Results 21 to 30 of about 70,257 (224)

Seed-Induced Heterogeneous Cross-Seeding Self-Assembly of Human and Rat Islet Polypeptides. [PDF]

ACS Omega, 2017
Amyloid peptides can misfold and aggregate into amyloid oligomers and fibrils containing conformationally similar β-sheet structures, which are linked to the pathological hallmark of many neurodegenerative diseases. These β-sheet-rich amyloid aggregates provide common structural motifs to accelerate amyloid formation by acting as seeds. However, little
Hu R, Ren B, Zhang M, Chen H, Liu Y, Liu L, Gong X, Jiang B, Ma J, Zheng J.   +9 more
europepmc   +4 more sources

Cross-seeding Controls Aβ Fibril Populations and Resulting Function [PDF]

The Journal of Physical Chemistry B, 2021
AbstractAmyloid peptides nucleate from monomers to aggregate into fibrils through primary nucleation; pre-existing fibrils can then act as seeds for additional monomers to fibrillize through secondary nucleation. Both nucleation processes can occur simultaneously, yielding a distribution of fibril polymorphs that can generate a spectrum of ...
Michael J. Lucas, Henry S. Pan, Eric J. Verbeke, Gina M. Partipilo, Ethan C. Helfman, Leah Kann, Benjamin K. Keitz, David W. Taylor, Lauren J. Webb   +8 more
openaire   +2 more sources

Linking Alzheimer’s Disease and Type 2 Diabetes: Characterization and Inhibition of Cytotoxic Aβ and IAPP Hetero-Aggregates

Frontiers in Molecular Biosciences, 2022
The cytotoxic self-aggregation of β-amyloid (Aβ) peptide and islet amyloid polypeptide (IAPP) is implicated in the pathogenesis of Alzheimer’s disease (AD) and Type 2 diabetes (T2D), respectively. Increasing evidence, particularly the co-deposition of Aβ
Kenana Al Adem, Aya Shanti, Amit Srivastava, Dirar Homouz, Dirar Homouz, Dirar Homouz, Sneha Ann Thomas, Mostafa Khair, Cesare Stefanini, Vincent Chan, Tae-Yeon Kim, Sungmun Lee, Sungmun Lee   +12 more
doaj   +1 more source

Cross-seeding by prion protein inactivates TDP-43

Brain, 2023
Abstract A common pathological denominator of various neurodegenerative diseases is the accumulation of protein aggregates. Neurotoxic effects are caused by a loss of the physiological activity of the aggregating protein and/or a gain of toxic function of the misfolded protein conformers.
Stella A Polido, Cristiana Stuani, Aaron Voigt, Papiya Banik, Janine Kamps, Verian Bader, Prerna Grover, Laura J Krause, Inga Zerr, Jakob Matschke, Markus Glatzel, Konstanze F Winklhofer, Emanuele Buratti, Jörg Tatzelt   +13 more
openaire   +3 more sources

“To Cross-Seed or Not To Cross-Seed”: A Pilot Study Using Metallo-β-lactamases [PDF]

Crystal Growth & Design, 2017
Knowledge of protein structures is of central importance in modern drug discovery and molecular biology, but to be useful the structures, including those obtained in the crystalline state, must be biologically relevant. Small variations in crystallization conditions can lead to alternative crystal forms, conformations, and oligomerization states ...
Areej Abuhammad, Michael A. McDonough, Jürgen Brem, Anne Makena, Steven Johnson, Christopher J. Schofield, Elspeth F. Garman   +6 more
openaire   +2 more sources

Studies on alpha-synuclein and islet amyloid polypeptide interaction

Frontiers in Molecular Biosciences, 2023
Introduction: Parkinson’s disease and type 2 diabetes have both elements of local amyloid depositions in their pathogenesis. In Parkinson’s disease, alpha-synuclein (aSyn) forms insoluble Lewy bodies and Lewy neurites in brain neurons, and in type 2 ...
Ye Wang, Joakim Bergström, Martin Ingelsson, Martin Ingelsson, Martin Ingelsson, Gunilla T. Westermark   +5 more
doaj   +1 more source

Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences [PDF]

PeerJ, 2013
Fragments of prostatic acid phosphatase (PAP248-286) in human semen dramatically increase HIV infection efficiency by increasing virus adhesion to target cells.
Kevin Hartman, Jeffrey R. Brender, Kazuaki Monde, Akira Ono, Margery L. Evans, Nataliya Popovych, Matthew R. Chapman, Ayyalusamy Ramamoorthy   +7 more
doaj   +2 more sources

Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids

eLife, 2022
Synergistic-aggregation and cross-seeding by two different proteins/peptides in the amyloid aggregation are well evident in various neurological disorders including Alzheimer’s disease.
Debdeep Chatterjee, Reeba S Jacob, Soumik Ray, Ambuja Navalkar, Namrata Singh, Shinjinee Sengupta, Laxmikant Gadhe, Pradeep Kadu, Debalina Datta, Ajoy Paul, Sakunthala Arunima, Surabhi Mehra, Chinmai Pindi, Santosh Kumar, Praful Singru, Sanjib Senapati, Samir K Maji   +16 more
doaj   +1 more source

Promiscuous Cross-seeding between Bacterial Amyloids Promotes Interspecies Biofilms [PDF]

Journal of Biological Chemistry, 2012
Amyloids are highly aggregated proteinaceous fibers historically associated with neurodegenerative conditions including Alzheimers, Parkinsons, and prion-based encephalopathies. Polymerization of amyloidogenic proteins into ordered fibers can be accelerated by preformed amyloid aggregates derived from the same protein in a process called seeding ...
Yizhou, Zhou, Daniel, Smith, Bryan J, Leong, Kristoffer, Brännström, Fredrik, Almqvist, Matthew R, Chapman   +5 more
openaire   +2 more sources

Model-based inference of metastatic seeding rates in de novo metastatic breast cancer reveals the impact of secondary seeding and molecular subtype

Scientific Reports, 2022
We present a stochastic network model of metastasis spread for de novo metastatic breast cancer, composed of tumor to metastasis (primary seeding) and metastasis to metastasis spread (secondary seeding), parameterized using the SEER (Surveillance ...
Noemi Vitos, Philip Gerlee
doaj   +1 more source