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Change History
Changed By: techman
Change Date: January 14, 2011 05:26PM
[Physics] [Molecular Biology] Physicists at Academia Sinica Identify Factors Governing Protein Aggregation, a Hallmark of Neurodegenerative Diseases
Change Date: January 14, 2011 05:26PM
[Physics] [Molecular Biology] Physicists at Academia Sinica Identify Factors Governing Protein Aggregation, a Hallmark of Neurodegenerative Diseases
[Physics] [Molecular Biology] Physicists at Academia Sinica Identify Factors Governing Protein Aggregation, a Hallmark of Neurodegenerative Diseases (<a href=http://mepopedia.com/forum/read.php?127,10499>Chinese Version</a>)
<i>Academia Sinica Newsletter</i> (2011/01/11) Dr. Chin-Kun HU, Research Fellow at Laboratory of Statistical and Computational Physics of the Institute of Physics at Academia Sinica, and his collaborators have recently identified a number of key factors governing protein aggregation. Increasing understanding of protein aggregation is important as protein aggregation is thought to play an important role in the onset and progression of neurodegenerative diseases such as Alzheimers disease and Parkinsons disease. The groups results have been published in a series of papers in <i>Physical Review Letters</i> (<i>PRL</i>) and <i>Journal of the Physical Society of Japan</i> (<i>JPSJ</i>).
Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Huntington's disease, spinocerebellar atrophy and frontotemporal lobar degeneration are caused by progressive loss of structure and function of neurons (including death of neurons) due to protein aggregation. For example, Alzheimer's disease is thought to be related to the aggregation of A帣40 (a protein made up of 40 amino acids) and A帣42 (a protein made up of 42 amino acids), while Huntington's disease and spinocerebellar atrophy are related to aggregation of PolyQ (a protein with a long sequence of the amino acid glutamine).
In a study published in <i>Physical Review Letters</i> on 19 November, 2010, Dr. Chin-Kun HU and his collaborators based in Poland, Vietnam and the US, used a lattice model to study the aggregation rates of proteins. They found that the probability of a protein sequence appearing in an aggregated conformation can be used to determine the temperature at which the protein can aggregate most easily. They also found a correlation between the time taken for the protein to aggregate and the strength of interactions between charged amino acids, which is consistent with previous experimental observations.
In another four articles published in the <i>Journal of the Physical Society of Japan</i> in February, May and October 2010, Dr. HU, together with Dr. Wen-Jong MA (now a member of the faculty at the Graduate Institute of Applied Physics, National Chengchi University, Taiwan), employed molecular dynamics to study relaxation and aggregation of protein chains under various conditions. They found that when the bending-angle dependent and torsion-angle dependent interactions are zero or very small, the protein chains tend to aggregate at lower temperatures. This finding has contributed to understanding the aggregation of A帣40 and A帣42 in Alzheimer's disease.
As the next step of the project, Dr. HU said that he and his collaborators would like to combine the results from computer simulations and analytic calculations with experimental data in an effort to formulate a general theory of protein aggregation to enable prediction of the influence of environment, mutation and drugs on protein aggregation rates and also predict the conditions most likely to prohibit protein aggregation.
Related Websites:
<a href=http://prl.aps.org/abstract/PRL/v105/i21/e218101>http://prl.aps.org/abstract/PRL/v105/i21/e218101</a>
<a href=http://jpsj.ipap.jp/>http://jpsj.ipap.jp/</a>
Media contacts:
Dr. Chin-Kun HU, Institute of Physics, Academia Sinica
(Tel) +886-2-2789-6720
Fang-Hsun YEH, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8820, (Fax) +886-2-2782-1551, (M) 0922-036-691
E-mail: hongsum@gate.sinica.edu.tw
Mei-Hui LIN, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8821, (Fax) +886-2-2782-1551, (M) 0921-845-234
E-mail: mhlin313@gate.sinica.edu.tw
Reference:
<a href=http://www.sinica.edu.tw/manage/gatenews/showsingle.php?_op=?rid:3798%26isEnglish:1>Academia Sinica Newsletter 2011/01/11</a>
<i>Academia Sinica Newsletter</i> (2011/01/11) Dr. Chin-Kun HU, Research Fellow at Laboratory of Statistical and Computational Physics of the Institute of Physics at Academia Sinica, and his collaborators have recently identified a number of key factors governing protein aggregation. Increasing understanding of protein aggregation is important as protein aggregation is thought to play an important role in the onset and progression of neurodegenerative diseases such as Alzheimers disease and Parkinsons disease. The groups results have been published in a series of papers in <i>Physical Review Letters</i> (<i>PRL</i>) and <i>Journal of the Physical Society of Japan</i> (<i>JPSJ</i>).
Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Huntington's disease, spinocerebellar atrophy and frontotemporal lobar degeneration are caused by progressive loss of structure and function of neurons (including death of neurons) due to protein aggregation. For example, Alzheimer's disease is thought to be related to the aggregation of A帣40 (a protein made up of 40 amino acids) and A帣42 (a protein made up of 42 amino acids), while Huntington's disease and spinocerebellar atrophy are related to aggregation of PolyQ (a protein with a long sequence of the amino acid glutamine).
In a study published in <i>Physical Review Letters</i> on 19 November, 2010, Dr. Chin-Kun HU and his collaborators based in Poland, Vietnam and the US, used a lattice model to study the aggregation rates of proteins. They found that the probability of a protein sequence appearing in an aggregated conformation can be used to determine the temperature at which the protein can aggregate most easily. They also found a correlation between the time taken for the protein to aggregate and the strength of interactions between charged amino acids, which is consistent with previous experimental observations.
In another four articles published in the <i>Journal of the Physical Society of Japan</i> in February, May and October 2010, Dr. HU, together with Dr. Wen-Jong MA (now a member of the faculty at the Graduate Institute of Applied Physics, National Chengchi University, Taiwan), employed molecular dynamics to study relaxation and aggregation of protein chains under various conditions. They found that when the bending-angle dependent and torsion-angle dependent interactions are zero or very small, the protein chains tend to aggregate at lower temperatures. This finding has contributed to understanding the aggregation of A帣40 and A帣42 in Alzheimer's disease.
As the next step of the project, Dr. HU said that he and his collaborators would like to combine the results from computer simulations and analytic calculations with experimental data in an effort to formulate a general theory of protein aggregation to enable prediction of the influence of environment, mutation and drugs on protein aggregation rates and also predict the conditions most likely to prohibit protein aggregation.
Related Websites:
<a href=http://prl.aps.org/abstract/PRL/v105/i21/e218101>http://prl.aps.org/abstract/PRL/v105/i21/e218101</a>
<a href=http://jpsj.ipap.jp/>http://jpsj.ipap.jp/</a>
Media contacts:
Dr. Chin-Kun HU, Institute of Physics, Academia Sinica
(Tel) +886-2-2789-6720
Fang-Hsun YEH, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8820, (Fax) +886-2-2782-1551, (M) 0922-036-691
E-mail: hongsum@gate.sinica.edu.tw
Mei-Hui LIN, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8821, (Fax) +886-2-2782-1551, (M) 0921-845-234
E-mail: mhlin313@gate.sinica.edu.tw
Reference:
<a href=http://www.sinica.edu.tw/manage/gatenews/showsingle.php?_op=?rid:3798%26isEnglish:1>Academia Sinica Newsletter 2011/01/11</a>
Changed By: techman
Change Date: January 14, 2011 05:20PM
[Physics] Physicists at Academia Sinica Identify Factors Governing Protein Aggregation, a Hallmark of Neurodegenerative Diseases
Change Date: January 14, 2011 05:20PM
[Physics] Physicists at Academia Sinica Identify Factors Governing Protein Aggregation, a Hallmark of Neurodegenerative Diseases
[Physics] Physicists at Academia Sinica Identify Factors Governing Protein Aggregation, a Hallmark of Neurodegenerative Diseases (<a href=http://mepopedia.com/forum/read.php?127,10499>Chinese Version</a>)
<i>Academia Sinica Newsletter</i> (2011/01/11) Dr. Chin-Kun HU, Research Fellow at Laboratory of Statistical and Computational Physics of the Institute of Physics at Academia Sinica, and his collaborators have recently identified a number of key factors governing protein aggregation. Increasing understanding of protein aggregation is important as protein aggregation is thought to play an important role in the onset and progression of neurodegenerative diseases such as Alzheimers disease and Parkinsons disease. The groups results have been published in a series of papers in <i>Physical Review Letters</i> (<i>PRL</i>) and <i>Journal of the Physical Society of Japan</i> (<i>JPSJ</i>).
Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Huntington's disease, spinocerebellar atrophy and frontotemporal lobar degeneration are caused by progressive loss of structure and function of neurons (including death of neurons) due to protein aggregation. For example, Alzheimer's disease is thought to be related to the aggregation of A帣40 (a protein made up of 40 amino acids) and A帣42 (a protein made up of 42 amino acids), while Huntington's disease and spinocerebellar atrophy are related to aggregation of PolyQ (a protein with a long sequence of the amino acid glutamine).
In a study published in <i>Physical Review Letters</i> on 19 November, 2010, Dr. Chin-Kun HU and his collaborators based in Poland, Vietnam and the US, used a lattice model to study the aggregation rates of proteins. They found that the probability of a protein sequence appearing in an aggregated conformation can be used to determine the temperature at which the protein can aggregate most easily. They also found a correlation between the time taken for the protein to aggregate and the strength of interactions between charged amino acids, which is consistent with previous experimental observations.
In another four articles published in the <i>Journal of the Physical Society of Japan</i> in February, May and October 2010, Dr. HU, together with Dr. Wen-Jong MA (now a member of the faculty at the Graduate Institute of Applied Physics, National Chengchi University, Taiwan), employed molecular dynamics to study relaxation and aggregation of protein chains under various conditions. They found that when the bending-angle dependent and torsion-angle dependent interactions are zero or very small, the protein chains tend to aggregate at lower temperatures. This finding has contributed to understanding the aggregation of A帣40 and A帣42 in Alzheimer's disease.
As the next step of the project, Dr. HU said that he and his collaborators would like to combine the results from computer simulations and analytic calculations with experimental data in an effort to formulate a general theory of protein aggregation to enable prediction of the influence of environment, mutation and drugs on protein aggregation rates and also predict the conditions most likely to prohibit protein aggregation.
Related Websites:
<a href=http://prl.aps.org/abstract/PRL/v105/i21/e218101>http://prl.aps.org/abstract/PRL/v105/i21/e218101</a>
<a href=http://jpsj.ipap.jp/>http://jpsj.ipap.jp/</a>
Media contacts:
Dr. Chin-Kun HU, Institute of Physics, Academia Sinica
(Tel) +886-2-2789-6720
Fang-Hsun YEH, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8820, (Fax) +886-2-2782-1551, (M) 0922-036-691
E-mail: hongsum@gate.sinica.edu.tw
Mei-Hui LIN, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8821, (Fax) +886-2-2782-1551, (M) 0921-845-234
E-mail: mhlin313@gate.sinica.edu.tw
Reference:
<a href=http://www.sinica.edu.tw/manage/gatenews/showsingle.php?_op=?rid:3798%26isEnglish:1>Academia Sinica Newsletter 2011/01/11</a>
<i>Academia Sinica Newsletter</i> (2011/01/11) Dr. Chin-Kun HU, Research Fellow at Laboratory of Statistical and Computational Physics of the Institute of Physics at Academia Sinica, and his collaborators have recently identified a number of key factors governing protein aggregation. Increasing understanding of protein aggregation is important as protein aggregation is thought to play an important role in the onset and progression of neurodegenerative diseases such as Alzheimers disease and Parkinsons disease. The groups results have been published in a series of papers in <i>Physical Review Letters</i> (<i>PRL</i>) and <i>Journal of the Physical Society of Japan</i> (<i>JPSJ</i>).
Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Huntington's disease, spinocerebellar atrophy and frontotemporal lobar degeneration are caused by progressive loss of structure and function of neurons (including death of neurons) due to protein aggregation. For example, Alzheimer's disease is thought to be related to the aggregation of A帣40 (a protein made up of 40 amino acids) and A帣42 (a protein made up of 42 amino acids), while Huntington's disease and spinocerebellar atrophy are related to aggregation of PolyQ (a protein with a long sequence of the amino acid glutamine).
