Methods aggregation and structural protein aggregation amyloid. Medical search. Frequent questions

Dissociation of the TTR tetramer is believed to be the rate-limiting step in the amyloid fibril formation cascade. (go.jp)
Protein aggregation and amyloid fibril formation prediction software from primary sequence: towards controlling the formation of bacterial inclusion bodies. (uoa.gr)
The remarkably efficient suppression of amyloid fibril formation by the DNAJB6 chaperone is dependent on a set of conserved S/T-residues and an oligomeric structure, features unusual among DNAJ chaperones. (lu.se)
Our results demonstrate that PQQ inhibits the amyloid fibril formation and cytotoxicity of the C-truncated alpha-synuclein variants. (biomedcentral.com)
Moreover, the C-terminal region regulates the amyloid aggregation and fibril formation of α-Syn. (biomedcentral.com)
Although many truncated variants have been characterized, some of the truncated α-Syn variants which exist in both the normal and the pathogenic brain, such as α-Syn119 and α-Syn133, have not yet been investigated through in vitro aggregation and fibril formation studies. (biomedcentral.com)
2018. Structural mechanisms of oligomer and amyloid fibril formation by the prion protein. . (ncbs.res.in)
2017. The G126V Mutation in the Mouse Prion Protein Hinders Nucleation-Dependent Fibril Formation by Slowing Initial Fibril Growth and by Increasing the Critical Concentration. . (ncbs.res.in)
Effect of environmental conditions on aggregation and fibril formation of barstar. (mdc-berlin.de)
This is important, not just for understanding amylin - but for understanding many amyloid diseases in which run-away fibril formation occurs. (leeds.ac.uk)

Alzheimer's disease (AD) is a progressive neurodegenerative disease characterized by extracellular deposition of Aβ peptides in senile plaques and intracellular accumulation of hyperphosphorylated τ protein in neuronal cells as neurofibrillary tangles. (springer.com)
Potentially toxic Aβ peptides are generated from the copper-binding amyloid precursor protein (APP) by two independent proteolytic events (Bayer et al. (springer.com)
The following study aimed to clarify the effects of β-lactam antibiotics to the cholinergic system, on acetylcholinesterase (AChE), butyrylcholinesterase (BuChE) activities, considering the structural differences of antibiotics, to evaluate the underlying mechanism of effects provided by protein-antibiotic interactions, and to clarify possible effects of the antibiotics on the aggregation of Aβ-peptides. (dntb.gov.ua)
We demonstrate the effectiveness of this approach by identifying drug-like, head-to-tail cyclic peptides that modulate the aggregation of the Alzheimer's disease-associated amyloid β peptide. (nature.com)
Starting from raw materials, we develop and maintain novel synthetic processes including chemical vapor deposition (e.g. graphene), sputter-deposition techniques (e.g. complex magnetic and non-magnetic multi-layer system), particles synthesis (e.g. magnetic particles), surfaces functionalization (e.g.: thiolation, silaniza-tion, peptides and protein grafting) as well as exfoliation and stacking techniques (e.g.. hBN and other 2D ma-terials). (empa.ch)
The structure of the oligomer with the S/T-rich region is a large step forward in the understanding of the function of DNAJB6 and how it can bind aggregation-prone peptides and prevent amyloid diseases. (lu.se)
Protein aggregation can be described as the fibrilization or formation of insoluble structures from completely or partially unfolded peptides [2] . (wikibooks.org)
The protease not only releases small peptides, such as the amyloid-β peptide, which drives Alzheimer's disease pathogenesis, but also intracellular domains, which can have critical functions in nuclear signaling. (cipsm.de)
The reason why Peter Lansbury and others used the term 'natively unfolded' for a-synuclein and other proteins, especially peptides, is that they do not exist, to a significant degree, in the same kind of stable structure that larger native proteins like myoglobin do. (alzforum.org)
Polymorphisms that slightly vary native peptides or inflammatory processes set the stage for abnormal protein folding and amyloid fibril deposition. (medscape.com)

Destabilization effects of them on amyloid peptide fibrillation were examined and protein-ligand interactions were evaluated with most potent antibiotics by molecular docking studies. (dntb.gov.ua)
Biochemical, biophysical and biological assays using isolated amyloid β peptide, primary neurons and various established Alzheimer's disease nematode models showed that the selected macrocycles potently inhibit the formation of neurotoxic amyloid β peptide aggregates. (nature.com)
The silkmoth eggshell as a natural amyloid shield for the safe development of insect oocyte and embryo: Insights from studies of silkmoth chorion protein peptide-analogues of the B family. (uoa.gr)
A peptide can bind to itself or to other proteins in the cell in an unnatural way. (wikibooks.org)
APOE binds to cell-surface receptors to deliver lipids and to the hydrophobic amyloid-β peptide, regulating amyloid-β aggregations and clearances in the brain. (dovepress.com)
Arguelles J, Lee J, Cardenas LV, Govind S, Singh S. In Silico Analysis of a Drosophila Parasitoid Venom Peptide Reveals Prevalence of the Cation-Polar-Cation Clip Motif in Knottin Proteins. (cuny.edu)
See also David Thirumalai's Emerging Ideas on the Molecular Basis of Protein and Peptide Aggregation ' (.pdf). (alzforum.org)
This small peptide hormone can aggregate or clump together to form amyloid fibrils (a fibre-like structure). (leeds.ac.uk)
the other is the peptide chain which formed the natural structure of protein through the folding process to obtain biological activity and express life information [ 2 ]. (ijpsonline.com)
Aim: the effect of liposomes bi-functionalized with phosphatidic acid and with a synthetic peptide derived from human apolipoprotein e has been evaluated on the aggregation features of different amyloidogenic proteins: human amyloid β1-40 (aβ1-40), transthyretin (ttR) variant s52P, human β2microglobulin (β2m) variants ΔN6 and D76N, serum amyloid a (saa). (unimi.it)
computed structural analysis of protein fibrillar aggregates and considerations on the multidentate features of liposomes allow to speculate a common mechanism of action, based on binding the β-stranded peptide regions responsible for the amyloid formation. (unimi.it)

