Results 51 to 60 of about 1,344,747 (350)

Organoids in pediatric cancer research

open access: yesFEBS Letters, EarlyView.
Organoid technology has revolutionized cancer research, yet its application in pediatric oncology remains limited. Recent advances have enabled the development of pediatric tumor organoids, offering new insights into disease biology, treatment response, and interactions with the tumor microenvironment.
Carla Ríos Arceo, Jarno Drost
wiley   +1 more source

Involvement of sulfur assimilation in the low β subunit content of soybean seed storage protein revealed by comparative transcriptome analysis

open access: yesCrop Journal, 2019
The β subunit of soybean [Glycine max (L.) Merr.] seed storage protein is of great significance in sulfur-containing amino acid balance and soybean processing properties. The objective of this study was to elucidate the relationship between the β subunit
Xi Zhang   +9 more
doaj   +1 more source

Expression and Circular Dichroism Studies of the Extracellular Domain of the alpha Subunit of the Nicotinic Acetylcholine Receptor [PDF]

open access: yes, 1997
To provide material suitable for structural studies of the nicotinic acetylcholine receptor, we have expressed and purified the NH2-terminal extracellular domain of the mouse muscle alpha subunit.
Bjorkman, Pamela J.   +3 more
core  

Repurposing drugs to target nonalcoholic steatohepatitis [PDF]

open access: yes, 2019
Nonalcoholic fatty liver disease (NAFLD) is a complex disorder that has evolved in recent years as the leading global cause of chronic liver damage.
Pirola, Carlos José   +1 more
core   +1 more source

Reciprocal control of viral infection and phosphoinositide dynamics

open access: yesFEBS Letters, EarlyView.
Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
wiley   +1 more source

Deduced Primary Structure of the β Subunit of Brain Type II Ca2+/calmodulin-dependent Protein Kinase Determined by Molecular Cloning [PDF]

open access: yes, 1987
cDNA clones coding for the β subunit of rat brain type II Ca2+/calmodulin-dependent protein kinase were isolated and sequenced. The clones, including one containing the entire coding region, hybridize at high stringency to a single band of poly(A)+ RNA ...
Bennett, Mark K., Kennedy, Mary B.
core  

Photosynthesis under far‐red light—evolutionary adaptations and bioengineering of light‐harvesting complexes

open access: yesFEBS Letters, EarlyView.
Phototrophs evolved light‐harvesting systems adapted for efficient photon capture in habitats enriched in far‐red radiation. A subset of eukaryotic pigment‐binding proteins can absorb far‐red photons via low‐energy chlorophyll states known as red forms.
Antonello Amelii   +8 more
wiley   +1 more source

Structure of an archaeal PCNA1-PCNA2-FEN1 complex: elucidating PCNA subunit and client enzyme specificity. [PDF]

open access: yes, 2006
The archaeal/eukaryotic proliferating cell nuclear antigen (PCNA) toroidal clamp interacts with a host of DNA modifying enzymes, providing a stable anchorage and enhancing their respective processivities.
Andrew S. Doré   +48 more
core   +4 more sources

The anti‐CRISPR protein AcrIE8.1 inhibits the type I‐E CRISPR‐Cas system by directly binding to the Cascade subunit Cas11

open access: yesFEBS Letters, EarlyView.
In this study, we present the structure of AcrIE8.1, a previously uncharacterized anti‐CRISPR protein that inhibits the type I‐E CRISPR‐Cas system. Through a combination of structural and biochemical analyses, we demonstrate that AcrIE8.1 directly binds to the Cas11 subunit of the Cascade complex to inhibit the CRISPR‐Cas system.
Young Woo Kang, Hyun Ho Park
wiley   +1 more source

Subunit counting in membrane-bound proteins [PDF]

open access: yesNature Methods, 2007
The subunit number and stoichiometry of membrane-bound proteins are difficult to determine without disrupting their membrane environment. Here we describe a single-molecule technique for counting subunits of proteins in live cell membranes by observing bleaching steps of GFP fused to a protein of interest.
Maximilian H, Ulbrich, Ehud Y, Isacoff
openaire   +2 more sources

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