The Materials Science of Protein Aggregation
Abstract Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer’s, Parkinson’s, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig’s disease), Huntington’s, and type II (mature onset) diabet...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Cox, D. L. [verfasserIn] Lashuel, H. [verfasserIn] Lee, K. Y. C. [verfasserIn] Singh, R. R. P. [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2005 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: MRS bulletin - Berlin : Springer, 1982, 30(2005), 6 vom: Juni, Seite 452-457 |
|---|---|
| Übergeordnetes Werk: |
volume:30 ; year:2005 ; number:6 ; month:06 ; pages:452-457 |
| Links: |
|---|
| DOI / URN: |
10.1557/mrs2005.123 |
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SPR041200241 |
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| 520 | |a Abstract Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer’s, Parkinson’s, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig’s disease), Huntington’s, and type II (mature onset) diabetes. In many cases, it has been demonstrated that conformational change and aggregation can occur outside living cells and complex biochemical networks. Hence, approaches from materials and physical science have enhanced our understanding of the role of protein aggregation in these diseases at the molecular and nanoscale levels. In this article, we will review what is known about these protein structures from the perspective of materials science, focusing on the details of emergent oligomeric and nanotube-like structures, their interactions with model lipid bilayers, how the structures relate to observed biological phenomena, and how protein aggregation and amyloid formation can be employed for the good in biology and materials science. | ||
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10.1557/mrs2005.123 doi (DE-627)SPR041200241 (SPR)mrs2005.123-e DE-627 ger DE-627 rakwb eng 670 ASE 51.00 bkl Cox, D. L. verfasserin aut The Materials Science of Protein Aggregation 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer’s, Parkinson’s, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig’s disease), Huntington’s, and type II (mature onset) diabetes. In many cases, it has been demonstrated that conformational change and aggregation can occur outside living cells and complex biochemical networks. Hence, approaches from materials and physical science have enhanced our understanding of the role of protein aggregation in these diseases at the molecular and nanoscale levels. In this article, we will review what is known about these protein structures from the perspective of materials science, focusing on the details of emergent oligomeric and nanotube-like structures, their interactions with model lipid bilayers, how the structures relate to observed biological phenomena, and how protein aggregation and amyloid formation can be employed for the good in biology and materials science. amyloid diseases (dpeaa)DE-He213 complex adaptive matter (dpeaa)DE-He213 emergent behavior (dpeaa)DE-He213 prion diseases (dpeaa)DE-He213 protein aggregation (dpeaa)DE-He213 protofibrils (dpeaa)DE-He213 nanotubes (dpeaa)DE-He213 nanowires (dpeaa)DE-He213 Lashuel, H. verfasserin aut Lee, K. Y. C. verfasserin aut Singh, R. R. P. verfasserin aut Enthalten in MRS bulletin Berlin : Springer, 1982 30(2005), 6 vom: Juni, Seite 452-457 (DE-627)379081628 (DE-600)2136359-6 1938-1425 nnns volume:30 year:2005 number:6 month:06 pages:452-457 https://dx.doi.org/10.1557/mrs2005.123 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_24 GBV_ILN_70 GBV_ILN_120 GBV_ILN_293 GBV_ILN_374 GBV_ILN_702 GBV_ILN_2190 GBV_ILN_4126 51.00 ASE AR 30 2005 6 06 452-457 |
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10.1557/mrs2005.123 doi (DE-627)SPR041200241 (SPR)mrs2005.123-e DE-627 ger DE-627 rakwb eng 670 ASE 51.00 bkl Cox, D. L. verfasserin aut The Materials Science of Protein Aggregation 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer’s, Parkinson’s, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig’s disease), Huntington’s, and type II (mature onset) diabetes. In many cases, it has been demonstrated that conformational change and aggregation can occur outside living cells and complex biochemical networks. Hence, approaches from materials and physical science have enhanced our understanding of the role of protein aggregation in these diseases at the molecular and nanoscale levels. In this article, we will review what is known about these protein structures from the perspective of materials science, focusing on the details of emergent oligomeric and nanotube-like structures, their interactions with model lipid bilayers, how the structures relate to observed biological phenomena, and how protein aggregation and amyloid formation can be employed