α-Synuclein induces deficiency in clathrin-mediated endocytosis through inhibiting synaptojanin1 expression.

Parkinson's disease (PD) is an age-related chronic neurological disorder, mainly characterized by the pathological feature of α-synuclein (α-syn) aggregation, with the exact disease pathogenesis unclear. During the onset and progression of PD, synaptic dysfunction, including dysregulation of axonal transport, impaired exocytosis, and endocytosis are identified as crucial events of PD pathogenesis. It has been reported that over-expression of α-syn impairs clathrin-mediated endocytosis (CME) in the synapses.

Heterologous expression and biochemical characterization of a cold-active lipase from Rhizopus microsporus suitable for oleate synthesis and bread making.

Objectives: Cold-active lipases which show high specific activity at low temperatures are attractive in industrial applications in terms of product stability and energy saving. We aimed to identify novel cold-active lipase suitable for oleates synthesis and bread making.

Results: A novel lipase gene (RmLipA) from Rhizopus microsporus was cloned and heterologously expressed in Pichia pastoris.

Psychosocial Mechanism of Adolescents' Depression: A Dose-Response Relation with Physical Activity.

Depression has become the most prevalent mental health problem in developing countries, and especially among adolescents. Lubans and his colleagues proposed a psychosocial mechanism to understand the trajectory of mental health (i.e.

High-level expression and characterization of a novel phospholipase C from Thielavia terrestris suitable for oil degumming.

A novel phospholipase C gene (TtPLC) from Thielavia terrestris CAU709 was cloned and efficiently expressed in Pichia pastoris. The deduced protein sequence of TtPLC shared the highest identity of 33% with the characterized phospholipase C from Arabidopsis thaliana. The highest phospholipase C yield of 98, 970 U mL, with a protein concentration of 4.

Biochemical characterization of a novel lipase from Malbranchea cinnamomea suitable for production of lipolyzed milkfat flavor and biodegradation of phthalate esters.

A novel lipase gene (McLipB) was cloned from a thermophilic fungus Malbranchea cinnamomea and expressed in Pichia pastoris. The deduced amino acid sequence of the lipase (McLipB) shared the highest identity of 46% with the Candida rugosa lipase LIP4. The extracellular lipase activity of 4304 U/mL with protein concentration of 7.

High-level expression of codon-optimized Thielavia terrestris cutinase suitable for ester biosynthesis and biodegradation.

A codon-optimized cutinase gene (TtCutopt) from Thielavia terrestris was over-expressed in Pichia pastoris. An extracellular activity reached 10,200 U/mL using high cell density fermentation. The optimal pH and temperature of TtCutopt were 7.