Amyloidogenesis and amyloid fibril formation. Medical search. Frequent questions

Small molecule inhibitors of islet amyloid polypeptide fibril formation. (jnu.ac.in)
Inhibiting the islet amyloid polypeptide fibril formation by the red wine compound resveratrol. (jnu.ac.in)
The laboratory of Pr Bourgault is studying the mechanisms by which the peptidic hormone islet amyloid polypeptide (IAPP) and the immunoglobulin light chain (LC) protein self-associate to form these well-defined amyloid fibrils. (uqam.ca)
Modulation of Amyloidogenesis Controlled by the C-Terminal Domain of Islet Amyloid Polypeptide Shows New Functions on Hepatocyte Cholesterol Metabolism. (phoenixpeptide.com)
The islet amyloid polypeptide (IAPP) or amylin maintains a key role in metabolism. (phoenixpeptide.com)
Graphene quantum dots rescue protein dysregulation of pancreatic β-cells exposed to human islet amyloid polypeptide", coauthored by Yunxiang, is now accepted for publication in Nano Research. (clemson.edu)
Single-molecular hetero-amyloidosis of human islet amyloid polypeptide", co-authored by Yanting and Yunxiang, is now accepted for publication in Nano Letter. (clemson.edu)
The aggregation of the amyloidogenic polypeptide IAPP (Islet Amyloid Polypeptide, amylin) is believed to play a direct role in the death of pancreatic β-islet cells in type II diabetes. (openbiochemistryjournal.com)
The misfolded amyloid protein found in the pancreas of individuals afflicted with type II diabetes is the 37-amino acid polypeptide IAPP (islet amyloid polypeptide, amylin). (openbiochemistryjournal.com)
PMDs) and involves human islet amyloid polypeptide (hIAPP) misfolding and accumulating in parts of the body, primarily in the pancreas, causing damage to islet cells and affecting glucose regulation. (silverchair.com)
In in vitro experiments, curcumin has been shown to suppress the aggregation and cytotoxicity of Aβ, αSyn, islet amyloid precursor protein, ATTR, and prion protein ( Stefani and Rigacci, 2013 ). (elifesciences.org)

Amyloidosis results from the accumulation of pathogenic amyloids-most of which are aggregates of misfolded proteins-in a variety of tissues. (medscape.com)
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)
[ 5 ] 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)
The modern era of amyloidosis classification began in the late 1960s with the development of methods to solubilize amyloid fibrils. (medscape.com)
The familial amyloid neuropathies (or familial amyloidotic neuropathies, neuropathic heredofamilial amyloidosis, familial amyloid polyneuropathy) are a rare group of autosomal dominant diseases wherein the autonomic nervous system and/or other nerves are compromised by protein aggregation and/or amyloid fibril formation. (wikipedia.org)
Lysozyme amyloidosis is a rare disease characterized by the deposition of amyloid fibrils of the enzyme lysozyme. (biomedcentral.com)
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins, which then aggregate extracellularly as insoluble fibrils, damaging the structure and function of affected organs. (nyu.edu)
We recently identified the first naturally occurring structural variant, D76N, of human β 2 - microglobulin (β 2 m), the ubiquitous light chain of class I major histocompatibility antigens, as the amyloid fibril protein in a family with a new phenotype of late onset fatal hereditary systemic amyloidosis. (nyu.edu)
Elucidation of this crucial causative event in clinical amyloidosis should also help to explain the hitherto mysterious timing and location of amyloid deposition. (nyu.edu)
Different light chains are responsible for two diseases with diametrically opposite mesangial alterations: Light chain deposition disease which results in the expansion of the mesangium due to accumulation of matrix proteins not present in the normal mesangium and AL (light chain-associated) amyloidosis where the native mesangial matrix is replaced by fibrils (amyloid). (heraldopenaccess.us)
Amyloidosis is a group of heterogeneous disorders characterized by the deposition of misfolded protein that aggregates into fibrils, affecting multiple organs including the heart, neural tissues, kidneys, and the gastrointestinal tract ( 1 ). (thischangedmypractice.com)
Amyloidosis is a large group of pathologic conditions in which a particular type of protein, called amyloid, is abnormally deposited in various tissues or organs. (hyperthermicwellness.com)
In addition, the deposition of amyloid fibrils may occur in specific areas of a single tissue (localized amyloidosis) or throughout the body (systemic amyloidosis). (hyperthermicwellness.com)
Each type of amyloidosis is classified according to clinical signs and the main peptide or protein that constitutes the amyloid fibrils. (hyperthermicwellness.com)
Amyloidosis depots contain not only the major fibrillar component but also minor nonfibrillar components such as glycosaminoglycans (GAGs), apolipoprotein E (apoE), and serum amyloid P (SAP) components [ 3 ]. (hyperthermicwellness.com)
To elucidate the mechanisms by which curcumin affects systemic amyloidosis, we investigated amyloid deposition and molecular changes in a mouse model of amyloid apolipoprotein A-II (AApoAII) amyloidosis, in which mice were fed a curcumin-supplemented diet. (elifesciences.org)
Taken together, these results demonstrate that curcumin is a PPARα activator and may affect expression levels of proteins involved in amyloid deposition to influence amyloidosis and metabolism in a complex manner. (elifesciences.org)
Amyloidosis is a group of diseases characterized by abnormal aggregation of proteins to form amyloid fibrils, and subsequent deposition in various tissues and organs, which can lead to severe functional failures. (elifesciences.org)

[ 6 ] In humans, about 23 different unrelated proteins are known to form amyloid fibrils in vivo. (medscape.com)
Amyloidogenic proteins are most often associated with neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and Huntington's disease, but there are more than two dozen human proteins known to form amyloid fibrils associated with disease. (biomedcentral.com)

Amyloidoses are a group of diseases defined by the formation of protein aggregates characterized by stacks of cross-beta sheets [ 1 ]. (biomedcentral.com)
However, there are number of cases in which the favorable states of proteins are rather unfolded, partially folded (e.g., "molten globular"), or misfolded (e.g., nonspecific aggregates or amyloid fibrils). (tau.ac.il)
Atomic force microscopy revealed that myricetin prevented fiber formation under rigorous conditions conducive to forming IAPP aggregates. (openbiochemistryjournal.com)
Ivan M. Vikhlyantsev Amyloids are insoluble fibrous protein aggregates, and their accumulation. (silverchair.com)
Moreover, amyloid aggregates of both. (silverchair.com)

NMR spectroscopic investigation of early events in IAPP amyloid fibril formation. (jnu.ac.in)
By combining chemical biology, biophysics and biochemistry, we aim at elucidating the roles of the microenvironment and the (transient) interactome on the kinetics and pathway of amyloidogenesis and at developing (bio)chemical approaches to control the assembly of IAPP and LC. (uqam.ca)
Our study on the direct observation of single-molecular fibril growth of IAPP fibrils with different morphologies in silico , first authored by Gangtong Huang, is now accepted for publication in JCIM. (clemson.edu)
These results indicate that myricetin is a strong inhibitor of IAPP amyloid aggregation and a potential lead molecule for the development of an amyloid inhibiting therapeutic. (openbiochemistryjournal.com)

Protein aggregation and amyloid deposition are associated with diseases as diverse as Alzheimer's disease, diabetes mellitus type 2 (DM-2), Creutzfel-Jakob disease and numerous amyloidoses. (uqam.ca)
The multicomponent nature of neuronal plaques in Alzheimer's disease signifies the possible recruitment of non-Aβ candidates during the amyloid growth of Aβ peptides. (shengsci.com)
Some of the most well-known amyloidoses are neurodegenerative diseases such as Alzheimer's disease (involving amyloid-beta peptide) and Parkinson's disease (involving alpha-synuclein protein). (biomedcentral.com)
Phenolic oxime oligomers inhibit Alzheimer's amyloid fibril formation and disaggregate fibrils in vitro. (univ-grenoble-alpes.fr)
A multimeric quinacrine conjugate as a potential inhibitor of Alzheimer's $\beta$-amyloid fibril formation. (univ-grenoble-alpes.fr)
Micrograph of a section of the cerebral cortex from a person with Alzheimer's disease , immunostained with an antibody to amyloid beta (brown), a protein fragment that accumulates in amyloid plaques and cerebral amyloid angiopathy . (wikipedia.org)
[9] However, some proteinaceous lesions lack birefringence and contain few or no classical amyloid fibrils, such as the diffuse deposits of amyloid beta (Aβ) protein in the brains of people with Alzheimer's. (wikipedia.org)
Spontaneous Formation of β-sheet Nano-barrels during the Early Aggregation of Alzheimer's Amyloid Beta", a joint work by Clemson, Monash University, Ningbo University, and Southwest University, is now accepted for publication in Nano Today. (clemson.edu)
One of the first known mechanisms is the accumulation of proteins: α-synuclein (Parkinson's disease), Tau (Alzheimer's disease) and β-amyloid (Alzheimer's disease and Parkinson's disease) proteins. (encyclopedia.pub)
In Parkinson's and Alzheimer's disease, protein aggregation concerns α-synuclein, Tau and β-amyloid proteins, respectively, although β-amyloid proteins are equally present in Parkinson's disease. (encyclopedia.pub)
Alzheimer's disease (AD) and the toxicity and mechanisms of amyloid protein aggregation will be emphasized in this review. (hyperthermicwellness.com)

To better understand the role of CsgE in curli formation, we have determined the solution NMR structure of a double mutant of CsgE (W48A/F79A) that appears to be similar to the wild-type (WT) protein in overall structure and function but does not form mixed oligomers at NMR concentrations similar to the WT. (wustl.edu)
It is believed that in each case, a protein misfolds and self-assembles into toxic oligomers and fibers, ultimately forming insoluble amyloid. (openbiochemistryjournal.com)
Aggregation of p53 into amyloid oligomers and fibrils has been shown. (silverchair.com)

This compound is a potent inhibitor of alpha-synuclein and beta-amyloid oligomerization and fibrillogenesis protecting against extracellular toxicity (2), also binds to transthyretin (TTR) with high affinity (21 to 58 nM) and inhibits TTR aggregation in human plasma and prevents TTR-induced cytotoxicity in vitro. (mayflowerbio.com)
Here we show that, uniquely, D76N β 2 mreadily forms amyloid fibrils in vitro under physiological extracellular conditions. (nyu.edu)
The classical, histopathological definition of amyloid is an extracellular , proteinaceous deposit exhibiting cross-beta structure. (wikidoc.org)
Arun Upadhyay Amyloids are high-order proteinaceous formations deposited in both intra- and extracellular spaces. (silverchair.com)

Due to the rareness of the other types of familial neuropathies, transthyretin amyloidogenesis-associated polyneuropathy should probably be considered first. (wikipedia.org)
U.S. FDA Approves VYNDAQEL® and VYNDAMAX™ for use in Patients with Transthyretin Amyloid Cardiomyopathy, a Rare and Fatal Disease. (medscape.com)
Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade. (medscape.com)
Sixty years of transthyretin familial amyloid polyneuropathy (TTR-FAP) in Europe: where are we now? (medscape.com)
2005). Susceptibility and modifier genes in Portuguese transthyretin V30M amyloid polyneuropathy: Complexity in a single-gene disease . (up.pt)
2016). A novel bis-furan scaffold for transthyretin stabilization and amyloid inhibition . (up.pt)

Spectroscopic characterization of diverse amyloid fibrils in-vitro by the fluorescent dye Nile red. (jnu.ac.in)
Wild type β 2 m is recruited by the variant into amyloid fibrils in vitro but is absent from amyloid deposited in vivo. (nyu.edu)
For these peptides , cross- polymerization (fibrils of one polypeptide sequence causing other fibrils of another sequence to form) is a phenomenon observed in vitro . (wikidoc.org)
Cofactors such as glycosaminoglycans and metal ions have been found associated with amyloid deposits in vivo and shown to affect protein assembly kinetics in vitro. (silverchair.com)
320) Eto M, Hashimoto T, Shimizu T, Iwatsubo T: Characterization of the unique in vitro effects of unsaturated fatty acids on the formation of amyloid beta fibrils. (u-tokyo.ac.jp)
Some natural phenolic compounds extracted from plants exhibit certain anti-amyloid activity in vitro and in vivo ( Stefani and Rigacci, 2013 ). (elifesciences.org)

Thus, amyloid may alter the normal function of tissues and cause serious changes in tissues and organs of the body [ 3 , 4 ]. (hyperthermicwellness.com)

The accumulated data support the model where protein fibrillogenesis proceeds via the formation of a relatively unfolded amyloidogenic conformation, which shares many structural properties with the pre-molten globule state, a partially folded intermediate first found during the equilibrium and kinetic (un)folding studies of several globular proteins and later described as one of the structural forms of natively unfolded proteins. (usf.edu)
Here, we show that amyloid fibrils of Aβ1-40 peptide can effectively initiate amyloid formation in different globular proteins and metabolites, converti. (shengsci.com)
Our results suggest general mechanistic principles of in vivo amyloid fibrillogenesis by globular proteins, a previously obscure process. (nyu.edu)