A number of human neurodegenerative diseases, including Alzheimer"s and Parkinson"s diseases (PD), are associated with the deposition of proteinaceous aggregates known as amyloid fibrils. (uni-goettingen.de)
Alpha-synuclein is found in healthy cells in the nervous system, but problems arise when it clumps together, or aggregates, into plaques known as amyloid that can disrupt normal function. (leeds.ac.uk)
When the control regions were deleted in the worms, alpha-synuclein no longer formed aggregates, and the worms were healthier and more mobile, even in old age, compared to worms expressing the normal alpha-synuclein protein. (leeds.ac.uk)
To this end, we investigate both protein aggregates at buffered aqueous solution-solid interfaces and in body fluids (blood and cerebrospinal fluid) from individuals at various stages of decline in memory and cognition through a col-laborative project with Kantonal Hospital St. Gallen. (empa.ch)
The onset of AD is nearly 20 years before symptoms such as confusion in time and place becomes visible (b) Summary of research results in profiling protein aggregates on red blood cells confirmed that the size, shape, morphology and prevalence of protein aggregates on RBCs varied depending on age and level of cognitive decline in individuals. (empa.ch)
Using a combination of experimental methods they show that a cytotoxic C-terminal truncated form of the alpha-synuclein protein that is abundant in vivo, aggregates into more strongly twisted fibrils that are more exposed to water. (uva.nl)
We demonstrated that the native fold is destabilized upon serine phosphorylation, and the resultant highly dynamic structures form amyloid-like ordered aggregates with high intermolecular β-structure content. (elte.hu)
In neurodegenerative diseases and amyloidoses, specific proteins self-assemble into amyloid fibrils and accumulate as pathological solid aggregates in a variety of tissues. (microrna.pro)
2019. Mechanistic approaches to understand the prion-like propagation of aggregates of the human tau protein. . (ncbs.res.in)
EPFL scientists have developed ClearTau, an innovative method and platform for reconstructing aggregates of the protein Tau found in Alzheimer's disease and other neurodegenerative diseases. (fitnessbossflorida.com)
ClearTau fibrils are morphologically consistent within single Tau isoforms and show key properties that make them similar to their natural counterparts, such as being positive to amyloid reporter dye, a high propensity for binding RNA, and seeding competency-the ability of ClearTau aggregates to induce the aggregation of other Tau proteins in neurons, a "domino effect" that gives rise to tauopathies. (fitnessbossflorida.com)
Therefore, there is an urgent need for methods that allow for reconstructing the biochemical and structural complexity of the disease-associated Tau pathological aggregates. (fitnessbossflorida.com)
Lashuel adds, "By combining the ClearTau method with other technologies that our lab has pioneered over the years, and being able to decorate Tau molecules with chemical modifications similar to those found in disease, we now have a powerful platform that enables us for the first time to screen for and identify conditions that produce Tau aggregates that are chemically and structurally similar to pathological brain-derived forms. (fitnessbossflorida.com)
We haven't done these measurements yet, but it should be possible to assess structural order in prefibrillar aggregates by doing solid-state NMR measurements, for example, on freeze-trapped solutions. (alzforum.org)
These aggregates are a hallmark of type 2 diabetes - although scientists do not yet know precisely how amyloid formation causes the disease. (leeds.ac.uk)
This could account for why the S20G-variant protein aggregates more quickly and is associated with more rapid onset of disease. (leeds.ac.uk)
Sheena Radford FRS, Astbury Professor of Biophysics and Director of the Astbury Centre and co-lead for the study, added, "We know that the S20G protein aggregates more quickly, and this study provides the rationale as to why that might be the case. (leeds.ac.uk)
Methods: the formation of fibrillar aggregates of the proteins was investigated by thioflavint fluorescence assay and validated by atomic Force Microscopy. (unimi.it)
liposomes also induce disaggregation of the amyloid aggregates of all the proteins investigated, with stronger effects on aβ1-40, β2 D76N and ttR. (unimi.it)

Using these methods, we previously showed that the N-terminal, non-amyloidogenic region of Aβ is involved in the network of interactions specifically stabilizing oligomers. (nature.com)
When coupled with ion mobility (IM-MS), the technique also allows the separation of signals from different structural variants of oligomers of the same order and measurement of their collisional cross section (Ω, Å 2 ). (nature.com)
We previously analyzed the IM-MS spectra of WT Aβ 1-40 and found that the population of oligomers of a given order (e.g. trimers, tetramers, pentamers, etc.) splits into two distinct structural variants, differing in their collisional cross section and, therefore, their structure 17 . (nature.com)
Here we aim to characterize pre-selected oligomers of polydisperse protein assemblies regarding their secondary, tertiary, and quaternary structure using a combination of MS, IM-MS and gas-phase spectroscopy techniques. (fu-berlin.de)
The purified protein is well folded and composed of oligomers with a varying number of subunits according to small-angle X-ray scattering (SAXS). (lu.se)
Toxic oligomers form at an early stage in the series of events that lead to Parkinson's Disease, which are believed to begin when alpha synuclein proteins malfunction and begin to stick together. (microrna.pro)
The claim that toxic oligomers form when alpha synuclein proteins malfunction and begin to stick together before their emergence exemplifies human idiocy. (microrna.pro)
Assembly of amyloid protofibrils via critical oligomers - A novel pathway of amyloid formation. (mdc-berlin.de)
The MRD method identifies coexisting oligomers from their rotational correlation times and determines their relative populations from the associated dispersion amplitudes. (lu.se)
Amyloid fibrils are made of normally soluble misfolded proteins that aggregate into oligomers and then insoluble fibrils. (msdmanuals.com)
However, some prefibrillar oligomers of amyloidogenic proteins have direct cellular toxicity, an important component of disease pathogenesis. (msdmanuals.com)

One major research focus is the role of protein misfolding in the onset of amyloidogenic diseases, including dialysis-related amyloidosis, Alzheimer's and Type II diabetes. (wikipedia.org)
her nomination reads: Sheena Radford is internationally distinguished for her seminal contributions to understanding how the dynamical properties of proteins enable them to fold and function biologically, or to misfold and cause degenerative diseases. (wikipedia.org)
They are also prone to aggregation, a phenomena which has been implicated for many diseases (the so-called misfolding and amyloid diseases). (berkeley.edu)
TTR misfolding and aggregation are associated with human amyloid diseases. (go.jp)
Investigator Professor Sheena Radford, FMedSci FRS, Director of the Astbury Centre for Structural Molecular Biology at the University of Leeds, said: "In trying to tackle diseases like Parkinson's, the first problem is identifying the key areas to target with small-molecules or protein-based medicines, as these proteins do not have a fixed structure, ruling out traditional methods of structure-based drug design. (leeds.ac.uk)
Protein misfolding and aggregation are common pathological features of several human diseases, including Alzheimer's disease and type 2 diabetes. (nature.com)
RBCs), and diagnosis (e.g.: protein aggregation diseases) and theranostics (magnetic particles for solid tumors treatment). (empa.ch)
Understanding the rules and distinguishing the differences between normal and aberrant protein aggregation is key to answering elemental questions from why we age to what triggers the early on-set of neurodegenerative diseases. (empa.ch)
Submicron-level structural alterations of amyloid proteins often occur prior to the onset of neurodegenerative diseases and before gross changes in the brain tissue can be detected with classical methods. (lu.se)
By elucidating the key structural aspects of the two fibrillar species, especially of the more cytotoxic 1-108-αS fibrils, the researchers hope to provide clues contributing to an understanding of molecular mechanisms underlying Parkinson's and other related amyloid diseases. (uva.nl)
Aggregation causes several serious diseases such as Alzheimer's and Type II Diabetes [1] . (wikibooks.org)
There are several diseases linked to protein aggregation. (wikibooks.org)
Amyloid fibrils are associated with a great variety of human diseases, including neurodegenerative conditions such as Parkinson's disease (PD). (chalmers.se)
Amyloid fibrils are associated with a number of human diseases, including Alzheimer's and Huntington's disease, Type II Diabetes Mellitus and prion diseases. (elte.hu)
Understanding the mutations in APOE, their structural properties, and their isoforms is important to determine its role in various diseases and to advance the development of therapeutic strategies. (dovepress.com)
Proteins do not self-assemble and quantized energy-dependent autophagy prevents "intrinsically" aggregation-prone proteins from causing all neurodegenerative diseases. (microrna.pro)
The formation of amyloid fibrils is also linked to other diseases including the neurodegenerative disorders Alzheimer's, Parkinson's and Huntingdon's Disease. (leeds.ac.uk)
Knowledge of amyloid structures such as those presented in this work may pave the way to better diagnosis and treatment of amyloid diseases by customised treatments dependent on the fibril type formed. (leeds.ac.uk)
Conclusion: thus, multifunctional liposomes perform as pharmacological chaperones with anti-amyloidogenic activity, with a promising potential for the treatment of a number of protein-misfolding diseases. (unimi.it)
[ 1 ] Many classic eponymic diseases were later found to be related to a diverse array of misfolded polypeptides (amyloid) that contain the common beta-pleated sheet architecture. (medscape.com)

The study focused on a protein called alpha-synuclein, which is linked to the onset and progression of Parkinson's disease. (leeds.ac.uk)
A short region of the alpha-synuclein protein, known as NAC, was assumed to be key to Parkinson's disease, as it is particularly aggregation-prone. (leeds.ac.uk)
In this study, researchers Dr Ciaran Doherty and PhD researcher Sabine Ulamec from the Astbury Centre at Leeds, found that two regions outside of NAC play a critical role in controlling amyloid formation of alpha-synuclein. (leeds.ac.uk)
They inserted alpha-synuclein and a variant of the protein lacking the master controller regions in to the muscle cells of nematode worms and monitored aggregation of the proteins and their effects on the mobility of the worms - a commonly used model organism in research into neurodegenerative disorders. (leeds.ac.uk)
To investigate whether the master controller regions identified in alpha-synuclein are also important for its function, the researchers looked at whether the modified protein could still fuse vesicles together. (leeds.ac.uk)
Using a combination of techniques, among which atomic force microscopy, UV-circular dichroism, X-ray diffraction and two-dimensional infrared spectroscopy, the researchers performed a structural analysis to explain the differences in the aggregation of wild-type alpha-synuclein (WT-αS) and the so-called C-terminal truncated form of the protein lacking 32 amino acids at the C-terminal end (1-108-αS). (uva.nl)
Although both of alpha-synuclein119 and alpha-synuclein133 showed a high cytotoxicity, alpha-synuclein133 showed a similar aggregation with full-length alpha-synuclein and no acceleration effect. (biomedcentral.com)

In 2016, Radford received an Investigator Award in Science for Protein-protein interactions in the early stages of amyloid assembly mechanisms. (wikipedia.org)
She has used sophisticated experimental techniques to characterise protein folding pathways in exquisite detail, in particular demonstrating that non-native as well as native-like interactions can play key roles in stabilising partially folded intermediate states. (wikipedia.org)
1. Algorithm development for the prediction of protein structure, function and interactions from amino acid sequence as well as construction of relevant databases. (uoa.gr)
gpDB: a database of GPCRs, G-proteins, effectors and their interactions. (uoa.gr)
Unique features of the structural model of hard cuticle proteins: implications for chitin-protein interactions and cross-linking in cuticle. (uoa.gr)
A database of human GPCRs, G-proteins, Effectors and their interactions. (uoa.gr)
Reversible protein aggregation typically results from weaker protein interactions. (wikibooks.org)
Ultra-high field NMR is the only method available to study the physical properties and interactions of IDPs. (bruker.com)
Novel GHz-class NMR technology enables advanced research into the structural basis for affinity and specificity of protein-ligand interactions, including a better understanding of structural features of cell membrane proteins, and the molecular mechanisms involved in protein folding and aggregation. (bruker.com)
Destabilization of polar interactions in the prion protein triggers misfolding and oligomerization. (ncbs.res.in)
2018. Mechanism of aggregation and membrane interactions of mammalian prion protein. . (ncbs.res.in)
2017. A Dry Transition State More Compact Than the Native State Is Stabilized by Non-Native Interactions during the Unfolding of a Small Protein. . (ncbs.res.in)
Despite the fact that the molecular aspects responsible for amyloid pathologies have not been deciphered, interactions of misfolded proteins with cell membranes appear to play essential roles in these disorders. (jnkinhibitor.com)
Fluoroalcohol-induced structural changes of proteins: some aspects of cosolvent-protein interactions. (mdc-berlin.de)
Protein conformation is critically linked to function and often controlled by interactions with regulatory factors. (cipsm.de)
Specifically, aggregation was found to be associated with increased cell fitness in the case of TDP-43 mutations, as it protects the host from aberrant interactions. (frontiersin.org)
Any situation, such as mutations or anomalous expression, could result in disruption of these beneficial interactions with consequent aggregation and depletion of normal function. (frontiersin.org)
Native or wild-type quaternary protein structure is usually born from a single translated protein sequence with one ordered conformation with downstream protein interactions. (medscape.com)

The targeted applications are in biochemical sensing (e.g.: biomarkers, proteins), imaging & spectroscopy (e.g. (empa.ch)
Using the PD protein a-synuclein (a-syn) as model, this project aims to explore the molecular origin and magnitude of the stability of amyloid fibrils and to relate this to their biological activities.Fibril stability will be explored from a thermodynamic viewpoint using chemical denaturants and biochemical methods. (chalmers.se)
the amyloidogenic protein is typed using a variety of immunohistologic and biochemical techniques. (msdmanuals.com)

