Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 155 entries
Sorted by: Best Match Show Resources per page
Breakout character of islet amyloid polypeptide hydrophobic mutations at the onset of type-2 diabetes.

Physical review. E, Statistical, nonlinear, and soft matter physics

Frigori RB.
PMID: 25493825
Phys Rev E Stat Nonlin Soft Matter Phys. 2014 Nov;90(5):052716. doi: 10.1103/PhysRevE.90.052716. Epub 2014 Nov 17.

Toxic fibrillar aggregates of islet amyloid polypeptide (IAPP) appear as the physical outcome of a peptidic phase transition signaling the onset of type-2 diabetes mellitus in different mammalian species. In particular, experimentally verified mutations on the amyloidogenic segment 20-29...

Cite
Frigori RB. Breakout character of islet amyloid polypeptide hydrophobic mutations at the onset of type-2 diabetes. Phys Rev E Stat Nonlin Soft Matter Phys. 2014;90(5):052716doi: 10.1103/PhysRevE.90.052716.
Frigori, R. B. (2014). Breakout character of islet amyloid polypeptide hydrophobic mutations at the onset of type-2 diabetes. Physical review. E, Statistical, nonlinear, and soft matter physics, 90(5), 052716. https://doi.org/10.1103/PhysRevE.90.052716
Frigori, Rafael B. "Breakout character of islet amyloid polypeptide hydrophobic mutations at the onset of type-2 diabetes." Physical review. E, Statistical, nonlinear, and soft matter physics vol. 90,5 (2014): 052716. doi: https://doi.org/10.1103/PhysRevE.90.052716
Frigori RB. Breakout character of islet amyloid polypeptide hydrophobic mutations at the onset of type-2 diabetes. Phys Rev E Stat Nonlin Soft Matter Phys. 2014 Nov;90(5):052716. doi: 10.1103/PhysRevE.90.052716. Epub 2014 Nov 17. PMID: 25493825.
Copy Download .nbib Format: NLM
Identification of Plant Extracts that Inhibit the Formation of Diabetes-Linked IAPP Amyloid.

Journal of herbal medicine

Fuentes AL, Hennessy K, Pascual J, Pepe N, Wang I, Santiago A, Chaggan C, Martinez J, Rivera E, Cota P, Cunha C, Nogaj LA, Moffet DA.
PMID: 27042401
J Herb Med. 2016 Mar;6(1):37-41. doi: 10.1016/j.hermed.2015.11.001.

The extracts of 27 vegetables, spices and herbs were screened for their functional ability to inhibit the aggregation of islet amyloid polypeptide (IAPP, amylin) into toxic amyloid aggregates. The aggregation of IAPP has been directly linked to the death...

Cite
Fuentes AL, Hennessy K, Pascual J, et al. Identification of Plant Extracts that Inhibit the Formation of Diabetes-Linked IAPP Amyloid. J Herb Med. 2016;6(1):37-41doi: 10.1016/j.hermed.2015.11.001.
Fuentes, A. L., Hennessy, K., Pascual, J., Pepe, N., Wang, I., Santiago, A., Chaggan, C., Martinez, J., Rivera, E., Cota, P., Cunha, C., Nogaj, L. A., & Moffet, D. A. (2016). Identification of Plant Extracts that Inhibit the Formation of Diabetes-Linked IAPP Amyloid. Journal of herbal medicine, 6(1), 37-41. https://doi.org/10.1016/j.hermed.2015.11.001
Fuentes, Ana Lucia, et al. "Identification of Plant Extracts that Inhibit the Formation of Diabetes-Linked IAPP Amyloid." Journal of herbal medicine vol. 6,1 (2016): 37-41. doi: https://doi.org/10.1016/j.hermed.2015.11.001
Fuentes AL, Hennessy K, Pascual J, Pepe N, Wang I, Santiago A, Chaggan C, Martinez J, Rivera E, Cota P, Cunha C, Nogaj LA, Moffet DA. Identification of Plant Extracts that Inhibit the Formation of Diabetes-Linked IAPP Amyloid. J Herb Med. 2016 Mar;6(1):37-41. doi: 10.1016/j.hermed.2015.11.001. PMID: 27042401; PMCID: PMC4815265.
Copy Download .nbib Format: NLM
Inhibition of Toxic IAPP Amyloid by Extracts of Common Fruits.

Journal of functional foods

Kao PY, Green E, Pereira C, Ekimura S, Juarez D, Whyte T, Arhar T, Malaspina B, Nogaj LA, Moffet DA.
PMID: 26893614
J Funct Foods. 2015 Jan 01;12:450-457. doi: 10.1016/j.jff.2014.12.013.