for the good in biology and materials science. amyloid diseases (dpeaa)DE-He213 complex adaptive matter (dpeaa)DE-He213 emergent behavior (dpeaa)DE-He213 prion diseases (dpeaa)DE-He213 protein aggregation (dpeaa)DE-He213 protofibrils (dpeaa)DE-He213 nanotubes (dpeaa)DE-He213 nanowires (dpeaa)DE-He213 Lashuel, H. verfasserin aut Lee, K. Y. C. verfasserin aut Singh, R. R. P. verfasserin aut Enthalten in MRS bulletin Berlin : Springer, 1982 30(2005), 6 vom: Juni, Seite 452-457 (DE-627)379081628 (DE-600)2136359-6 1938-1425 nnns volume:30 year:2005 number:6 month:06 pages:452-457 https://dx.doi.org/10.1557/mrs2005.123 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_24 GBV_ILN_70 GBV_ILN_120 GBV_ILN_293 GBV_ILN_374 GBV_ILN_702 GBV_ILN_2190 GBV_ILN_4126 51.00 ASE AR 30 2005 6 06 452-457 |
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10.1557/mrs2005.123 doi (DE-627)SPR041200241 (SPR)mrs2005.123-e DE-627 ger DE-627 rakwb eng 670 ASE 51.00 bkl Cox, D. L. verfasserin aut The Materials Science of Protein Aggregation 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer’s, Parkinson’s, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig’s disease), Huntington’s, and type II (mature onset) diabetes. In many cases, it has been demonstrated that conformational change and aggregation can occur outside living cells and complex biochemical networks. Hence, approaches from materials and physical science have enhanced our understanding of the role of protein aggregation in these diseases at the molecular and nanoscale levels. In this article, we will review what is known about these protein structures from the perspective of materials science, focusing on the details of emergent oligomeric and nanotube-like structures, their interactions with model lipid bilayers, how the structures relate to observed biological phenomena, and how protein aggregation and amyloid formation can be employed for the good in biology and materials science. amyloid diseases (dpeaa)DE-He213 complex adaptive matter (dpeaa)DE-He213 emergent behavior (dpeaa)DE-He213 prion diseases (dpeaa)DE-He213 protein aggregation (dpeaa)DE-He213 protofibrils (dpeaa)DE-He213 nanotubes (dpeaa)DE-He213 nanowires (dpeaa)DE-He213 Lashuel, H. verfasserin aut Lee, K. Y. C. verfasserin aut Singh, R. R. P. verfasserin aut Enthalten in MRS bulletin Berlin : Springer, 1982 30(2005), 6 vom: Juni, Seite 452-457 (DE-627)379081628 (DE-600)2136359-6 1938-1425 nnns volume:30 year:2005 number:6 month:06 pages:452-457 https://dx.doi.org/10.1557/mrs2005.123 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_24 GBV_ILN_70 GBV_ILN_120 GBV_ILN_293 GBV_ILN_374 GBV_ILN_702 GBV_ILN_2190 GBV_ILN_4126 51.00 ASE AR 30 2005 6 06 452-457 |
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10.1557/mrs2005.123 doi (DE-627)SPR041200241 (SPR)mrs2005.123-e DE-627 ger DE-627 rakwb eng 670 ASE 51.00 bkl Cox, D. L. verfasserin aut The Materials Science of Protein Aggregation 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer’s, Parkinson’s, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig’s disease), Huntington’s, and type II (mature onset) diabetes. In many cases, it has been demonstrated that conformational change and aggregation can occur outside living cells and complex biochemical networks. Hence, approaches from materials and physical science have enhanced our understanding of the role of protein aggregation in these diseases at the molecular and nanoscale levels. In this article, we will review what is known about these protein structures from the perspective of materials science, focusing on the details of emergent oligomeric and nanotube-like structures, their interactions with model lipid bilayers, how the structures relate to observed biological phenomena, and how protein aggregation and amyloid formation can be employed for the good in biology and materials science. amyloid diseases (dpeaa)DE-He213 complex adaptive matter (dpeaa)DE-He213 emergent behavior (dpeaa)DE-He213 prion diseases (dpeaa)DE-He213 protein aggregation (dpeaa)DE-He213 protofibrils (dpeaa)DE-He213 nanotubes (dpeaa)DE-He213 nanowires (dpeaa)DE-He213 Lashuel, H. verfasserin aut Lee, K. Y. C. verfasserin aut Singh, R. R. P. verfasserin aut Enthalten in MRS bulletin Berlin : Springer, 1982 30(2005), 6 vom: Juni, Seite 452-457 (DE-627)379081628 (DE-600)2136359-6 1938-1425 nnns volume:30 year:2005 number:6 month:06 pages:452-457 https://dx.doi.org/10.1557/mrs2005.123 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_24 GBV_ILN_70 GBV_ILN_120 GBV_ILN_293 GBV_ILN_374 GBV_ILN_702 GBV_ILN_2190 GBV_ILN_4126 51.00 ASE AR 30 2005 6 06 452-457 |