Gurry T., Stu ltz CM. Intrinsically Disordered Proteins: Where Computation Meets Experiment. (mit.edu)
in Intrinsically Disordered Proteins . (mit.edu)
Stultz CM. Constructing Ensembles for Intrinsically Disordered Proteins. (mit.edu)
Huang A., Stultz CM. Modeling Intrinsically Disordered Proteins with Bayesian Statistics. (mit.edu)
Bruker's GHz-class NMR technology enables novel research in functional structural biology of proteins and protein complexes like intrinsically disordered proteins (IDPs). (bruker.com)
An intrinsically disordered protein (IDP) is a protein that is unable to fold into a stable or ordered three-dimensional structure. (bruker.com)
The biological importance of intrinsically disordered proteins (IDPs) has been discovered in recent years by sequence-specific assignments using NMR. (bruker.com)
2021. Microsecond dynamics during the binding-induced folding of an intrinsically disordered protein. . (ncbs.res.in)
Are there temperature-dependent structural transitions in the "intrinsically unstructured" protein prothymosin α? (mdc-berlin.de)

[ 4 ] In humans, about 23 different unrelated proteins are known to form amyloid fibrils in vivo. (medscape.com)

These proteins undergo a spontaneous transition from a soluble, often partially folded form into an insoluble, beta-sheet rich amyloid fibril. (fu-berlin.de)
An impediment to the successful production of large quantities of natively folded proteins in Escherichia coli is the tendency of many proteins to become insoluble when overexpressed. (iucr.org)
There is extensive literature on the variables leading to insoluble recombinant expression of proteins. (iucr.org)
Amyloidosis is a clinical disorder caused by extracellular and/or intracellular deposition of insoluble abnormal amyloid fibrils that alter the normal function of tissues. (medscape.com)
Amyloidosis is any of a group of disparate conditions characterized by extracellular deposition of insoluble fibrils composed of misaggregated proteins. (msdmanuals.com)
Amyloid deposits are composed of small (about 10 nm diameter), insoluble fibrils that form congophilic beta-pleated sheets that can be identified by x-ray diffraction. (msdmanuals.com)

Intrinsic Aggregation Propensity of the CsgB Nucleator Protein is Crucial for Curli Fiber Formation. (uoa.gr)
AMYLPRED 2: A Consensus Method for Amyloid Propensity Prediction. (uoa.gr)
Several in vitro studies have shown the propensity of α-Syn to aggregate into amyloid fibrils, a process that is accelerated by the truncation of its C-terminal. (biomedcentral.com)
This structural arrangement could lead to a greater propensity for aggregation. (leeds.ac.uk)

Zusätzlich können die Phosphorylierungnachahmer (S129E und S129D) den Effekt von Phosphorylierung auf die strukturellen und Aggregations-Eigenschaften von S in vitro nicht reproduzieren. (uni-goettingen.de)
Zn(2+) enhances TTR aggregation in vitro, and is a component of ex vivo TTR amyloid fibrils. (rcsb.org)

All types of amyloid consist of one major fibrillar protein that defines the type of amyloid. (medscape.com)
In addition to the fibrillar amyloid protein, the deposits also contain serum amyloid P component and glycosaminoglycans. (msdmanuals.com)

Here, we focus on decoding the aggregation pathways of proteins impli-cated in the pathology of Alzheimer's disease using liquid-based scanning probe microscopy, chemical spec-troscopy and machine learning-based data analysis for protein classification in body fluids. (empa.ch)
The long-term research goal of the lab is to apply computer modeling to gain insight into cellular signal transduction pathways, specifically to provide deeper insight into both the normal and aberrant subcellular targeting of domains contained in proteins which are part of macromolecular complexes and function in various biological processes. (cuny.edu)
2022. Differentiating between the sequence of structural events on alternative pathways of folding of a heterodimeric protein. . (ncbs.res.in)
2021. Mapping Distinct Sequences of Structure Formation Differentiating Multiple Folding Pathways of a Small Protein. . (ncbs.res.in)
The pathways related to cell protein folding and degradation need to be elucidated because of training was set. (ijpsonline.com)
Many mechanisms of protein function contribute to amyloidogenesis, including "nonphysiologic proteolysis, defective or absent physiologic proteolysis, mutations involving changes in thermodynamic or kinetic properties, and pathways that are yet to be defined. (medscape.com)

In addition to the native conformation, a protein sequence populates small fluctuations around the native state, partially unfolded forms and even the globally unfolded conformation. (berkeley.edu)
2017. Identification and structural characterization of the precursor conformation of the prion protein which directly initiates misfolding and oligomerization. . (ncbs.res.in)
[4] Computational techniques such as molecular dynamics simulations can be used in conjunction with empirical structure determination strategies to extend and study protein structure, conformation and function. (cloudfront.net)
Here we report the selection of camelid-derived single-domain antibodies (nanobodies) that modulate the conformation and spectral properties of the green fluorescent protein (GFP). (cipsm.de)

A second research focus is on the folding of outer membrane proteins of Gram-negative organisms. (wikipedia.org)
Proteins in this outer membrane facilitate transport with the outside world. (wikipedia.org)
By studying them, we can discover some of the essential features that enable transmembrane beta-barrel proteins to fold into a membrane. (wikipedia.org)
Human dystrophin structural changes upon binding to anionic membrane lipid. (cea.fr)
Dos Santos Morais R, Delalande O, Pérez J, Mouret L, Bondon A, Martel A, Appavou MS, Le Rumeur E, Hubert JF, Combet S. Contrast-matched isotropic bicelles: a versatile tool to specifically probe the solution structure of peripheral membrane proteins using SANS. (cea.fr)
OMPdb: A database of ß-barrel outer membrane proteins from Gram negative bacteria. (uoa.gr)
Evaluation of methods for predicting the topology of β-barrel outer membrane proteins and a consensus prediction method. (uoa.gr)
Prediction of Membrane lipid-Binding Proteins. (uoa.gr)
A database of Molecular Recognition Features in Membrane Proteins. (uoa.gr)
The trimeric Sec61/SecY complex is a protein-conducting channel (PCC) for secretory and membrane proteins. (cipsm.de)

2022. α-Synuclein aggregation intermediates form fibril polymorphs with distinct prion-like properties. . (ncbs.res.in)

