827-43C1AD50-E65F-419E-B1B4-8E3120039B60Q27667373-940917CE-EBC5-445F-A7CF-56564864C0D6Q27675364-C6BD3BB7-5602-412D-A886-BAC74C889C9BQ30985487-070C98ED-F789-4199-96C4-9109A39ADFFDQ33514131-5FF23B84-8725-4599-B443-F9228638E273Q34425961-4E9DA0A1-2F7E-4CC5-BEED-A49E1A7EF73CQ34574986-CB9B3C33-2846-4D80-B708-8F298B4F221EQ34602310-7BF51C7D-CB6E-4596-9730-C95A5C96AFD8Q38344029-A521E9F4-159E-4626-99A1-04FD7FE1BFDEQ40317981-A87C830C-6A55-42A3-8EC3-902943DFD721Q52855523-F7737B44-27D2-4C03-99B3-749F466D4692
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
James E Flint
@ast
James E Flint
@en
James E Flint
@es
James E Flint
@nl
type
label
James E Flint
@ast
James E Flint
@en
James E Flint
@es
James E Flint
@nl
prefLabel
James E Flint
@ast
James E Flint
@en
James E Flint
@es
James E Flint
@nl
P106
P1153
35944120400
P21
P31
P496
0000-0003-2923-7813