Articles with "hiapp" as a keyword



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Human Islet Amyloid Polypeptide (hIAPP) Protofibril‐Specific Antibodies for Detection and Treatment of Type 2 Diabetes

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Published in 2022 at "Advanced Science"

DOI: 10.1002/advs.202202342

Abstract: Abstract Type 2 diabetes mellitus (T2D) is a major public health concern and is characterized by sustained hyperglycemia due to insulin resistance and destruction of insulin‐producing β cells. One pathological hallmark of T2D is the… read more here.

Keywords: protofibril specific; hiapp; human islet; type diabetes ... See more keywords
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Evidence for different in vitro oligomerization behaviors of synthetic hIAPP obtained from different sources

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Published in 2020 at "Analytical and Bioanalytical Chemistry"

DOI: 10.1007/s00216-020-02560-5

Abstract: Type 2 diabetes is characterized by the aggregation of human islet amyloid polypeptide (hIAPP), from monomer to amyloid deposits that are made of insoluble fibrils. Discrepancies concerning the nature of formed species or oligomerization kinetics… read more here.

Keywords: different sources; vitro oligomerization; evidence different; hiapp ... See more keywords
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The flanking peptides issue from the maturation of the human islet amyloid polypeptide (hIAPP) slightly modulate hIAPP-fibril formation but not hIAPP-induced cell death.

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Published in 2019 at "Biochimie"

DOI: 10.1016/j.biochi.2019.12.005

Abstract: Type 2 diabetes mellitus is a disease characterized by the formation of amyloid fibrillar deposits consisting mainly in human islet amyloid polypeptide (hIAPP), a peptide co-produced and co-secreted with insulin. hIAPP and insulin are synthesized… read more here.

Keywords: flanking peptides; hiapp; formation; fibril formation ... See more keywords
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The pressure and temperature perturbation approach reveals a whole variety of conformational substates of amyloidogenic hIAPP monitored by 2D NMR spectroscopy.

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Published in 2019 at "Biophysical chemistry"

DOI: 10.1016/j.bpc.2019.106239

Abstract: The intrinsically disordered human islet amyloid polypeptide (hIAPP) is a 37 amino acid peptide hormone that is secreted by pancreatic beta cells along with glucagon and insulin. The glucose metabolism of humans is regulated by… read more here.

Keywords: conformational substates; spectroscopy; hiapp; self assembly ... See more keywords
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Assessing the role of osmolytes on the conformational harmony of islet amyloid polypeptide.

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Published in 2020 at "International journal of biological macromolecules"

DOI: 10.1016/j.ijbiomac.2020.08.104

Abstract: Several pathological disorders have known linkages with the misfolding and abnormal oligomerization of peptides and proteins and their accumulation into numerous aggregates. One such peptide is human islet amyloid polypeptide (hIAPP) responsible for amyloid aggregation… read more here.

Keywords: aggregation; islet amyloid; hiapp; amyloid polypeptide ... See more keywords
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A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP.

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Published in 2017 at "Journal of the American Chemical Society"

DOI: 10.1021/jacs.7b08830

Abstract: Transiently populated oligomers formed en route to amyloid fibrils may constitute the most toxic aggregates associated with many amyloid-associated diseases. Most nucleation theories used to describe amyloid aggregation predict low oligomer concentrations and do not… read more here.

Keywords: energy barrier; energy; hiapp; oligomeric intermediate ... See more keywords
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Tuning the rate of aggregation of hIAPP into amyloid using small-molecule modulators of assembly

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Published in 2022 at "Nature Communications"

DOI: 10.1038/s41467-022-28660-7

Abstract: Human islet amyloid polypeptide (hIAPP) self-assembles into amyloid fibrils which deposit in pancreatic islets of type 2 diabetes (T2D) patients. Here, we applied chemical kinetics to study the mechanism of amyloid assembly of wild-type hIAPP… read more here.

Keywords: small molecule; hiapp; aggregation; aggregation hiapp ... See more keywords
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Binuclear ruthenium complexes inhibit the fibril formation of human islet amyloid polypeptide

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Published in 2017 at "RSC Advances"

DOI: 10.1039/c6ra28107a

Abstract: The deposition of human islet amyloid polypeptide (hIAPP) is closely correlated with type II diabetes mellitus (T2DM). hIAPP misfolding, as a significant causative factor of T2DM, can lead to the failure of islet transplant. Therefore,… read more here.

Keywords: islet amyloid; islet; human islet; hiapp ... See more keywords
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His18 promotes reactive oxidative stress production in copper-ion mediated human islet amyloid polypeptide aggregation

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Published in 2020 at "RSC Advances"

DOI: 10.1039/c9ra09943c

Abstract: Copper ions play a critical role in human islet amyloid polypeptide (hIAPP) aggregation, which has been found in more than 90% of patients with type-2 diabetes (T2D). The role of Cu(II) in the cell cytotoxicity… read more here.

Keywords: islet amyloid; human islet; hiapp; copper ... See more keywords
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Anti-aggregation effect of carbon quantum dots on diabetogenic and beta-cell cytotoxic amylin and beta amyloid heterocomplexes.

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Published in 2022 at "Nanoscale"

DOI: 10.1039/d2nr03173f

Abstract: Pancreatic islet amyloid deposition is a pathological hallmark of Type 2 diabetes (T2D), contributing to reduced functional β-cell mass. Islet amyloids result not only from the aggregation and fibrillation of human islet amyloid polypeptide (hIAPP),… read more here.

Keywords: aggregation; cell; carbon; hiapp ... See more keywords
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Linking hIAPP misfolding and aggregation with type 2 diabetes mellitus: a structural perspective

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Published in 2022 at "Bioscience Reports"

DOI: 10.1042/bsr20211297

Abstract: Abstract There are over 40 identified human disorders that involve certain proteins folding incorrectly, accumulating in the body causing damage to cells and organs and causing disease. Type 2 Diabetes Mellitus (T2DM) is one of… read more here.

Keywords: hiapp; linking hiapp; type diabetes; hiapp misfolding ... See more keywords