Results 161 to 170 of about 1,578,929 (319)
The presence of biotin‐binding avidin proteins in fish and their biological significance are poorly characterized. We cataloged fish avidins and demonstrate that they are widely present and evolutionarily conserved. We created avd knockout zebrafish and show that zebavidin is dispensable for development and that resistance of avd knockout embryos in ...
Anni K. Saralahti +5 more
wiley +1 more source
HELIN Access Services Affinity Group minutes for 10/18/12
Minutes of the Access Services Affinity Group of the HELIN Consortium for October ...
HELIN Consortium. Access Services Affinity Group
core
In this study, a novel esterase from the thermoacidophilic archaeon Thermoplasma acidophilum was biochemically and structurally characterized. Our results demonstrate that Ta0887 is a highly thermostable esterase that preferentially hydrolyzes p‐nitrophenyl hexanoate and possesses an α‐helical cap domain that likely contributes to its substrate ...
Alejandro Delgado‐Rey +4 more
wiley +1 more source
Germinal Center Selection and Plasma Cell Differentiation. [PDF]
Sprumont A, Bannard O.
europepmc +1 more source
HELIN E-Resources Affinity Group Minutes for 1/22/2015
Minutes of the E-Resources Affinity Group of the HELIN Consortium for Jan ...
HELIN Consortium. E-Resources Affinity Group
core
Threonine 348 regulates the subcellular localization of PTEN
Thr348 in the C2 domain is a key contributor to PTEN subcellular localization. The PTEN350 fragment and PTENA4 accumulated in the nucleus, whereas PTENK13R,A4 predominantly localized to the plasma membrane. In contrast, substitution of Thr348 with Asp (T348D) disrupted these characteristic localization patterns, resulting in predominant cytoplasmic ...
Takashi Kato, Suzu Tanaka, Miyu Ohashi
wiley +1 more source
DyAb: sequence-based antibody design and property prediction in a low-data regime. [PDF]
Lin JY +15 more
europepmc +1 more source
HELIN E-Resources Affinity Group minutes for 10/23/2014
Minutes of the E-Resources Affinity Group of the HELIN Consortium for Oct ...
HELIN Consortium. E-Resources Affinity Group
core
A minimal cellulosome‐like system in Cellulosilyticum lentocellum
Cellulose‐degrading bacteria typically use cellulosomes, large multi‐enzyme complexes on a scaffold protein. In Cellulosilyticum lentocellum, we characterise a far smaller arrangement, a single scaffold bound to one cellulase through a single cohesin‐dockerin interaction.
John Allan +2 more
wiley +1 more source
Evaluating molecular docking for binding affinity predictions: a systematic analysis of key parameters and the utility of AlphaFold2 structures for the Schrödinger dataset. [PDF]
Tornesakis K +3 more
europepmc +1 more source