Polymorphisms that slightly vary native peptides or inflammatory processes set the stage for abnormal protein folding and amyloid fibril deposition. (medscape.com)
Amyloidogenesis highlighted by designed peptides forming supramolecular self-assemblies. (univ-grenoble-alpes.fr)
Generally, amyloid refers to misfolded peptides or proteins that demonstrate a stable, cross-beta super-secondary structure that renders it insoluble, fibrous-like, and resistant to proteolysis. (hyperthermicwellness.com)

Genotypic-phenotypic variations in a series of 65 patients with familial amyloid polyneuropathy. (medscape.com)
The course and prognostic factors of familial amyloid polyneuropathy after liver transplantation. (medscape.com)

The formation of amyloid fibrils in vivo is poorly understood. (nyu.edu)
The CsgG-CsgE complex is the curli secretion channel and is essential for the formation of the curli fibril in vivo. (wustl.edu)

Various descriptive classification systems were proposed based on the organ distribution of amyloid deposits and clinical findings. (medscape.com)
These deposits often recruit various sugars and other components such as Serum Amyloid P component , resulting in complex, and sometimes heterogeneous structures. (wikidoc.org)
amyloid deposits exhibit an apple-green birefringence under a polarized light microscope after staining with the dye Congo red and appear as rigid, nonbranching fibrils 7.5 to 10 nm in diameter under extremely high magnification using an electron microscope [ 5 ]. (hyperthermicwellness.com)

[ 2 ] 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)
There are dozens of different amyloid diseases caused by a variety of both wild type (WT) and mutant forms of proteins [ 2 ]. (biomedcentral.com)
However, not all amyloid diseases affect the brain. (biomedcentral.com)
Understanding curli formation can provide the information necessary to develop treatments and therapeutic agents for biofilm-related infections and may benefit the prevention and treatment of amyloid diseases. (wustl.edu)
Several well-known examples of human amyloid-related diseases and the official nomenclature and classification of their causative agents are shown in Table 1 (See link). (hyperthermicwellness.com)

Despite the similar effect in the heart, AL and ATTR are two patho-physiologically different disease processes leading to CA. In AL disease, the amyloid proteins are light chains produced by clonal plasma cells in the bone marrow ( 4 ). (thischangedmypractice.com)
Title: Closing the gaps between Chemistry, Physics, Biology and Clinical Medicine: ATTR amyloidogenesis. (lu.se)

It is believed that the neuropathogenesis of this disease may be triggered by the accumulation of toxic amyloid in the central nervous system (CNS). (hyperthermicwellness.com)

In addition, the CZ-based particles have been found to exhibit an anti-amyloidogenic effect on the amyloid aggregation of insulin and lysozyme in a dose- and temperature-dependent manner. (nature.com)
Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion. (jnu.ac.in)
Lysozyme is an antimicrobial protein that is used as a general model to study amyloid fibril formation. (biomedcentral.com)
Studies aimed at elucidating the process of amyloid formation of lysozyme tend to focus on partial unfolding of the native state due to the relative instability of mutant amyloidogenic variants. (biomedcentral.com)
This study used lysozyme as a model to demonstrate the utility of combining 3D structural analysis with RIN analysis for studying the general process of amyloidogenesis. (biomedcentral.com)
Results indicated that binding of two or more amyloidogenic lysozyme mutants may be involved in amyloid nucleation by placing key residues (21, 62, 104, 122, and 112-117) in proximity before partial unfolding occurs. (biomedcentral.com)
Since lysozyme is structurally and functionally well-characterized, the protein provides a useful model for understanding the complex process of amyloid fibril formation [ 13 ]. (biomedcentral.com)
Several studies have investigated the role of amyloidogenic mutations on lysozyme amyloid formation with a focus on the first identified mutations, I56T and D67H. (biomedcentral.com)

Designed amyloid $\beta$ peptide fibril-a tool for high-throughput screening of fibril inhibitors. (univ-grenoble-alpes.fr)

To date, at least 28 different proteins have been identified as amyloids in humans [ 3 , 5 - 7 ]. (hyperthermicwellness.com)