In a study published in <i>Physical Review Letters</i> on 19 November, 2010, Dr. Chin-Kun HU and his collaborators based in Poland, Vietnam and the US, used a lattice model to study the aggregation rates of proteins. They found that the probability of a protein sequence appearing in an aggregated conformation can be used to determine the temperature at which the protein can aggregate most easily. They also found a correlation between the time taken for the protein to aggregate and the strength of interactions between charged amino acids, which is consistent with previous experimental observations.
In another four articles published in the <i>Journal of the Physical Society of Japan</i> in February, May and October 2010, Dr. HU, together with Dr. Wen-Jong MA (now a member of the faculty at the Graduate Institute of Applied Physics, National Chengchi University, Taiwan), employed molecular dynamics to study relaxation and aggregation of protein chains under various conditions. They found that when the bending-angle dependent and torsion-angle dependent interactions are zero or very small, the protein chains tend to aggregate at lower temperatures. This finding has contributed to understanding the aggregation of A帣40 and A帣42 in Alzheimer's disease.
As the next step of the project, Dr. HU said that he and his collaborators would like to combine the results from computer simulations and analytic calculations with experimental data in an effort to formulate a general theory of protein aggregation to enable prediction of the influence of environment, mutation and drugs on protein aggregation rates and also predict the conditions most likely to prohibit protein aggregation.
Related Websites:
<a href=http://prl.aps.org/abstract/PRL/v105/i21/e218101>http://prl.aps.org/abstract/PRL/v105/i21/e218101</a>
<a href=http://jpsj.ipap.jp/>http://jpsj.ipap.jp/</a>
Media contacts:
Dr. Chin-Kun HU, Institute of Physics, Academia Sinica
(Tel) +886-2-2789-6720
Fang-Hsun YEH, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8820, (Fax) +886-2-2782-1551, (M) 0922-036-691
E-mail: hongsum@gate.sinica.edu.tw
Mei-Hui LIN, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8821, (Fax) +886-2-2782-1551, (M) 0921-845-234
E-mail: mhlin313@gate.sinica.edu.tw
Reference:
<a href=http://www.sinica.edu.tw/manage/gatenews/showsingle.php?_op=?rid:3798%26isEnglish:1>Academia Sinica Newsletter 2011/01/11</a>
Original Message
雿: techmanDate: January 14, 2011 05:13PM
[Physics] Physicists at Academia Sinica Identify Factors Governing Protein Aggregation, a Hallmark of Neurodegenerative Diseases
[Physics] Physicists at Academia Sinica Identify Factors Governing Protein Aggregation, a Hallmark of Neurodegenerative Diseases (Chinese Version)
Academia Sinica Newsletter (2011/01/11) Dr. Chin-Kun HU, Research Fellow at Laboratory of Statistical and Computational Physics of the Institute of Physics at Academia Sinica, and his collaborators have recently identified a number of key factors governing protein aggregation. Increasing understanding of protein aggregation is important as protein aggregation is thought to play an important role in the onset and progression of neurodegenerative diseases such as Alzheimers disease and Parkinsons disease. The groups results have been published in a series of papers in Physical Review Letters (PRL) and Journal of the Physical Society of Japan (JPSJ).
Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Huntington's disease, spinocerebellar atrophy and frontotemporal lobar degeneration are caused by progressive loss of structure and function of neurons (including death of neurons) due to protein aggregation. For example, Alzheimer's disease is thought to be related to the aggregation of A帣40 (a protein made up of 40 amino acids) and A帣42 (a protein made up of 42 amino acids), while Huntington's disease and spinocerebellar atrophy are related to aggregation of PolyQ (a protein with a long sequence of the amino acid glutamine).
In a study published in Physical Review Letters on 19 November, 2010, Dr. Chin-Kun HU and his collaborators based in Poland, Vietnam and the US, used a lattice model to study the aggregation rates of proteins. They found that the probability of a protein sequence appearing in an aggregated conformation can be used to determine the temperature at which the protein can aggregate most easily. They also found a correlation between the time taken for the protein to aggregate and the strength of interactions between charged amino acids, which is consistent with previous experimental observations.
In another four articles published in the Journal of the Physical Society of Japan in February, May and October 2010, Dr. HU, together with Dr. Wen-Jong MA (now a member of the faculty at the Graduate Institute of Applied Physics, National Chengchi University, Taiwan), employed molecular dynamics to study relaxation and aggregation of protein chains under various conditions. They found that when the bending-angle dependent and torsion-angle dependent interactions are zero or very small, the protein chains tend to aggregate at lower temperatures. This finding has contributed to understanding the aggregation of A帣40 and A帣42 in Alzheimer's disease.