The aggregation of the 37-amino acid polypeptide islet amyloid polypeptide (IAPP, amylin), as either insoluble amyloid or as small oligomers, appears to play a direct role in the death of pancreatic β-islet cells in type 2 diabetes. It is...

Cite
Kao PY, Green E, Pereira C, et al. Inhibition of Toxic IAPP Amyloid by Extracts of Common Fruits. J Funct Foods. 2015;12:450-457doi: 10.1016/j.jff.2014.12.013.
Kao, P. Y., Green, E., Pereira, C., Ekimura, S., Juarez, D., Whyte, T., Arhar, T., Malaspina, B., Nogaj, L. A., & Moffet, D. A. (2015). Inhibition of Toxic IAPP Amyloid by Extracts of Common Fruits. Journal of functional foods, 12450-457. https://doi.org/10.1016/j.jff.2014.12.013
Kao, Pei-Yu, et al. "Inhibition of Toxic IAPP Amyloid by Extracts of Common Fruits." Journal of functional foods vol. 12 (2015): 450-457. doi: https://doi.org/10.1016/j.jff.2014.12.013
Kao PY, Green E, Pereira C, Ekimura S, Juarez D, Whyte T, Arhar T, Malaspina B, Nogaj LA, Moffet DA. Inhibition of Toxic IAPP Amyloid by Extracts of Common Fruits. J Funct Foods. 2015 Jan 01;12:450-457. doi: 10.1016/j.jff.2014.12.013. PMID: 26893614; PMCID: PMC4754987.
Copy Download .nbib Format: NLM
The new proof of neuro-endocrine-immune network-expression of islet amyloid polypeptide in plasma cells in gastric mucosa of peptic ulcer patients.

World journal of gastroenterology

Huang Y, Lu SJ, Dong JX, Li F.
PMID: 11819614
World J Gastroenterol. 2000 Jun;6(3):417-418. doi: 10.3748/wjg.v6.i3.417.

No abstract available.

Cite
Huang Y, Lu SJ, Dong JX, et al. The new proof of neuro-endocrine-immune network-expression of islet amyloid polypeptide in plasma cells in gastric mucosa of peptic ulcer patients. World J Gastroenterol. 2000;6(3):417-418doi: 10.3748/wjg.v6.i3.417.
Huang, Y., Lu, S. J., Dong, J. X., & Li, F. (2000). The new proof of neuro-endocrine-immune network-expression of islet amyloid polypeptide in plasma cells in gastric mucosa of peptic ulcer patients. World journal of gastroenterology, 6(3), 417-418. https://doi.org/10.3748/wjg.v6.i3.417
Huang, Yan, et al. "The new proof of neuro-endocrine-immune network-expression of islet amyloid polypeptide in plasma cells in gastric mucosa of peptic ulcer patients." World journal of gastroenterology vol. 6,3 (2000): 417-418. doi: https://doi.org/10.3748/wjg.v6.i3.417
Huang Y, Lu SJ, Dong JX, Li F. The new proof of neuro-endocrine-immune network-expression of islet amyloid polypeptide in plasma cells in gastric mucosa of peptic ulcer patients. World J Gastroenterol. 2000 Jun;6(3):417-418. doi: 10.3748/wjg.v6.i3.417. PMID: 11819614; PMCID: PMC4688768.
Copy Download .nbib Format: NLM
Homeodomain protein IDX-1: a master regulator of pancreas development and insulin gene expression.

Trends in endocrinology and metabolism: TEM

Stoffers DA, Thomas MK, Habener JF.
PMID: 18406800
Trends Endocrinol Metab. 1997 May-Jun;8(4):145-51. doi: 10.1016/s1043-2760(97)00008-8.

The homeodomain protein IDX-1 appears to be a "master regulator" of pancreas development and beta-cell differentiation and function. In murine gene inactivation models and in a human subject with a homozygous mutation of the IDX-1 gene, the pancreas fails...

Cite
Stoffers DA, Thomas MK, Habener JF. Homeodomain protein IDX-1: a master regulator of pancreas development and insulin gene expression. Trends Endocrinol Metab. 1997;8(4):145-51doi: 10.1016/s1043-2760(97)00008-8.
Stoffers, D. A., Thomas, M. K., & Habener, J. F. (1997). Homeodomain protein IDX-1: a master regulator of pancreas development and insulin gene expression. Trends in endocrinology and metabolism: TEM, 8(4), 145-51. https://doi.org/10.1016/s1043-2760(97)00008-8
Stoffers, D A, et al. "Homeodomain protein IDX-1: a master regulator of pancreas development and insulin gene expression." Trends in endocrinology and metabolism: TEM vol. 8,4 (1997): 145-51. doi: https://doi.org/10.1016/s1043-2760(97)00008-8
Stoffers DA, Thomas MK, Habener JF. Homeodomain protein IDX-1: a master regulator of pancreas development and insulin gene expression. Trends Endocrinol Metab. 1997 May-Jun;8(4):145-51. doi: 10.1016/s1043-2760(97)00008-8. PMID: 18406800.
Copy Download .nbib Format: NLM
Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers.