Aβ1-40 mediated aggregation of proteins and metabolites unveils the relevance of amyloid cross-seeding in amyloidogenesis. (shengsci.com)

Amyloids are insoluble fibrous protein aggregations sharing specific structural traits. (wikidoc.org)

Since the structure of proteins in amyloid plaques are different from the native structure, amyloidogenic proteins must at least partially unfold during amyloidogenesis. (biomedcentral.com)
331) Hashimoto T, Fujii D, Naka Y, Kashiwagi-Hakozaki M, Matsuo Y, Matsuura Y, Wakabayashi T, Iwatsubo T: Collagenous Alzheimer amyloid plaque component impacts on the compaction of amyloid-β plaques. (u-tokyo.ac.jp)

The amyloid fibrils are well-organized nanostructures that results from the self-assembly of a given polypeptide chain. (uqam.ca)
There are two broad classes of amyloid-forming polypeptide sequences. (wikidoc.org)

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)
Obviously, molecular mechanisms describing amyloidogenesis of ordered and natively unfolded proteins are different. (usf.edu)
So far, there have been a vast number of studies that have hypothesized disease mechanisms for AD, the majority of which support the amyloid hypothesis. (hyperthermicwellness.com)
Potential mechanisms related to overproduction or impaired clearance of these amyloids that may lead to its abnormal deposition in the brain as well as some possible molecular targets for AD treatment will be the focus of this review. (hyperthermicwellness.com)

The work "Amphiphilic Surface Chemistry of Fullerenols Is Necessary for Inhibiting the Amyloid Aggregation of Alpha-Synuclein NACore" first authored by Yunxiang Sun is now accepted for publication in Nanoscale. (clemson.edu)

Evaluation of the new F23R variant demonstrated inhibition of β-sheet structure and, therefore, amyloid formation on the native C-terminal, phenomenon that was associated with functional optimization in calcium and cholesterol management coupled with the optimization of insulin secretion by beta cells. (phoenixpeptide.com)
Our collaborative work, "Inhibition of Amyloid Beta Toxicity in Zebrafish with A Chaperone-Gold Nanoparticle Dual Strategy", is now accepted for publication in Nature Communications. (clemson.edu)

Although the accumulation of amyloidogenic proteins in neuroinflammatory conditions is generally considered pathologic, in a murine model of multiple sclerosis, amyloid-forming fibrils, comprised of hexapeptides, are anti-inflammatory. (phoenixpeptide.com)

2010). Randomization of Amyloid-β-Peptide(1-42) Conformation by Sulfonated and Sulfated Nanoparticles Reduces Aggregation and Cytotoxicity . (up.pt)

Congo red staining of a cardiac biopsy specimen containing amyloid, viewed under polarized light. (medscape.com)
cardiac amyloid no longer a zebra diagnosis? (thischangedmypractice.com)
This Changed My Practice » New insight into "HFpEF" - cardiac amyloid no longer a zebra diagnosis? (thischangedmypractice.com)

Because the formation of amyloid fibrils is nearly irreversible, maintaining proteostasis and inhibiting amyloid aggregation present a challenge for development of an effective treatment. (elifesciences.org)

2015). Polymer-doxycycline conjugates as fibril disrupters: An approach towards the treatment of a rare amyloidotic disease . (up.pt)
Glutamine-rich polypeptides are important in the amyloidogenesis of yeast and mammalian prions , as well as Huntington's disease . (wikidoc.org)
In Parkinson's disease, insoluble α-synuclein fibrils compose the Lewy bodies and Lewy neurites. (encyclopedia.pub)

We are probing the relation between the supramolecular organization, the molecular architecture and the stability to develop amyloids with precise dynamic properties. (uqam.ca)
This amyloid layer acts as a molecular scaffold that promotes localised melanin synthesis and the adhesion of immune cells around the non-self intruder during encapsulation response. (cirn-na.com)

However, some species do not form amyloid fibril structures. (phoenixpeptide.com)
Recently, this definition has come into question as some classic amyloid species have been observed in distinctly intracellular locations. (wikidoc.org)

Functional amyloids play a beneficial role in a variety of physiologic processes (eg, long-term memory formation, gradual release of stored peptide hormones). (medscape.com)
Curli, consisting primarily of major structural subunit CsgA, are functional amyloids produced on the surface of Escherichia coli, as well as many other enteric bacteria, and are involved in cell colonization and biofilm formation. (wustl.edu)
Functional amyloids in insect immune response. (cirn-na.com)