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10.1557/mrs2005.123 doi (DE-627)SPR041200241 (SPR)mrs2005.123-e DE-627 ger DE-627 rakwb eng 670 ASE 51.00 bkl Cox, D. L. verfasserin aut The Materials Science of Protein Aggregation 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer’s, Parkinson’s, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig’s disease), Huntington’s, and type II (mature onset) diabetes. In many cases, it has been demonstrated that conformational change and aggregation can occur outside living cells and complex biochemical networks. Hence, approaches from materials and physical science have enhanced our understanding of the role of protein aggregation in these diseases at the molecular and nanoscale levels. In this article, we will review what is known about these protein structures from the perspective of materials science, focusing on the details of emergent oligomeric and nanotube-like structures, their interactions with model lipid bilayers, how the structures relate to observed biological phenomena, and how protein aggregation and amyloid formation can be employed for the good in biology and materials science. amyloid diseases (dpeaa)DE-He213 complex adaptive matter (dpeaa)DE-He213 emergent behavior (dpeaa)DE-He213 prion diseases (dpeaa)DE-He213 protein aggregation (dpeaa)DE-He213 protofibrils (dpeaa)DE-He213 nanotubes (dpeaa)DE-He213 nanowires (dpeaa)DE-He213 Lashuel, H. verfasserin aut Lee, K. Y. C. verfasserin aut Singh, R. R. P. verfasserin aut Enthalten in MRS bulletin Berlin : Springer, 1982 30(2005), 6 vom: Juni, Seite 452-457 (DE-627)379081628 (DE-600)2136359-6 1938-1425 nnns volume:30 year:2005 number:6 month:06 pages:452-457 https://dx.doi.org/10.1557/mrs2005.123 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_24 GBV_ILN_70 GBV_ILN_120 GBV_ILN_293 GBV_ILN_374 GBV_ILN_702 GBV_ILN_2190 GBV_ILN_4126 51.00 ASE AR 30 2005 6 06 452-457 |
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The Materials Science of Protein Aggregation |
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Abstract Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer’s, Parkinson’s, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig’s disease), Huntington’s, and type II (mature onset) diabetes. In many cases, it has been demonstrated that conformational change and aggregation can occur outside living cells and complex biochemical networks. Hence, approaches from materials and physical science have enhanced our understanding of the role of protein aggregation in these diseases at the molecular and nanoscale levels. In this article, we will review what is known about these protein structures from the perspective of materials science, focusing on the details of emergent oligomeric and nanotube-like structures, their interactions with model lipid bilayers, how the structures relate to observed biological phenomena, and how protein aggregation and amyloid formation can be employed for the good in biology and materials science. |
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Abstract Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer’s, Parkinson’s, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig’s disease), Huntington’s, and type II (mature onset) diabetes. In many cases, it has been demonstrated that conformational change and aggregation can occur outside living cells and complex biochemical networks. Hence, approaches from materials and physical science have enhanced our understanding of the role of protein aggregation in these diseases at the molecular and nanoscale levels. In this article, we will review what is known about these protein structures from the perspective of materials science, focusing on the details of emergent oligomeric and nanotube-like structures, their interactions with model lipid bilayers, how the structures relate to observed biological phenomena, and how protein aggregation and amyloid formation can be employed for the good in biology and materials science. |
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Abstract Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer’s, Parkinson’s, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig’s disease), Huntington’s, and type II (mature onset) diabetes. In many cases, it has been demonstrated that conformational change and aggregation can occur outside living cells and complex biochemical networks. Hence, approaches from materials and physical science have enhanced our understanding of the role of protein aggregation in these diseases at the molecular and nanoscale levels. In this article, we will review what is known about these protein structures from the perspective of materials science, focusing on the details of emergent oligomeric and nanotube-like structures, their interactions with model lipid bilayers, how the structures relate to observed biological phenomena, and how protein aggregation and amyloid formation can be employed for the good in biology and materials science. |
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