Results 231 to 240 of about 228,811 (282)

Beyond species diversity: Functional responses of cave arthropods to microclimatic stability and structural complexity

open access: yesEcological Entomology, EarlyView.
Species richness declined along cave microclimatic gradient, while diversity increased with habitat heterogeneity, highlighting distinct roles of abiotic conditions and structural complexity in shaping arthropod communities. Functional traits shifted along the microclimatic gradient, with larger‐bodied and more eye‐regressed arthropods dominating under
Raluca Ioana Bǎncilǎ   +7 more
wiley   +1 more source

The malate–aspartate shuttle supports thermogenic lipid mobilization in brown adipocytes

open access: yesThe FEBS Journal, EarlyView.
Brown fat cells burn lipids within their mitochondria to generate heat. This process involves two energy “shuttles,” one of which is naturally blocked during heat production. We found that the second shuttle (MASh) is not required to generate heat. However, when MASh is disabled, the fatty acids meant for fuel are instead converted back into stored fat.
Michaela Veliova   +12 more
wiley   +1 more source

Steroidogenic compensation and lipid deficiency with enhanced NAD+ salvage in small‐for‐gestational‐age placenta

open access: yesThe FEBS Journal, EarlyView.
Fetal growth restriction is associated with placental metabolic adaptations. In small‐for‐gestational‐age placenta (SGA), cholesterol receptors and steroidogenic enzymes are upregulated, enhancing steroidogenesis. NAD salvage pathway is also increased to support NADP+/NADPH requirements.
Serena Xodo   +4 more
wiley   +1 more source

Superficial Retinal Intercapillary Oxygen Diffusion and Perfusion Deficit Alterations in Patients With Coronary Artery Disease. [PDF]

open access: yesInvest Ophthalmol Vis Sci
Jeremic N   +10 more
europepmc   +1 more source

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation

open access: yesThe FEBS Journal, EarlyView.
Investigated mutations in transthyretin (TTR) disrupt the F87‐centered hydrophobic core that stabilizes its tetrameric structure. The mild I107V mutation weakens inter‐chain packing, while H88R fully abolishes tetramer formation, yielding a monomeric, aggregation‐prone form. Structural, biophysical, and computational analyses reveal that both mutations
István L. Bódy   +7 more
wiley   +1 more source

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