Saraiva MJ, Birken S, Costa PP. Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. (medscape.com)

All types of amyloid consist of one major fibrillar protein that defines the type of amyloid. (medscape.com)

We hypothesized that an amylin hexapeptide that forms fibrils can attenuate the systemic inflammatory response in a murine model of sepsis. (phoenixpeptide.com)

[9] Subsequent research has shown that many different proteins can form amyloid, and that all amyloids show birefringence in cross- polarized light after staining with the dye Congo red , as well as a fibrillar ultrastructure when viewed with an electron microscope . (wikipedia.org)

These observations lead to much interest in the significance and mechanism of formation of such unfolded, misfolded or partially folded structures in physiological as well as pathological conditions. (tau.ac.il)
A characteristic of several CAP proteins is their formation of amyloid -like structures in the presence of lipids. (silverchair.com)

The flexibility of this structural form is essential for the conformational rearrangements driving the formation of the core cross-beta structure of the amyloid fibril. (usf.edu)
An auto-catalytic surface for conformational replication of amyloid fibrils- Genesis of an amyloid world? (jnu.ac.in)

This 37-residues-peptide could form pancreatic amyloids, which are a characteristic feature of diabetes mellitus type 2. (phoenixpeptide.com)
Here we show that a protein produced by haemocytes of Heliothis virescens (Lepidoptera, Noctuidae) larvae, belonging to XendoU family, generates amyloid fibrils, which accumulate in large cisternae of the rough endoplasmic reticulum and are released upon immune challenge, to form a layer coating non-self objects entering the haemocoel. (cirn-na.com)

Type 2 diebetes, amyloid, amylin. (openbiochemistryjournal.com)

In 1902, at the Karlsbad meeting of the Gesellschaft Deutscher Naturforscher und rzte, Franz Hofmeister said:[2] "The type of condensation described here through formation of CO NH CH= groups may thus explain both the building up of protein substances in the organism, as well as their breakdown in the intestinal tract and in the tissues. (pdffox.com)

Some of these, although demonstrably cross-beta sheet, fail other characteristic tests of amyloid, such as the Congo Red birefringence test . (wikidoc.org)
Micrograph of amyloid in a section of liver that has been stained with the dye Congo red and viewed with crossed polarizing filters, yielding a typical orange-greenish birefringence. (wikipedia.org)

Curcumin supplementation for 12 weeks significantly increased AApoAII amyloid deposition relative to controls, especially in the liver and spleen. (elifesciences.org)

CsgE could establish a paradigm for the regulation of amyloidogenesis because of its unique role in curli formation. (wustl.edu)

Identifying residues in the native state that may be involved in amyloid formation could provide novel drug targets to prevent a range of amyloidoses. (biomedcentral.com)

2007). A primer of amyloid nomenclature . (up.pt)

Amyloid polymerization is generally sequence-sensitive, that is, causing mutations in the sequence can prevent self-assembly, especially if the mutation is a beta-sheet breaker, such as proline . (wikidoc.org)

Anatomy10

Organisms2

Diseases15

Chemicals and Drugs55

Analytical, Diagnostic and Therapeutic Techniques and Equipment26

Psychiatry and Psychology1

Phenomena and Processes29

Disciplines and Occupations1

Technology, Industry, Agriculture2

Information Science4

Health Care1

Islet11

Amyloidosis18

Known to form amyloid fibrils2

Aggregates5

IAPP4

Alzheimer's11

Oligomers3

Extracellular4

Transthyretin6

Vitro6

Alter the normal function of tissues1

Globular proteins3

Peptides3

Familial amyloid polyne2

Vivo2

Deposits3

Diseases5

ATTR2

Toxic amyloid1

Lysozyme8

Inhibitors1

Proteins have been identified1

Aggregation of proteins1

Insoluble fibrous1

Plaques2

Polypeptide2

Mechanisms4

Alpha-synuclein1

Inhibition2

Amyloidogenic proteins1

Conformation1

Cardiac3

Inhibiting1

Disease3

Molecular2

Species2

Functional3

Polyneuropathy1

Major fibrillar1

Systemic1

Fibrillar1

Structures2

Conformational2

Form2

Amylin1

Tissues1

Birefringence2

Liver1

Curli1

Native1

Nomenclature1

Mutations1