Results 61 to 70 of about 3,835,960 (298)

Degradation mechanism of the von Willebrand factor A2 domain by nattokinase

open access: yesFEBS Letters, EarlyView.
Nattokinase, a natto‐derived protease, exhibits potent antithrombotic effects. This study demonstrates that nattokinase directly cleaves the von Willebrand factor (vWF) A2 domain in vitro. Unlike the native regulator ADAMTS13, nattokinase degrades folded vWF independently of shear stress.
Ryuichi Hyakumoto   +3 more
wiley   +1 more source

The Prion-like domain in the exomer-dependent cargo Pin2 serves as a trans-Golgi retention motif [PDF]

open access: yes, 2014
Prion and prion-like domains (PLDs) are found in many proteins throughout the animal kingdom. We found that the PLD in the S. cerevisiae exomer-depen- dent cargo protein Pin2 is involved in the regulation of protein transport and localization. The domain
Ritz, Alicja M.   +11 more
core   +1 more source

Health and growth of weaned Holstein and crossbred calves fed bovine plasma proteins in grower feed

open access: yesJournal of Dairy Science
: Feeding plasma protein has been shown to have health benefits and help ameliorate stress in preweaning calves, aiding their ability to handle the challenges of weaning and initial social interactions.
M.L. Pister   +3 more
doaj   +1 more source

PLASMA LIPID TRANSFER PROTEINS [PDF]

open access: yesAnnual Review of Biochemistry, 1988
The plasma lipid transfer proteins mediate the transfer and exchange of phospholipids and neutral lipids between the plasma lipoproteins. The cholesteryl ester transfer protein (CETP) and the phospholipid transfer protein (PLTP) are members of the lipid transfer/lipopolysaccharide binding gene family.
openaire   +4 more sources

ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains

open access: yesFEBS Letters, EarlyView.
CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens   +8 more
wiley   +1 more source

Microbiome‐blood–brain barrier interactions in aging — mechanisms and therapeutic potential

open access: yesFEBS Letters, EarlyView.
Aging reshapes the gut microbiome (↓SCFA‐producing commensals; ↑pro‐inflammatory outputs), shifting circulating metabolites (↓SCFAs; ↑LPS, ↑TMAO, ↑PAA) that act at the BBB to increase nonspecific transcytosis, alter transport, and promote astrocyte reactivity, heightening brain vulnerability.
Daniel Cuervo‐Zanatta   +3 more
wiley   +1 more source

Generation of specific antibodies against the rap1A, rap1B and rap2 small GTP-binding proteins. Analysis of rap and ras proteins in membranes from mammalian cells [PDF]

open access: yes, 1992
Specific antibodies against rap1A and rap1B small GTP-binding proteins were generated by immunization of rabbits with peptides derived from the C-terminus of the processed proteins.
Schwaner, I.   +5 more
core   +1 more source

Exposure–Response Relationship of Toxic Metal(loid)s in Mammals: Their Bioinorganic Chemistry in Blood Is an Intrinsic Component of the Selectivity Filters That Mediate Organ Availability

open access: yesToxics
The gastrointestinal tract mediates the absorption of nutrients from the diet, which is increasingly contaminated with toxic metal(loid) species (TMs) and thus threatens food safety.
Manon Fanny Degorge, Jürgen Gailer
doaj   +1 more source

Discerning protein pools by selective staining with self‐labeling tags

open access: yesFEBS Letters, EarlyView.
Cell surface proteins have an intra‐ and extracellular pool. Combining genetic fusion to self‐labeling tags that can be addressed with small molecule fluorophores allows separating these pools. We highlight recent developments and techniques for state‐of‐the‐art interrogation of cell surface proteins in the complex tissue setting.
Kati Fischermanns, Johannes Broichhagen
wiley   +1 more source

Peripheral lysosomes recruit PLEKHG3 to focal adhesions and restrain protrusion dynamics

open access: yesFEBS Letters, EarlyView.
Proximity‐dependent labeling at the LAMTOR complex revealed the Rho GEF PLEKHG3 as a lysosome‐proximal protein directing the study toward the influence of lysosome positioning on actin dynamics and cell motility. We show that PLEKHG3 colocalizes with lysosomes at focal adhesion sites and observe that forced peripheral dispersion of lysosomes hinders ...
Rainer Ettelt   +8 more
wiley   +1 more source

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