Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation.
about
VnD: a structure-centric database of disease-related SNPs and drugsSelf-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EASEdge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphataseA motor neuron disease-associated mutation in p150Glued perturbs dynactin function and induces protein aggregation.Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions.Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.A comparative structural bioinformatics analysis of the insulin receptor family ectodomain based on phylogenetic information.Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20Prevention of amyloid-like aggregation as a driving force of protein evolution.Mapping the structural transition in an amyloidogenic apolipoprotein A-IFolding versus aggregation: polypeptide conformations on competing pathwaysThe importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidosesNatural selection against protein aggregation on self-interacting and essential proteins in yeast, fly, and worm.Freedom not aggregation.Global computational mutagenesis provides a critical stability framework in protein structures.Putative aggregation initiation sites in prion protein.
P2860
Q24607829-D95C7382-142C-4B2F-9379-18A5D8806173Q27677102-C014220C-B60E-4CA0-A8F3-6D1CBE942A7EQ27690644-F884EE5C-AB1D-4383-AF83-F2005134110BQ30480370-DBC30CDA-66AD-47E6-BD98-B37C5DBB5ECCQ30502077-24ED28F6-DD8A-46B1-B066-ABA5EA992552Q33356197-64EFE210-FA5D-4191-BB63-CCCBC99D1B5FQ33383201-14242862-7ED4-4232-BDDB-271BADD791BBQ34114138-63A647F7-670E-4648-9D31-8DCCAAA26AC6Q34658253-ED660CA3-A588-4CDF-AEDD-AE78BCCAE0A0Q36833883-3025845D-118A-432A-B9D1-8F20815783F8Q36858313-8F08CF18-C328-44EB-AA7F-3EE041D5B341Q41920394-2430A452-2DF7-488C-8A7F-46D72234B7CEQ43069194-8855FEB3-04A8-4D10-94E7-7DB8428CAA66Q46147132-65D74392-6EDF-455E-A536-410076ABD67CQ46245936-B96B78EF-9FCF-4735-AF11-6EE395B100F5Q47844161-C8D82F4F-CC10-4034-B892-2CB5CA410764
P2860
Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation.
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Glycine residues appear to be ...... bility to inhibit aggregation.
@ast
Glycine residues appear to be ...... bility to inhibit aggregation.
@en
Glycine residues appear to be ...... bility to inhibit aggregation.
@nl
type
label
Glycine residues appear to be ...... bility to inhibit aggregation.
@ast
Glycine residues appear to be ...... bility to inhibit aggregation.
@en
Glycine residues appear to be ...... bility to inhibit aggregation.
@nl
prefLabel
Glycine residues appear to be ...... bility to inhibit aggregation.
@ast
Glycine residues appear to be ...... bility to inhibit aggregation.
@en
Glycine residues appear to be ...... bility to inhibit aggregation.
@nl
P2093
P50
P921
P1433
P1476
Glycine residues appear to be ...... bility to inhibit aggregation.
@en
P2093
Claudia Parrini
Fabrizio Chiti
Giampietro Ramponi
Niccolò Taddei
P304
P356
10.1016/J.STR.2005.04.022
P577
2005-08-01T00:00:00Z