Results 61 to 70 of about 1,155,621 (272)

Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase. [PDF]

, 2011
Partitioning of polypeptides between protein folding and amyloid formation is of outstanding pathophysiological importance. Using yeast phosphoglycerate kinase as model, here we identify the features of the energy landscape that decide the fate of the ...
Gottfried Köhler, Agócs, Gergely, Köhler, Gottfried, Szabó, Bence T, Osváth, Szabolcs, Bence T. Szabó, Szabolcs Osváth, Gergely Agócs   +7 more
core   +1 more source

The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer

Molecular Oncology, EarlyView.
Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad, Silvio Carlo Ermanno Tosatto, Emanuela Leonardi   +2 more
wiley   +1 more source

Protein mis-folding and human disease

, 2010
Serum Amyloid P Component (SAP), a putative molecular chaperone, is a homopentamericplasma protein of 25kDa subunits. It binds to the amyloid fibrils ofmisfolded proteins, which cause amyloidosis in humans. SAP not only stabilizesamyloid fibrils but also
Pal, Mohinder
core   +1 more source

PACT - Prediction of amyloid cross-interaction by threading

Scientific Reports, 2023
Amyloid proteins are often associated with the onset of diseases, including Alzheimer’s, Parkinson’s and many others. However, there is a wide class of functional amyloids that are involved in physiological functions, e.g., formation of microbial ...
Jakub W. Wojciechowski, Witold Szczurek, Natalia Szulc, Monika Szefczyk, Malgorzata Kotulska   +4 more
doaj   +1 more source

Inflammatory components in human Alzheimer's disease and after active amyloid-β42 immunization

, 2013
Inflammatory processes are important in the pathogenesis of Alzheimer's disease and in response to amyloid-β immunotherapy. We investigated the expression of multiple inflammatory markers in the brains of 28 non-immunized patients with Alzheimer's ...
Cheaveau, M., Morgan, William, Cheaveau, Matthew, Boche, Delphine, Bharambe, V., Holmes, C., Love, S., Nicoll, James A R, Harris, Scott, Bharambe, Viraj, Neal, James W, Love, Seth, Nicoll, J.A.R., Zotova, E., Boche, D., Morgan, W., Neal, J.W., Holmes, Clive, Zotova, Elina   +18 more
core   +1 more source

Amyloid tracers detect multple binding sites in Alzheimer´s disease brain tissue. [PDF]

, 2013
Imaging fibrillar amyloid-β deposition in the human brain in vivo by positron emission tomography has improved our understanding of the time course of amyloid-β pathology in Alzheimer’s disease. The most widely used amyloid-β imaging tracer so far is 11C-
Nordberg, A,, Ni, Ruiqing, Marutle, Amelia, Gillberg, P-G, Marutle, A,, Bergfors, A, Nordberg, Agneta, Gillberg, Per-Göran, Bergfors, Assar, Ni, R,   +9 more
core   +1 more source

Bacterial functional amyloids: Order from disorder

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2019
The discovery of intrinsic disorderness in proteins and peptide regions has given a new and useful insight into the working of biological systems. Due to enormous plasticity and heterogeneity, intrinsically disordered proteins or regions in proteins can perform myriad of functions.
Neha, Jain, Matthew R, Chapman
openaire   +3 more sources

Amyloid-DNA Composites of Bacterial Biofilms Stimulate Autoimmunity [PDF]

Immunity, 2015
Research on the human microbiome has established that commensal and pathogenic bacteria can influence obesity, cancer, and autoimmunity through mechanisms mostly unknown. We found that a component of bacterial biofilms, the amyloid protein curli, irreversibly formed fibers with bacterial DNA during biofilm formation.
Gallo, Paul M., Rapsinski, Glenn J., Wilson, R. Paul, Oppong, Gertrude O., Sriram, Uma, Goulian, Mark, Buttaro, Bettina, Caricchio, Roberto, Gallucci, Stefania, Tükel, Çagla   +9 more
openaire   +2 more sources

Adenosine triphosphate as a modulator of protein interactions and stability

FEBS Open Bio, EarlyView.
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley   +1 more source

Time‐Resolved Multidimensional NMR Spectroscopy Reveals the Bifurcated Folding Pathway of a Thrombin‐Binding DNA G4–Azobenzene Derivative Complex

Angewandte Chemie, EarlyView.
A photoswitchable ligand was used to trigger conformational changes within the thrombin binding aptamer DNA G‐Quadruplex. These reversible ligand driven rearrangements were examined by time‐resolved NMR experiments to gain insight of the dynamic folding landscape of the G‐quadruplex.
Jason Martins, Julia Wirmer‐Bartoschek, Harald Schwalbe   +2 more
wiley   +2 more sources