This has been done with the use of native mass spectrometry, NMR and single molecule methods to characterize intermediates of protein folding and in amyloid formation. (wikipedia.org)
Our use of different hydrogen exchange methods to study three different types of intermediates of E. coli ribonuclease H (the acid molten globule, the higher energy conformations of the native state and a kinetic folding intermediate) has been particularly powerful. (berkeley.edu)
Our studies on the mechanism of folding include investigating the role of topological complexity using permuted proteins, the nature and function of folding intermediates, and studies on the role of mechanical unfolding using single molecule measurements. (berkeley.edu)
Whereas there is increasing knowledge about the factors that drive aggregation, the structural characteristics of intermediates and the molecular details that determine the arrangement of misfolded prote! (uni-goettingen.de)
Folding of firefly (photinus pyralis) luciferase: aggregation and reactivation of unfolding intermediates. (mdc-berlin.de)

Sheena Elizabeth Radford OBE FRS FMedSci is a British biophysicist, and Astbury Professor of Biophysics in the Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology at the University of Leeds. (wikipedia.org)
and �Astbury Centre for Structural RGS19 Inhibitor Synonyms Molecular Biology and College of Molecular and Cellular Biology, University of Leeds, Leeds, United KingdomABSTRACT Amyloid fibril accumulation is a pathological hallmark of various devastating problems, which includes Alzheimer's disease, prion illnesses, variety II diabetes, and other folks. (jnkinhibitor.com)

In 2021, an advance in biomolecular design was the creation of new proteins that were shown in the lab to spontaneously fold into their intended structures and embed into lipid membranes as reported in Science with lead author Anastassia Vorobieva. (wikipedia.org)
2021. The Lys 280 ➔ Gln mutation mimicking disease-linked acetylation of Lys 280 in tau extends the structural core of fibrils and modulates their catalytic properties. . (ncbs.res.in)
2021. Structural Characterization of the Cooperativity of Unfolding of a Heterodimeric Protein Using Hydrogen Exchange-Mass Spectrometry. . (ncbs.res.in)

The electron microscopes are housed within the Astbury Biostructure Laboratory , a major international research centre for structural biology established in 2016 with funding from the University of Leeds and the Wellcome Trust. (leeds.ac.uk)

Researchers from Amsterdam and Enschede have for the first time performed a structural comparison of two types of amyloid fibrils that have been associated with Parkinson's disease. (uva.nl)

Detailed knowledge of the structural features that are potentially important for oligomer-mediated neurotoxicity is a prerequisite for the rational design of oligomerization modifiers. (nature.com)
Instead of adopting one defined oligomerization state, some proteins exist as equilibrium of several distinctly sized species. (fu-berlin.de)
Methylene blue inhibits amyloid Aβ oligomerization by promoting fibrillization. (nature.com)

Alzheimer disease (AD) is biologically defined by the presence of β-amyloid-containing plaques and tau-containing neurofibrillary tangles. (medscape.com)
Pathologic hallmarks of the disease include beta-amyloid (Aβ) plaques, neurofibrillary tangles (NFTs), and reactive gliosis. (medscape.com)
Alzheimer Disease Alzheimer disease causes progressive cognitive deterioration and is characterized by beta-amyloid deposits and neurofibrillary tangles in the cerebral cortex and subcortical gray matter. (msdmanuals.com)

A number of normal (wild-type) and mutant proteins are susceptible to such misfolding and aggregation (amyloidogenic proteins), thus accounting for the wide variety of causes and types of amyloidosis. (msdmanuals.com)
For amyloidosis to develop, in addition to production of amyloidogenic proteins, there is probably also a failure of the normal clearance mechanisms for such misfolded proteins. (msdmanuals.com)
In systemic amyloidosis, circulating amyloidogenic proteins form deposits in a variety of organs. (msdmanuals.com)

Surprisingly, proteins with very different amino acid sequences and three-dimensional structures aggregate into amyloid fibrils that share common characteristics, such as a similar morphology and a specific beta-sheet-based molecular architecture. (uni-goettingen.de)
Limorenko and Lashuel thought that they could use immobilized heparin or other co-factors known to induce Tau aggregation to nudge the protein to change its shape and aggregate. (fitnessbossflorida.com)

The most relevant example of polydisperse systems are probably amyloid forming proteins occurring in neurodegenerative disorders such as Alzheimer's and Parkinson's disease. (fu-berlin.de)
A master control region of a protein linked to Parkinson's disease has been identified for the first time. (leeds.ac.uk)
One example of what can be observed in living brain tissue is the formation of beta-sheet structures, characteristic of amyloid proteins involved in Alzheimer's and Parkinson's. (lu.se)
Oligomeric species populated during the aggregation process of α-synuclein have been linked to neuronal impairment in Parkinson's disease and related neurodegenerative disorders. (microrna.pro)

When we're taught biochemistry, we see proteins in their physiologically active forms. (alzforum.org)

We have found that although protein stability can be altered by single amino acid substitution, evolution for optimal function requires more subtle and delocalized mechanisms.Recent results implicate structure in the unfolded state as playing an important and novel role for the thermostability of these proteins. (berkeley.edu)
In order to reveal the molecular mechanisms underlying pH sensitivity and structural stabilities of TTR, neutron diffraction studies were conducted using the IBARAKI Biological Crystal Diffractometer with the time-of-flight method. (go.jp)
Methods The inhibition/activation mechanisms for each antibiotic were examined kinetically by Ellman method. (dntb.gov.ua)
Whilst much is known about the kinetics and mechanisms by which amyloid fibrils form, less attention has been paid to their stabilities and modes of disintegration. (chalmers.se)
Using mutational analysis and published structural data, we will define stability hotspots within the a-syn sequences, arguing how these could be important targets for future stability-modifying therapies.We will also develop a nanofluidic method to study the rates and mechanisms of depolymerization of individual fibrils in solution, exploring the concept of fibril polymorphism. (chalmers.se)
Polymerization of proteins into amyloid protofibrils shares common critical oligomeric states but differs in the mechanisms of their formation. (mdc-berlin.de)

2009. Pyrano[3,2-c]quinoline-6-chlorotacrine hybrids as a novel family of acetylcholinesterase- and beta-amyloid-directed anti-Alzheimer compounds . (ub.edu)

