Results 121 to 130 of about 737,709 (296)

Tau acetylation at K331 has limited impact on tau pathology in vivo

FEBS Letters, EarlyView.
We mapped tau post‐translational modifications in humanized MAPT knock‐in mice and in amyloid‐bearing double knock‐in mice. Acetylation within the repeat domain, particularly around K331, showed modest increases under amyloid pathology. To test functional relevance, we generated MAPTK331Q knock‐in mice.
Shoko Hashimoto, Yukio Matsuba, Mika Takahashi, Takaomi C. Saido   +3 more
wiley   +1 more source

Calpain small subunit homodimerization is robust and calcium‐independent

FEBS Letters, EarlyView.
Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy, Trina Dykstra‐MacPherson, Mathias A. Bell, Peter L. Davies, Ruby May A. Sullan   +4 more
wiley   +1 more source

Protein aggregation: folding aggregates, inclusion bodies and amyloid

Folding and Design, 1998
Aggregation results in the formation of inclusion bodies, amyloid fibrils and folding aggregates. Substantial data support the hypothesis that partially folded intermediates are key precursors to aggregates, that aggregation involves specific intermolecular interactions and that most aggregates involve beta sheets.
openaire   +2 more sources

Structural insights into an engineered feruloyl esterase with improved MHET degrading properties

FEBS Letters, EarlyView.
A feruloyl esterase was engineered to mimic key features of MHETase, enhancing the degradation of PET oligomers. Structural and computational analysis reveal how a point mutation stabilizes the active site and reshapes the binding cleft, expading substrate scope.
Panagiota Karampa, Konstantinos Makryniotis, Theofani‐Iosifina Sousani, Evangelos Topakas, Vangelis Daskalakis, Maria Dimarogona   +5 more
wiley   +1 more source

Polysorbates, peroxides, protein aggregation, and immunogenicity – a growing concern

Journal of Excipients and Food Chemicals, 2016
Aggregation can have a number of deleterious effects on biotherapeutics including the loss of efficacy, the induction of unwanted immunogenicity, altered pharmacokinetics, and reduced shelf life. Aggregation is ameliorated by the inclusion of surfactants
Edward T. Maggio
doaj  

On the statistical mechanics of prion diseases

, 2001
We simulate a two-dimensional, lattice based, protein-level statistical mechanical model for prion diseases (e.g., Mad Cow disease) with concommitant prion protein misfolding and aggregation.
A. Coghlan, A. Slepoy, C. I. Lasmézas, D. J. Stekel, D. L. Cox, D. O. V. Alonso, F. Pázmándi, H. Rudyk, J. H. Come, J. Masel, J. N. Onuchic, J. S. Griffith, K. Post, M. A. Nowak, M. Beekes, M. Eigen, M. Horiuchi, M. Horiuchi, M. Laurent, R. Demaimay, R. M. Anderson, R. R. P. Singh, R. V. Kulkarni, S. B. Prusiner, T. R. Serio, W. Swietnicki   +25 more
core   +1 more source

Gut microbiome and aging—A dynamic interplay of microbes, metabolites, and the immune system

FEBS Letters, EarlyView.
Age‐dependent shifts in microbial communities engender shifts in microbial metabolite profiles. These in turn drive shifts in barrier surface permeability of the gut and brain and induce immune activation. When paired with preexisting age‐related chronic inflammation this increases the risk of neuroinflammation and neurodegenerative diseases.
Aaron Mehl, Eran Blacher
wiley   +1 more source

Study of cosolvent-induced α-chymotrypsin fibrillogenesis: Does protein surface hydrophobicity trigger early stages of aggregation reaction? [PDF]

The misfolding of specific proteins is often associated with their assembly into fibrillar aggregates, commonly termed amyloid fibrils. Despite the many efforts expended to characterize amyloid formation in vitro, there is no deep knowledge about the ...
A Ahmad, A Cammers-Goodwin, A Cao, A Coli, A Cooper, A Lorenzo, A Monji, AFSA Habeeb, BC Hummel, BI Kurganov, CR Cantor, D Canet, D Hamada, D Hong, D Howlett, D Morshedi, E Gazit, EDB Clark, F Chiti, G Plakoutsi, G Soldi, G Zettlmeissl, H Shoval, H Shoval, HA Khanova, HB Dixon, Hosnieh Soori, HT Wright, I Pallares, JC Janson, JCS Breitner, JM Mason, K Gast, K Verstraete, LN Arnaudov, LO Tjernberg, M Goodman, M Holley, M Pappolla, ME McGrath, Mojtaba Amani, MR Nilsson, MT Fisher, N Rezaei-Ghaleh, N Rezaei-Ghaleh, N Rezaei-Ghaleh, N Rezaei-Ghaleh, N Rezaei-Ghaleh, OH Lowry, R Eisert, R Khodarahmi, R Khodarahmi, R Khodarahmi, R Khodarahmi, R Khurana, R Sabate, R Walgers, R Yazdanparast, Reza Khodarahmi, S Meehan, SJ Hamodrakas, SL Snyder, T Cohen, V Bellotti, VN Uversky, VN Uversky, Y Porat   +66 more
core   +1 more source

A methionine‐lined active site governs carbocation stabilization and product specificity in a bacterial terpene synthase

FEBS Letters, EarlyView.
This study reveals a unique active site enriched in methionine residues and demonstrates that these residues play a critical role by stabilizing carbocation intermediates through novel sulfur–cation interactions. Structure‐guided mutagenesis further revealed variants with significantly altered product profiles, enhancing pseudopterosin formation. These
Marion Ringel, Carl P. O. Helmer, Shani Zev, Ronja Driller, Emily Buhr, Markus Reinbold, Renana Schwartz, Gabriel Foley, Mikael Boden, Daniel Garbe, Gerhard Schenk, Dan Thomas Major, Bernhard Loll, Thomas Brück   +13 more
wiley   +1 more source

Valosin‐containing protein counteracts ATP‐driven dissolution of FUS condensates through its ATPase activity in vitro

FEBS Letters, EarlyView.
Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura, Shin‐ichi Tate, Kyota Yasuda   +2 more
wiley   +1 more source