As the next step of the project, Dr. HU said that he and his collaborators would like to combine the results from computer simulations and analytic calculations with experimental data in an effort to formulate a general theory of protein aggregation to enable prediction of the influence of environment, mutation and drugs on protein aggregation rates and also predict the conditions most likely to prohibit protein aggregation.
Related Websites:
http://prl.aps.org/abstract/PRL/v105/i21/e218101
http://jpsj.ipap.jp/
Media contacts:
Dr. Chin-Kun HU, Institute of Physics, Academia Sinica
(Tel) +886-2-2789-6720
Fang-Hsun YEH, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8820, (Fax) +886-2-2782-1551, (M) 0922-036-691
E-mail: hongsum@gate.sinica.edu.tw
Mei-Hui LIN, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8821, (Fax) +886-2-2782-1551, (M) 0921-845-234
E-mail: mhlin313@gate.sinica.edu.tw
Reference:
Academia Sinica Newsletter 2011/01/11
Academia Sinica Newsletter (2011/01/11) Dr. Chin-Kun HU, Research Fellow at Laboratory of Statistical and Computational Physics of the Institute of Physics at Academia Sinica, and his collaborators have recently identified a number of key factors governing protein aggregation. Increasing understanding of protein aggregation is important as protein aggregation is thought to play an important role in the onset and progression of neurodegenerative diseases such as Alzheimers disease and Parkinsons disease. The groups results have been published in a series of papers in Physical Review Letters (PRL) and Journal of the Physical Society of Japan (JPSJ).
Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Huntington's disease, spinocerebellar atrophy and frontotemporal lobar degeneration are caused by progressive loss of structure and function of neurons (including death of neurons) due to protein aggregation. For example, Alzheimer's disease is thought to be related to the aggregation of A帣40 (a protein made up of 40 amino acids) and A帣42 (a protein made up of 42 amino acids), while Huntington's disease and spinocerebellar atrophy are related to aggregation of PolyQ (a protein with a long sequence of the amino acid glutamine).
In a study published in Physical Review Letters on 19 November, 2010, Dr. Chin-Kun HU and his collaborators based in Poland, Vietnam and the US, used a lattice model to study the aggregation rates of proteins. They found that the probability of a protein sequence appearing in an aggregated conformation can be used to determine the temperature at which the protein can aggregate most easily. They also found a correlation between the time taken for the protein to aggregate and the strength of interactions between charged amino acids, which is consistent with previous experimental observations.
In another four articles published in the Journal of the Physical Society of Japan in February, May and October 2010, Dr. HU, together with Dr. Wen-Jong MA (now a member of the faculty at the Graduate Institute of Applied Physics, National Chengchi University, Taiwan), employed molecular dynamics to study relaxation and aggregation of protein chains under various conditions. They found that when the bending-angle dependent and torsion-angle dependent interactions are zero or very small, the protein chains tend to aggregate at lower temperatures. This finding has contributed to understanding the aggregation of A帣40 and A帣42 in Alzheimer's disease.
As the next step of the project, Dr. HU said that he and his collaborators would like to combine the results from computer simulations and analytic calculations with experimental data in an effort to formulate a general theory of protein aggregation to enable prediction of the influence of environment, mutation and drugs on protein aggregation rates and also predict the conditions most likely to prohibit protein aggregation.
Related Websites:
http://prl.aps.org/abstract/PRL/v105/i21/e218101
http://jpsj.ipap.jp/
Media contacts:
Dr. Chin-Kun HU, Institute of Physics, Academia Sinica
(Tel) +886-2-2789-6720
Fang-Hsun YEH, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8820, (Fax) +886-2-2782-1551, (M) 0922-036-691
E-mail: hongsum@gate.sinica.edu.tw
Mei-Hui LIN, Office of Public Affairs, Central Office of Administration, Academia Sinica
(Tel) +886-2-2789-8821, (Fax) +886-2-2782-1551, (M) 0921-845-234
E-mail: mhlin313@gate.sinica.edu.tw
Reference:
Academia Sinica Newsletter 2011/01/11
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