Proteins from thermophilic organisms must retain their native structures under extreme conditions, where their homologues from mesophilic organisms denature. (berkeley.edu)
With OPTIR, we can follow the formation of structures that precede the aggregation of amyloid proteins directly in the living tissue. (lu.se)
Early structural biologists throughout the 19th and early 20th centuries were primarily only able to study structures to the limit of the naked eye's visual acuity and through magnifying glasses and light microscopes. (cloudfront.net)
Through the discovery of X-rays and its applications to protein crystals, structural biology was revolutionized, as now scientists could obtain the three-dimensional structures of biological molecules in atomic detail. (cloudfront.net)
[9] During this time, modeling of protein structures was done using balsa wood or wire models. (cloudfront.net)

2017. Chemical Denaturants Smoothen Ruggedness on the Free Energy Landscape of Protein Folding. . (ncbs.res.in)
2017. Expression and purification of single cysteine-containing mutant variants of the mouse prion protein by oxidative refolding. . (ncbs.res.in)
2017. Modulation of the Extent of Cooperative Structural Change During Protein Folding by Chemical Denaturant. . (ncbs.res.in)

In cell culture systems, Cu supplementation was found to stimulate the non-amyloidogenic APP pathway thereby suppressing the formation of β amyloid (Borchardt et al. (springer.com)
A combined computational strategy of sequence and structural analysis predicts the existence of a functional eicosanoid pathway in Drosophila melanogaster. (cuny.edu)
Chaperonin Containing Tailless Complex Polypeptide 1 (CCT-1) is one of the important elements of protein folding pathway in cells and proteasome is an important component of Adenosine Triphosphate (ATP) dependent protein degradation pathway in cells. (ijpsonline.com)
They are involved in the formation of protein folding/degradation signalling pathway, maintaining the normal spatial structure and normal biological function of protein [ 3 ]. (ijpsonline.com)

She became the Deputy Director of the Astbury Centre for Structural Molecular Biology in 2009 then Director in 2012. (wikipedia.org)
Her nomination reads: Sheena Radford is Professor of Structural Molecular Biology at the University of Leeds. (wikipedia.org)
This feature is already widely utilized for the analysis of complex mixtures in proteomics and metabolomics and has recently been shown to be also of exceptional use for structural biology. (fu-berlin.de)
Coherent neutron scattering provides structural information in addition to, or instead of, the more classical structural methods used in structural biology (XR-crystallography, NMR, cryo-electron microscopy) in challenging situations such as protein assemblies or proteins in complex environments. (cea.fr)
The finding, made by scientists from the University of Leeds' Astbury Centre for Structural Molecular Biology , provides a new target for the development of therapies to try and slow down or even prevent the disease. (leeds.ac.uk)
Their findings are published today in Nature Structural and Molecular Biology . (leeds.ac.uk)
The Biophysics and Bioinformatics Laboratory of the Department of Cell Biology and Biophysics of the University of Athens focuses over the last three decades on research related to the elucidation of the principles governing protein structure and function, under the supervision of Associate Professor Vassiliki A. Iconomidou . (uoa.gr)
NMR has evolved into a powerful technique in structural biology for studying the dynamics of proteins, including IDPs. (bruker.com)
Bruker is helping shed light on functional-structural biology research with advanced NMR solutions. (bruker.com)
Structural biology is a field that is many centuries old which, as defined by the Journal of Structural Biology , deals with structural analysis of living material (formed, composed of, and/or maintained and refined by living cells) at every level of organization. (cloudfront.net)
Recent developments in the field have included the generation of X-ray free electron lasers , allowing analysis of the dynamics and motion of biological molecules, [12] and the use of structural biology in assisting synthetic biology . (cloudfront.net)
Currently, solid-state NMR is widely used in the field of structural biology to determine the structure and dynamic nature of proteins ( protein NMR ). (cloudfront.net)
In research published today in the journal Nature Structural and Molecular Biology, scientists at the University of Leeds report that they have been able to visualise the structure of amylin fibrils using the latest electron microscope technology. (leeds.ac.uk)
Neil Ranson, Professor of Structural Molecular Biology and Deputy Director of the Astbury Centre for Structural Molecular Biology at the University of Leeds, co-led the project. (leeds.ac.uk)

Methods Mol Biol. (mit.edu)
Scarpati M, Heavner ME, Wiech E, Singh S. Proteomic Tools for the Analysis of Cytoskeleton Proteins.Methods Mol Biol. (cuny.edu)

These data highlight structural and functional roles of Zn(2+) in TTR-related amyloidoses, as well as in holo-RBP recognition and vitamin A homeostasis. (rcsb.org)
These peculiar properties confer them completely different functional advantages, compared with proteins that have a well-defined 3D structure. (bruker.com)
Sphingolipids constitute a complex class of bioactive lipids with diverse structural and functional roles in neural tissue. (mdpi.com)
2009. Structural plasticity and functional implications of internal cavities in distal mutants of type 1 non-symbiotic hemoglobin AHb1 from Arabidopsis thaliana . (ub.edu)
Here we demonstrate that PSRP1 is not a bona fide ribosomal protein, but rather a functional homologue of the Escherichia coli cold-shock protein pY. (cipsm.de)
A variety of imaging modalities, including structural and functional magnetic resonance imaging (MRI) and positron emission tomography (PET) studies of cerebral metabolism, have shown characteristic changes in the brain of patients with Alzheimer disease in prodromal and even presymptomatic states. (medscape.com)
Mostajeran M, Wetterling F, W Blixt F, Edvinsson L, Ansar S. Acute mitogen-activated protein kinase 1/2 inhibition improves functional recovery and vascular changes after ischaemic stroke in rat-monitored by 9.4 T magnetic resonance imaging. (lu.se)

With a novel microspectroscopy approach combining optical and photothermal imaging, MultiPark researchers can follow early alterations of proteins involved in Alzheimer's disease, before neurons degenerate. (lu.se)
Apolipoprotein E (APOE) is a lipid-transport protein abundantly expressed in most neurons in the central nervous system. (dovepress.com)
α-Synuclein (140 aa) is a natively unfolded protein that is enriched in the presynaptic terminal of the neurons in the brain. (biomedcentral.com)

She has built on these findings to define key steps in the aberrant self-assembly of misfolded proteins into amyloid fibrils, particularly in dialysis related amyloidosis, and to relate these molecular processes to pathogenesis. (wikipedia.org)

These data indicate that this eukaryotic cell-free expression system has a high success rate and that the addition of specific reagents can increase the yield of soluble protein. (iucr.org)

