Ostwald Process Intensification by Catalytic Oxidation of Nitric Oxide. [PDF]
Gopakumar J +6 more
europepmc +1 more source
Process intensification of atorvastatin calcium crystallization for target polymorph development via continuous combined cooling and antisolvent crystallization using an oscillatory baffled crystallizer. [PDF]
Kshirsagar S +3 more
europepmc +1 more source
Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane +11 more
wiley +1 more source
Process Intensification at the Nanoscale: Embedding SiC in Zeolites for Energy-Efficient Catalysis. [PDF]
Young AF +5 more
europepmc +1 more source
Process intensification of continuous-flow seATRP by a sonicated multi-reactor setup.
Zhang S, Junkers T, Kuhn S.
europepmc +1 more source
A new reactor for process intensification involving the simultaneous application of adjustable ultrasound and microwave radiation. [PDF]
Călinescu I +4 more
europepmc +1 more source
Mass spectrometry based identification of AMP‐O‐Tris generated by Thermococcus onnurineus Cas10
Isolated Thermococcus onnurineus Cas10 generates the noncanonical ATP‐derived product AMP‐O‐Tris while in Tris‐containing buffer as identified via mass spectrometry, revealing relaxed nucleophile selectivity under isolated conditions. These findings suggest that multiprotein Csm complex assembly restricts Cas10 reactivity toward canonical cyclic ...
Su‐Jin Lee +6 more
wiley +1 more source
Process Intensification for Recombinant Marburg Virus Glycoprotein Production Using <i>Drosophila</i> S2 Cells. [PDF]
Göbel S +7 more
europepmc +1 more source
Ultrasound-assisted solution crystallization of fotagliptin benzoate: Process intensification and crystal product optimization. [PDF]
Fang L +6 more
europepmc +1 more source
This paper reveals how human lactoferrin–albumin fusion (hLF‐HSA) potently suppresses lung adenocarcinoma cell migration. hLF‐HSA upregulates NHE7, leading to Golgi alkalization, disruption of the Golgi secretome, downregulation of MMP1, and reversal of EMT. These findings suggest a novel Golgi‐targeting strategy to suppress cancer cell migration.
Hana Nopia +3 more
wiley +1 more source

