Results 31 to 40 of about 1,115,659 (268)

The planar cell polarity protein Vangl2 interacts with the PDZ‐domains of Scribble but not with a unique PDZ‐like domain in Inturned

open access: yesFEBS Letters, EarlyView.
Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes   +4 more
wiley   +1 more source

Predicting protein disorder by analyzing amino acid sequence

open access: yesBMC Genomics, 2008
Background Many protein regions and some entire proteins have no definite tertiary structure, presenting instead as dynamic, disorder ensembles under different physiochemical circumstances.
Yang Mary, Yang Jack Y
doaj   +1 more source

Low level sequence variant analysis of recombinant proteins: an optimized approach.

open access: yesPLoS ONE, 2012
Sequence variants in recombinant biopharmaceuticals may have a relevant and unpredictable impact on clinical safety and efficacy. Hence, their sensitive analysis is important throughout bioprocess development.
Anne Zeck   +10 more
doaj   +1 more source

Molecular diagnosis and genetic relationship of foot and mouth disease virus serotype Asia1/Basne/Sul/2015 [PDF]

open access: yesIraqi Journal of Veterinary Sciences, 2019
Foot and Mouth Disease (FMD) is the most economically important viral-induced livestock disease worldwide. From April to May of 2015, tongue epithelial tissue samples were collected from 36 cattle in six villages, which share the border with Iran ...
Jeza Muhamad Abdul aziz   +2 more
doaj   +1 more source

Calpain small subunit homodimerization is robust and calcium‐independent

open access: yesFEBS Letters, EarlyView.
Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy   +4 more
wiley   +1 more source

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

open access: yesFEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai   +4 more
wiley   +1 more source

Incorporating background frequency improves entropy-based residue conservation measures

open access: yesBMC Bioinformatics, 2006
Background Several entropy-based methods have been developed for scoring sequence conservation in protein multiple sequence alignments. High scoring amino acid positions may correlate with structurally or functionally important residues.
Samudrala Ram, Wang Kai
doaj   +1 more source

Modulation of Homer1 EVH1 domain internal dynamics by putative autism‐associated mutations

open access: yesFEBS Letters, EarlyView.
The putative autism‐associated M65I and S97L variants of the EVH1 domain of the postsynaptic scaffold protein Homer1 do not exhibit substantial changes in their overall structure or partner binding. Both of them, but especially the M65I variant, show altered internal dynamics relative to the wild‐type domain on the μs‐ms timescale, indicated by the ...
Fanni Farkas   +6 more
wiley   +1 more source

SSE: a nucleotide and amino acid sequence analysis platform

open access: yesBMC Research Notes, 2012
Background There is an increasing need to develop bioinformatic tools to organise and analyse the rapidly growing amount of nucleotide and amino acid sequence data in organisms ranging from viruses to eukaryotes.
Simmonds Peter
doaj   +1 more source

The Amino Acid Sequence of Chromatium Ferredoxin

open access: yesJournal of Biological Chemistry, 1970
The amino acid sequence of Chromatium ferredoxin was determined by studies of thermolysin peptides of S-carboxymethylcysteinylferredoxin and chymotryptic peptides of oxidized ferredoxin. The 81 amino acid residues in the molecule have the following sequence: Ala-Leu-Met-Ile-Thr-Asp-Gln-Cys-Ile-Asn-Cys-Asn-Val-Cys-Gln-Pro-Glu-Cys-Pro-Asn-Gly-Ala-Ile-Ser-
H, Matsubara   +3 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy