CSHL 2014 Molecular Chaperones & Stress Response Conference

CSHL 2014 分子伴侣

• 批准号: 8651595
• 负责人: DAVID J. STEWART
• 金额: $ 3.01万
• 依托单位: COLD SPRING HARBOR LABORATORY
• 依托单位国家: 美国
• 财政年份: 2014
• 资助国家: 美国
• 起止时间: 2014-04-01 至 2015-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8651595
• 关键词: Affect; Aging; Aging-Related Process; Alzheimer' s Disease; Amino Acids; Amyloidosis; Animal Model; Area; Attention; Basic Science; Biogenesis; Biomedical Research; Businesses; Cell physiology; Cells; Characteristics; Communicable Diseases; Complex; Data; Degradation Pathway; Development; Diabetes Mellitus; Discipline; Disease; Ensure; Environment; Equilibrium; Evaluation; Explosion; Faculty; Failure; Feedback; Financial Support; Fostering; Future; General Population; Goals; Health; Heart Diseases; Heat shock proteins; Heat-Shock Response; Homeostasis; Hormones; Humanities; International; Investments; Knowledge; Laboratories; Life; Malignant Neoplasms; Measures; Metabolic Diseases; Metabolism; Methods; Molecular Chaperones; Molecular Machines; Neurodegenerative Disorders; Oral; Organism; Parkinson Disease; Participant; Pathway Analysis; Pathway interactions; Peptide Hydrolases; Physiology; Play; Polymers; Postdoctoral Fellow; Prion Diseases; Process; Protein Biosynthesis; Proteins; Quality Control; Questionnaires; Recording of previous events; Research Institute; Research Personnel; Ribosomes; Role; Schedule; Science; Scientist; Signal Transduction; Slide; Stress; Thinking; Time; Translating; Work; abstracting; age related; base; biological adaptation to stress; cell type; clinically relevant; graduate student; improved; in vivo; insight; interest; lectures; meetings; normal aging; novel; novel strategies; polypeptide; posters; protein aggregate; protein aggregation; protein degradation; protein folding; protein function; protein misfolding; repaired; repository; response; success; symposium

DESCRIPTION (provided by applicant): This proposal is a request for partial financial support for a meeting on Molecular Chaperones and Stress Responses to be held at Cold Spring Harbor Laboratory from April 29 - May 3, 2014. This meeting is the premier international format for presentation of new results in this area, and is attended by representatives from virtually every major laboratory in the field. The explosion of new information on how the folded state of proteins is acquired and maintained in vivo and the involvement of this process in an increasing number of disease states and in normal aging guarantees the excitement of this meeting. Because of the recent developments that have identified new and emerging molecular machines and their mechanism of action, there will be two session devoted to mechanistic insight of protein folding machines. Additionally, it is becoming more clear that these machines do not work in isolation, but are orchestrated in a network of folding machineries. Therefore, for the first time we will have a session devoted to network evaluation of protein folding. Protein misfolding and disease will be heavily represented at the meeting and emerging principles that suggest the spread of misfolded disease causing proteins will be predominantly displayed and discussed in it own session. The diverse protein quality control strategies used by a cell to ensure the integrity of the secretory pathway during times of protein folding stress will be represented as well as a new emerging topic on spatial quality control within a cell. The field of heat shock proteins and molecular chaperones has grown rapidly and draws interest not only from traditional scientific disciplines in the basic sciences but also from numerous areas of biomedical research including neurodegenerative disease, infectious diseases, cancer, heart disease and aging. The meeting will include nine lecture sessions and three poster sessions. The proposed sessions include: 1) Protein Folding machines, 2) Protein folding machines 2, 3) Networks of protein homeostasis, 4) Spatial quality control, 5) Protein misfolding diseases - infectious spreading, 6) ER quality control, 7) Protein degradation pathways, 8) Protein synthesis, 9) Functional aggregation. Each session will consist of eight to nine oral presentations and will be chaired by an invited speaker. A maximum of two additional speakers will be pre-invited per session and the remainder will be selected from submitted abstracts. This balance of talks allows the meeting to feature presentations by leading scientists, to be responsive to exciting new developments, to encourage diverse participation and to recognize new investigators.

描述（由申请人提供）：本提案是为将于2014年4月29日至5月3日在冷泉港实验室举行的分子伴侣和应激反应会议提供部分资金支持的请求。该会议是介绍该领域新成果的首要国际形式，几乎所有主要实验室的代表都参加了该会议。关于蛋白质折叠状态如何在体内获得和维持的新信息的爆炸，以及这一过程在越来越多的疾病状态和正常衰老中的参与，保证了这次会议的兴奋。由于最近的发展已经确定了新的和新兴的分子机器及其作用机制，将有两个会议专门讨论蛋白质折叠机的机械见解。此外，越来越清楚的是，这些机器并不是孤立工作的，而是在一个折叠机器网络中精心安排的。因此，我们将第一次专门讨论蛋白质折叠的网络评估。蛋白质错误折叠和疾病将在会议上有大量的代表，而新出现的原则表明错误折叠的疾病引起的蛋白质的传播将主要在会议上展示和讨论。不同的蛋白质质量控制策略，用于细胞，以确保在蛋白质折叠应力的时间分泌途径的完整性，将代表以及一个新出现的主题空间质量控制细胞内。热休克蛋白和分子伴侣领域发展迅速，不仅引起了基础科学传统学科的兴趣，而且引起了包括神经退行性疾病、传染病、癌症、心脏病和衰老在内的众多生物医学研究领域的兴趣。会议将包括九个讲座和三个海报会议。拟议的会议包括：1）蛋白质折叠机，2）蛋白质折叠机2，3）蛋白质稳态网络，4）空间质量控制，5）蛋白质错误折叠疾病-感染性传播，6）ER质量控制，7）蛋白质降解途径，8）蛋白质合成，9）功能聚集。每场会议将包括八至九次口头发言，并将由一名特邀发言者主持。每届会议最多将预先邀请两名发言者，其余发言者将从提交的摘要中选出。这种会谈的平衡使会议能够由领先的科学家进行演讲，对令人兴奋的新发展做出反应，鼓励多元化的参与并认识新的研究者。