Results 191 to 200 of about 2,997,351 (334)
Protein O‐glycosylation in the Bacteroidota phylum
Species of the Bacteroidota phylum exhibit a unique O‐glycosylation system. It modifies noncytoplasmic proteins on a specific amino acid motif with a shared glycan core but a species‐specific outer glycan. A locus of multiple glycosyltransferases responsible for the synthesis of the outer glycan has been identified.
Lonneke Hoffmanns +2 more
wiley +1 more source
Andexanet alfa for the reversal of the low-molecular-weight heparin enoxaparin. [PDF]
van Haaps TF +11 more
europepmc +1 more source
Adsorption of Binary Hydrocarbon Mixtures on Activated Charcoal — Molecular Weight Variation [PDF]
Fernando Ore, R. W. Moulton
openalex +1 more source
Cleavable N‐terminal Thioredoxin fusion enabled soluble expression and purification of otherwise insoluble SARS‐CoV‐2 Nucleocapsid (N) protein. A four‐step purification strategy yielded highly homogeneous, RNA‐free N protein. Binding assays showed high RNA affinity (Kd ~ 28 nm). The study will facilitate high‐resolution structural studies of N protein,
Shweta Singh, Gagan D. Gupta
wiley +1 more source
Author Correction: Accurate molecular recognition from the lowest unoccupied molecular orbital
Xuehua Zhou, Shixing Yang, Chao Han
doaj +1 more source
The Molecular Weight of Myeloperoxidase. [PDF]
Anders Ehrenberg +5 more
openalex +1 more source
Microfluidic electro‐viscoelastic manipulation of extracellular vesicles
The electro‐viscoelastic manipulation as a potential method for separation of particles based on size. The particles introduced as a sheath flow migrate to the channel center under the influence of simultaneously applied electric field and pressure driven flow.
Seyedamirhosein Abdorahimzadeh +7 more
wiley +1 more source
Effect of SiO<sub>2</sub> Nanoparticles on PNVCL Polymerization and Molecular Weight Control. [PDF]
Gabriel AM +2 more
europepmc +1 more source
The analysis of the osmotic pressures of the serum proteins, and the molecular weights of albumins and globulins [PDF]
G. S. Adair, Muriel Elaine Robinson
openalex +1 more source
Two‐way inhibition of PAX5 transcriptional activity by PAX5::CBFA2T3
PAX5::CBFA2T3 (PAX5‐C) is a fusion protein of the B‐cell transcription factor, PAX5, and is found in B‐cell ALL. We propose a putative model of two‐way inhibition of PAX5 transcriptional activity by PAX5‐C. There are two ways of repression by PAX5‐C: DNA‐binding‐dependent way and HDAC‐dependent way, with either being sufficient for the repression. HDAC
Reina Ueno +12 more
wiley +1 more source