Molecular neurodegeneration

Kayed R, Head E, Sarsoza F, Saing T, Cotman CW, Necula M, Margol L, Wu J, Breydo L, Thompson JL, Rasool S, Gurlo T, Butler P, Glabe CG.
PMID: 17897471
Mol Neurodegener. 2007 Sep 26;2:18. doi: 10.1186/1750-1326-2-18.

BACKGROUND: Amyloid-related degenerative diseases are associated with the accumulation of misfolded proteins as amyloid fibrils in tissue. In Alzheimer disease (AD), amyloid accumulates in several distinct types of insoluble plaque deposits, intracellular Abeta and as soluble oligomers and the...

Cite
Kayed R, Head E, Sarsoza F, et al. Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegener. 2007;2:18doi: 10.1186/1750-1326-2-18.
Kayed, R., Head, E., Sarsoza, F., Saing, T., Cotman, C. W., Necula, M., Margol, L., Wu, J., Breydo, L., Thompson, J. L., Rasool, S., Gurlo, T., Butler, P., & Glabe, C. G. (2007). Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Molecular neurodegeneration, 218. https://doi.org/10.1186/1750-1326-2-18
Kayed, Rakez, et al. "Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers." Molecular neurodegeneration vol. 2 (2007): 18. doi: https://doi.org/10.1186/1750-1326-2-18
Kayed R, Head E, Sarsoza F, Saing T, Cotman CW, Necula M, Margol L, Wu J, Breydo L, Thompson JL, Rasool S, Gurlo T, Butler P, Glabe CG. Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegener. 2007 Sep 26;2:18. doi: 10.1186/1750-1326-2-18. PMID: 17897471; PMCID: PMC2100048.
Copy Download .nbib Format: NLM
Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences.

PeerJ

Hartman K, Brender JR, Monde K, Ono A, Evans ML, Popovych N, Chapman MR, Ramamoorthy A.
PMID: 23638387
PeerJ. 2013 Feb 12;1:e5. doi: 10.7717/peerj.5. Print 2013.

Fragments of prostatic acid phosphatase (PAP248-286) in human semen dramatically increase HIV infection efficiency by increasing virus adhesion to target cells. PAP248-286 only enhances HIV infection in the form of amyloid aggregates termed SEVI (Semen Enhancer of Viral Infection),...

Cite
Hartman K, Brender JR, Monde K, et al. Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences. PeerJ. 2013;1:e5doi: 10.7717/peerj.5.
Hartman, K., Brender, J. R., Monde, K., Ono, A., Evans, M. L., Popovych, N., Chapman, M. R., & Ramamoorthy, A. (2013). Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences. PeerJ, 1e5. https://doi.org/10.7717/peerj.5
Hartman, Kevin, et al. "Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences." PeerJ vol. 1 (2013): e5. doi: https://doi.org/10.7717/peerj.5
Hartman K, Brender JR, Monde K, Ono A, Evans ML, Popovych N, Chapman MR, Ramamoorthy A. Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences. PeerJ. 2013 Feb 12;1:e5. doi: 10.7717/peerj.5. Print 2013. PMID: 23638387; PMCID: PMC3629062.
Copy Download .nbib Format: NLM
Kill two birds with one stone: making multi-transgenic pre-diabetes mouse models through insulin resistance and pancreatic apoptosis pathogenesis.

PeerJ

Kong S, Ruan J, Zhang K, Hu B, Cheng Y, Zhang Y, Yang S, Li K.
PMID: 29682407
PeerJ. 2018 Apr 17;6:e4542. doi: 10.7717/peerj.4542. eCollection 2018.

BACKGROUND: Type 2 diabetes is characterized by insulin resistance accompanied by defective insulin secretion. Transgenic mouse models play an important role in medical research. However, single transgenic mouse models may not mimic the complex phenotypes of most cases of...