Radford's research investigates protein folding, protein aggregation and amyloid disease. (wikipedia.org)
Her achievements have involved the innovative application of biophysical techniques to protein folding problems. (wikipedia.org)
Her early work in Oxford on hen lysozyme was the foundation for current views that proteins fold on complex multidimensional landscapes, commonly known as folding funnels. (wikipedia.org)
Understanding the sequence determinants of the energy landscape is therefore fundamental to the biological process that proteins carry out as well as protein folding itself. (berkeley.edu)
This hypothesis unites a lot of work in the field of and has also provided insight and experimental tests for current theoretical work on protein folding. (berkeley.edu)
Other projects in the lab focus on the mechanism of protein misfolding, the structural and energetic mechanism of signaling, computational identification of folding modules, and the role of ligand binding. (berkeley.edu)
In order for us to understand protein aggregation, we need to understand more about protein folding in general. (wikibooks.org)
Advances have been made in understanding the protein folding process. (wikibooks.org)
The general folding process of a protein can be described as a "stochastic search" for the native state [3] [7] . (wikibooks.org)
The 20 residue long Trp-cage miniprotein is a great model to complete both computational and experimental studies on protein folding and stability. (elte.hu)
We showed that Trp-cage miniprotein and its variants are indeed a realistic model of larger globular systems of composite folding and aggregation landscapes and helps us to understand the fundamentals of protein aggregation and amyloid formation. (elte.hu)
Imperiali B. Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation. (mit.edu)
2023. Replacement of the native cis prolines by alanine leads to simplification of the complex folding mechanism of a small globular protein. . (ncbs.res.in)
2022. Heterogeneity in Protein Folding and Unfolding Reactions. . (ncbs.res.in)
2022. Native State Hydrogen Exchange-Mass Spectrometry Methods to Probe Protein Folding and Unfolding. . (ncbs.res.in)
2019. Observation of Continuous Contraction and a Metastable Misfolded State during the Collapse and Folding of a Small Protein. . (ncbs.res.in)
2018. The Osmolyte TMAO Modulates Protein Folding Cooperativity by Altering Global Protein Stability. . (ncbs.res.in)
Time-resolved dynamic light scattering as a method to monitor compaction during protein folding. (mdc-berlin.de)
Protein Folding and Neurodegeneration: Biophysics to the Rescue? (alzforum.org)
This does not change our view of protein folding in the least. (alzforum.org)
The results showed that chaperonin containing tailless complex polypeptide the large number of proteins involved, the complex relationship between proteins and the lack of research on the effects of movement and cell protein folding and degradation. (ijpsonline.com)
As the expression vector of life information, the specific spatial structure formed by protein folding is the basis of its biological function. (ijpsonline.com)

Fig. 4: The selected cyclic pentapeptides AβC5-34 and AβC5-116 inhibit Aβ-induced aggregation and cytotoxicity in vivo. (nature.com)

Low pH is known to promote dissociation into monomer and the formation of amyloid fibrils. (go.jp)
Hexapeptide Tandem Repeats Dictate the Formation of Silkmoth Chorion, a Natural Protective Amyloid. (uoa.gr)
Disulfide bond formation of free thiols is a common mechanism for covalent aggregation. (wikibooks.org)
Oxidation of tyrosine residues can lead to formation of bityrosine which often results in aggregation. (wikibooks.org)
In addition, Trp-cage is suitable for modeling aggregation and amyloid formation. (elte.hu)
We characterized the amyloid formation of several sequence modified and side-chain phosphorylated Trp-cage variants. (elte.hu)
APOE is also involved in the formation of chylomicrons and VLDL and affects the activity of other lipid metabolism-associated proteins and enzymes, such as hepatic lipase and lipoprotein lipase. (dovepress.com)
Given the double valence of protein aggregation that can result either in the formation of toxic assemblies or physiologically required organelles, it has long been debated what could determine whether aggregation is beneficial or detrimental from an evolutionary perspective. (frontiersin.org)

Transthyretin (TTR) is a tetrameric protein. (go.jp)
Human transthyretin (TTR) is a homotetrameric protein involved in several amyloidoses. (rcsb.org)

The amyloidoses are referred to with a capital A (for amyloid) followed by an abbreviation for the fibril protein. (medscape.com)

In this study, we first characterized the aggregation and cytotoxicity of C-truncated alpha-synuclein119 and alpha-synuclein133 which have been found in both the normal and the pathogenic brain. (biomedcentral.com)
In spite of increasing proof for the involvement of membranes in amyloid-mediated cytotoxicity, the pursuit for therapeutic strategies has focused on stopping self-assembly from the proteins comprising the amyloid plaques. (jnkinhibitor.com)

Only 10% of amyloidosis deposits consist of components such as glycosaminoglycans (GAGs), apolipoprotein-E (apoE), and serum amyloid P-component (SAP), while nearly 90% of the deposits consist of amyloid fibrils that are formed by the aggregation of misfolded proteins. (medscape.com)

2 In the blood, APOE protein could interact with lipids, resulting in lipoproteins, including very-low-density lipoproteins (VLDL). (dovepress.com)
[2] [3] The cells within the biofilm produce the EPS components, which are typically a polymeric conglomeration of extracellular polysaccharides , proteins , lipids and DNA . (wikipedia.org)

This suggests that the ability to fibrillate is an intrinsic property of a polypeptide chain and that the native structure is not necessarily the only ordered structure that each protein can assume. (uni-goettingen.de)
The model (containing two strands of chiral amino acid residues) allows the possibility to form either a single or double inter- or intra-strand disulfide bridges and to assess the stability of β-strand foldamers as function of disulfide bridges and their oxidation states via a QM based description, heading to explain the intrinsic feature of polypeptide aggregation. (elte.hu)

2010. Structural determinants of the multifunctional profile of dual binding site acetylcholinesterase inhibitors as anti-Alzheimer agents . (ub.edu)
2009. High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases . (ub.edu)
2008. Structural determinants of ligand migration in Mycobacterium tuberculosis truncated hemoglobin O . Proteins. (ub.edu)
We have analyzed the interaction of Hep1 with mitochondrial Hsp70 (Ssc1) and the determinants in Ssc1 which make it prone to aggregation. (cipsm.de)

Therefore it allows for characterization of the structural properties of each form in separation. (nature.com)

To investigate the importance of these 'master controller' regions in protein aggregation in living cells, the team joined forces with Dr Patricija van Oosten Hawle and her students, also members of the Astbury Centre in Leeds. (leeds.ac.uk)

[8] The first tertiary protein structure , that of myoglobin , was published in 1958 by John Kendrew . (cloudfront.net)

Exploring the 'aggregation-prone' core of human Cystatin C: A structural study. (uoa.gr)

