Results 131 to 140 of about 287,910 (304)

PARK(ing) time–How park deficiency affects the biological clock in a Drosophila model of Parkinson's disease

FEBS Letters, EarlyView.
Drosophila park mutants serve as a model for Parkinson's disease. We used this strain to investigate the connection between oxidative stress and the circadian clock mechanism. We showed that increased oxidative stress affects the physiology of pacemaker cells, disrupting their daily structural plasticity. Lack of rhythmic signaling from pacemaker cells
Kamila Zientara, Kinga Skoczek, Elzbieta Pyza, Milena Damulewicz   +3 more
wiley   +1 more source

Lysosomal targeting of liposomes with acidic pH and Cathepsin B induces protein aggregate clearance

Cell Communication and Signaling
The autophagy-lysosomal pathway is a cellular degradation mechanism that regulates protein quality by eliminating aggregates and maintaining normal protein function.
Minsol Jeon, Da-Eun Kim, So Young Choi, Seoyoung Kim, Seongchan Kim, Hyojin Lee, Hyunkyung Kim   +6 more
doaj   +1 more source

Structural insights and therapeutic targets in Acinetobacter baumannii capsule biosynthesis

FEBS Letters, EarlyView.
Hypervirulent KL49 A. baumannii's capsular polysaccharide contains the nonulosonic acid 8‐epi‐Leg5,7Ac2, synthesized by epimerization via ElaA, ElaB, and ElaC. Crystal structures of ElaA, ElaB, and ElaC reveal their role in CMP‐Leg5,7Ac2 synthesis and regioselective C8 epimerization.
Woo Cheol Lee, Junho Jeong, Chae Yeong Lee, Hyunjoon Cho, Man Hwan Oh, Je Chul Lee, Jee‐Young Lee, Yangmee Kim   +7 more
wiley   +1 more source

Cellular Handling of Protein Aggregates by Disaggregation Machines

, 2018
Both acute proteotoxic stresses that unfold proteins and expression of disease-causing mutant proteins that expose aggregation-prone regions can promote protein aggregation.
Mogk, Axel, Kampinga, Harm H., Kampinga, Harm H.; id_orcid, Harm H. Kampinga, Bernd Bukau, Axel Mogk, Bukau, Bernd   +6 more
core   +1 more source

A Structural Proteomics Exploration of Synphilin-1 and Alpha-Synuclein Interaction in Pathogenesis of Parkinson’s Disease

Biomolecules
Pathological significance of interaction of Synphilin-1 with mutated alpha-synuclein is well known to have serious consequences in causing the formation of inclusion bodies that are linked to Parkinson’s disease (PD). Information extracted so far pointed
Asmita Tripathi, Rajkrishna Mondal, Malay Mandal, Tapobrata Lahiri, Manoj Kumar Pal   +4 more
doaj   +1 more source

α‐Synuclein aggregation landscape from phase separation to neurotoxic intermediates

FEBS Letters, EarlyView.
Alpha‐synuclein aggregation in Parkinson's disease involves a complex landscape of transient intermediates, including oligomers, fibrils and liquid–liquid phase separation (LLPS). A view is emerging in which LLPS maturation into solid‐like condensates may contribute to the formation of neurotoxic species.
Silvia Arino, Giuliana Fusco, Alfonso De Simone   +2 more
wiley   +1 more source

Kinetics of Protein Aggregates Disposal by Aggrephagy

, 2017
Macroautophagy has generated considerable interest because of its ability to recognize and target protein inclusions found prevalent in neurodegenerative diseases to lysosomes for elimination.
Wong, Esther, E. Wong, Tan, S., S. Tan
core   +1 more source

Formation, structures and properties of whey protein aggregates

, 2015
The native whey proteins have been intensively used in a multitude of food applications due to their high nutritional, biological, and versatile techno-functional properties.
Bouhallab, Said, Famelart, Marie-Hélène, Guyomarc'H, Fanny, Croguennec, Thomas   +3 more
core   +1 more source

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

FEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

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

FEBS 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, Brendan W. Chandler, Anna M. Schmoker, Jaye L. Weinert, Charlotte A. Kearns, Warren T. Yacawych, Amila Šemić, Alicia M. Ebert, Bryan A. Ballif   +8 more
wiley   +1 more source