Cite
Kong S, Ruan J, Zhang K, et al. Kill two birds with one stone: making multi-transgenic pre-diabetes mouse models through insulin resistance and pancreatic apoptosis pathogenesis. PeerJ. 2018;6:e4542doi: 10.7717/peerj.4542.
Kong, S., Ruan, J., Zhang, K., Hu, B., Cheng, Y., Zhang, Y., Yang, S., & Li, K. (2018). Kill two birds with one stone: making multi-transgenic pre-diabetes mouse models through insulin resistance and pancreatic apoptosis pathogenesis. PeerJ, 6e4542. https://doi.org/10.7717/peerj.4542
Kong, Siyuan, et al. "Kill two birds with one stone: making multi-transgenic pre-diabetes mouse models through insulin resistance and pancreatic apoptosis pathogenesis." PeerJ vol. 6 (2018): e4542. doi: https://doi.org/10.7717/peerj.4542
Kong S, Ruan J, Zhang K, Hu B, Cheng Y, Zhang Y, Yang S, Li K. Kill two birds with one stone: making multi-transgenic pre-diabetes mouse models through insulin resistance and pancreatic apoptosis pathogenesis. PeerJ. 2018 Apr 17;6:e4542. doi: 10.7717/peerj.4542. eCollection 2018. PMID: 29682407; PMCID: PMC5909684.
Copy Download .nbib Format: NLM
Effect of Terminal Modifications on the Adsorption and Assembly of hIAPP(20-29).

ACS omega

Hajiraissi R, Hanke M, Gonzalez Orive A, Duderija B, Hofmann U, Zhang Y, Grundmeier G, Keller A.
PMID: 31459500
ACS Omega. 2019 Feb 05;4(2):2649-2660. doi: 10.1021/acsomega.8b03028. eCollection 2019 Feb 28.

The assembly of peptides and proteins into nanoscale amyloid fibrils via formation of intermolecular β-sheets not only plays an important role in the development of degenerative diseases but also represents a promising approach for the synthesis of functional nanomaterials....

Cite
Hajiraissi R, Hanke M, Gonzalez Orive A, et al. Effect of Terminal Modifications on the Adsorption and Assembly of hIAPP(20-29). ACS Omega. 2019;4(2):2649-2660doi: 10.1021/acsomega.8b03028.
Hajiraissi, R., Hanke, M., Gonzalez Orive, A., Duderija, B., Hofmann, U., Zhang, Y., Grundmeier, G., & Keller, A. (2019). Effect of Terminal Modifications on the Adsorption and Assembly of hIAPP(20-29). ACS omega, 4(2), 2649-2660. https://doi.org/10.1021/acsomega.8b03028
Hajiraissi, Roozbeh, et al. "Effect of Terminal Modifications on the Adsorption and Assembly of hIAPP(20-29)." ACS omega vol. 4,2 (2019): 2649-2660. doi: https://doi.org/10.1021/acsomega.8b03028
Hajiraissi R, Hanke M, Gonzalez Orive A, Duderija B, Hofmann U, Zhang Y, Grundmeier G, Keller A. Effect of Terminal Modifications on the Adsorption and Assembly of hIAPP(20-29). ACS Omega. 2019 Feb 05;4(2):2649-2660. doi: 10.1021/acsomega.8b03028. eCollection 2019 Feb 28. PMID: 31459500; PMCID: PMC6649277.
Copy Download .nbib Format: NLM
Islet amyloid deposits preferentially in the highly functional and most blood-perfused islets.

Endocrine connections

Ullsten S, Bohman S, Oskarsson ME, Nilsson KPR, Westermark GT, Carlsson PO.
PMID: 28790139
Endocr Connect. 2017 Oct;6(7):458-468. doi: 10.1530/EC-17-0148. Epub 2017 Aug 08.

Islet amyloid and beta cell death in type 2 diabetes are heterogeneous events, where some islets are affected early in the disease process, whereas others remain visibly unaffected. This study investigated the possibility that inter-islet functional and vascular differences...

Cite
Ullsten S, Bohman S, Oskarsson ME, et al. Islet amyloid deposits preferentially in the highly functional and most blood-perfused islets. Endocr Connect. 2017;6(7):458-468doi: 10.1530/EC-17-0148.
Ullsten, S., Bohman, S., Oskarsson, M. E., Nilsson, K. P. R., Westermark, G. T., & Carlsson, P. O. (2017). Islet amyloid deposits preferentially in the highly functional and most blood-perfused islets. Endocrine connections, 6(7), 458-468. https://doi.org/10.1530/EC-17-0148
Ullsten, Sara, et al. "Islet amyloid deposits preferentially in the highly functional and most blood-perfused islets." Endocrine connections vol. 6,7 (2017): 458-468. doi: https://doi.org/10.1530/EC-17-0148
Ullsten S, Bohman S, Oskarsson ME, Nilsson KPR, Westermark GT, Carlsson PO. Islet amyloid deposits preferentially in the highly functional and most blood-perfused islets. Endocr Connect. 2017 Oct;6(7):458-468. doi: 10.1530/EC-17-0148. Epub 2017 Aug 08. PMID: 28790139; PMCID: PMC5574281.
Copy Download .nbib Format: NLM
Nanoparticles modulate membrane interactions of human Islet amyloid polypeptide (hIAPP).