However, their structural properties remain elusive due to the dynamic and heterogeneous character of oligomeric species coexisting in solution. (nature.com)
When coupled with hydrogen deuterium exchange (HDX), in solution or gas phase, MS provides insight into the structural dynamics of different oligomeric forms. (nature.com)

[2] Finally, in the 21st century, electron microscopy also saw a drastic revolution with the development of more coherent electron sources, aberration correction for electron microscopes, and reconstruction software that enabled the successful implementation of high resolution cryo-electron microscopy, thereby permitting the study of individual proteins and molecular complexes in three-dimensions at angstrom resolution. (cloudfront.net)

2. Application of a variety of Biophysical methods and techniques for protein structure determination and for structural studies of complex, physiologically important, Biological tissues such as insect chorion and cuticle. (uoa.gr)
2009. Synthesis, structural analysis, and biological evaluation of thioxoquinazoline derivatives as phosphodiesterase 7 inhibitors . (ub.edu)
aggregation can be required in specific cases to increase the functionality of a biological system. (frontiersin.org)
Pharmaceutical research has successfully incorporated a wealth of molecular modeling methods, within a variety of drug discovery programs, to study complex biological and chemical systems. (mdpi.com)

Nevertheless, new approaches, mainly based on mass spectrometry, provide unique access to these different structural forms. (nature.com)

In 2020, a collaboration between scientists at the University of Leeds and AstraZeneca led to the development of a technique that, "allows fragments of antibodies to be screened for susceptibility to aggregation caused by structure disruption much earlier in the drug discovery process. (wikipedia.org)
These proteins share a similar nanoscale structure, a transmembrane beta-barrel, through which other molecules can pass. (wikipedia.org)
For instance, many proteins share the same native structure yet their cellular dynamics and function, in other words their energy landscapes, are different. (berkeley.edu)
Structural comparison with the X-ray crystal structure at acidic pH identified the three amino acid residues responsible for the pH sensitivity of TTR. (go.jp)
ins in amyloid fibrils are still only understood in outline.Here in Chapter 3, it is demonstrated, by a combination of solution-state and solid-state NMR spectroscopy, that the structure of amyloid fibrils of á-synuclein (aS) is directly correlated to the conformational properties of the unfolded state and monomeric state of misfolding proteins. (uni-goettingen.de)
Alternative methods of structure analysis that would provide experimental insight into each of the co-existing species and their dynamic nature need to be explored. (nature.com)
We explored the structure of DNAJB6 using a combination of structural methods. (lu.se)
Amyloid fibrils are primarily composed of beta sheets and the main chain dominates the protein's structure. (wikibooks.org)
Recombinant expression of proteins of interest in Escherichia coli is an important tool in the determination of protein structure. (iucr.org)
Burger V., Arenas D., Stultz CM. A Structure-free Method for Quantifying Conformational Flexibility in proteins. (mit.edu)
Burger V., Nolasco D., Stultz CM., Expanding the Range of Protein Function at the Far end of the Order-Structure Continuum. (mit.edu)
Linder D., Gurry T., Stultz CM. Towards a Consensus in Protein Structure Nomenclature. (mit.edu)
Stultz CM. Protein Structure along the order-disorder continuum. (mit.edu)
The increased spectral resolution and sensitivity of the 1.2 GHz NMR has already enabled research teams to look more deeply at proteins and better understand the initial steps of amyloid-type protein aggregation as well as the function and structure of the Tau protein, both commonly associated with Alzheimer's disease. (bruker.com)
Tau is a protein found in the human brain that plays an important role in maintaining the structure and function of nerve cells. (fitnessbossflorida.com)
[1] Likewise, NMR spectroscopy allowed information about protein structure and dynamics to be obtained. (cloudfront.net)
Conversion of yeast phosphoglycerate kinase into amyloid-like structure. (mdc-berlin.de)
Proteins: Structure, Function, and Bioinformatics 39 (3): 204-211. (mdc-berlin.de)
This would fundamentally change our conventional thinking about protein structure-function relationship, no? (alzforum.org)
I do not think there is a contradiction to the conventional thinking of protein structure-function relation. (alzforum.org)
S cientists have for the first time identified the structure of a protein fibre linked to early-onset type 2 diabetes. (leeds.ac.uk)
The image shows the structure of the amyloid fibrils in the wild-type amylin and also in the S20G variant. (leeds.ac.uk)
The amyloid deposits themselves are metabolically inert but interfere physically with organ structure and function. (msdmanuals.com)

An additional common property of aggregation into amyloid fibrils is the presence of partially or fully unfolded states of the misfolding proteins. (uni-goettingen.de)
2022. Evolutionarily conserved proline residues impede the misfolding of the mouse prion protein by destabilizing an aggregation-competent partially unfolded form . (ncbs.res.in)

Many companies are taking advantage of bioinformatics techniques to predict aggregation. (wikibooks.org)

Pepsin crystals were the first proteins to be crystallized for use in X-ray diffraction, by Theodore Svedberg who received the 1962 Nobel Prize in Chemistry. (cloudfront.net)

Fig. 2: The selected cyclic pentapeptides AβC5-34 and AβC5-116 interfere with the normal Aβ aggregation process. (nature.com)

Anatomy20

Organisms20

Diseases21

Chemicals and Drugs94

Analytical, Diagnostic and Therapeutic Techniques and Equipment38

Psychiatry and Psychology2

Phenomena and Processes66

Disciplines and Occupations3

Technology, Industry, Agriculture3

Information Science5

Health Care2

Fibril formation10

Peptides10

Peptide11

Aggregates19

Oligomers11

Diseases20

Alpha-synuclein7

Interactions18

Biochemical3

Intrinsically9

Form amyloid fibrils1

Insoluble6

Propensity4

Vitro2

Fibrillar2

Pathways6

Conformation4

Membrane10

Prion-like properties1

Intermediates5

Molecular and Cel2

20213

20161

Types of amyloid1

Oligomerization3

Neurofibrillary tangles3

Amyloidogenic proteins3

Aggregate2

Parkinson's4

Biochemistry1

Mechanisms6

Beta-amyloid1

Structures5

20173

Pathway4

Biology14

Biol2

Functional7

Neurons3

Aberrant1

Soluble1

Folding22

Vivo1

Formation8

Transthyretin2

Amyloidoses1

Cytotoxicity2

Glycosaminoglycans1

Lipids2

Polypeptide2

Determinants4

Characterization1

Astbury Centre1

Myoglobin1

Prone1

Oligomeric2

Complexes1

Biological4

Mass spectrometry1

Structure23

Partially2

Bioinformatics1

DIFFRACTION1

Interfere1