Biochimica et biophysica acta. Biomembranes

Peretz Y, Malishev R, Kolusheva S, Jelinek R.
PMID: 29641979
Biochim Biophys Acta Biomembr. 2018 Sep;1860(9):1810-1817. doi: 10.1016/j.bbamem.2018.03.029. Epub 2018 Apr 08.

The dramatic expansion of nanotechnology applications, particularly the advent of nanomaterials and nanoparticles (NPs) into the consumer economy, have led to heightened awareness of their potential health risks. This study examines the impact of several NPs upon membrane-induced aggregation...

Cite
Peretz Y, Malishev R, Kolusheva S, et al. Nanoparticles modulate membrane interactions of human Islet amyloid polypeptide (hIAPP). Biochim Biophys Acta Biomembr. 2018;1860(9):1810-1817doi: 10.1016/j.bbamem.2018.03.029.
Peretz, Y., Malishev, R., Kolusheva, S., & Jelinek, R. (2018). Nanoparticles modulate membrane interactions of human Islet amyloid polypeptide (hIAPP). Biochimica et biophysica acta. Biomembranes, 1860(9), 1810-1817. https://doi.org/10.1016/j.bbamem.2018.03.029
Peretz, Yossef, et al. "Nanoparticles modulate membrane interactions of human Islet amyloid polypeptide (hIAPP)." Biochimica et biophysica acta. Biomembranes vol. 1860,9 (2018): 1810-1817. doi: https://doi.org/10.1016/j.bbamem.2018.03.029
Peretz Y, Malishev R, Kolusheva S, Jelinek R. Nanoparticles modulate membrane interactions of human Islet amyloid polypeptide (hIAPP). Biochim Biophys Acta Biomembr. 2018 Sep;1860(9):1810-1817. doi: 10.1016/j.bbamem.2018.03.029. Epub 2018 Apr 08. PMID: 29641979.
Copy Download .nbib Format: NLM
Physical and Toxicological Profiles of Human IAPP Amyloids and Plaques.

Science bulletin

Kakinen A, Sun Y, Javed I, Faridi A, Pilkington EH, Faridi P, Purcell AW, Zhou R, Ding F, Lin S, Chun Ke P, Davis TP.
PMID: 30662791
Sci Bull (Beijing). 2019 Jan 15;64(1):26-35. doi: 10.1016/j.scib.2018.11.012. Epub 2018 Nov 22.

Although much has been learned about the fibrillization kinetics, structure and toxicity of amyloid proteins, the properties of amyloid fibrils beyond the saturation phase are often perceived as chemically and biologically inert, despite evidence suggesting otherwise. To fill this...

Cite
Kakinen A, Sun Y, Javed I, et al. Physical and Toxicological Profiles of Human IAPP Amyloids and Plaques. Sci Bull (Beijing). 2018;64(1):26-35doi: 10.1016/j.scib.2018.11.012.
Kakinen, A., Sun, Y., Javed, I., Faridi, A., Pilkington, E. H., Faridi, P., Purcell, A. W., Zhou, R., Ding, F., Lin, S., Chun Ke, P., & Davis, T. P. (2019). Physical and Toxicological Profiles of Human IAPP Amyloids and Plaques. Science bulletin, 64(1), 26-35. https://doi.org/10.1016/j.scib.2018.11.012
Kakinen, Aleksandr, et al. "Physical and Toxicological Profiles of Human IAPP Amyloids and Plaques." Science bulletin vol. 64,1 (2019): 26-35. doi: https://doi.org/10.1016/j.scib.2018.11.012
Kakinen A, Sun Y, Javed I, Faridi A, Pilkington EH, Faridi P, Purcell AW, Zhou R, Ding F, Lin S, Chun Ke P, Davis TP. Physical and Toxicological Profiles of Human IAPP Amyloids and Plaques. Sci Bull (Beijing). 2019 Jan 15;64(1):26-35. doi: 10.1016/j.scib.2018.11.012. Epub 2018 Nov 22. PMID: 30662791; PMCID: PMC6333423.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 155 entries