CSHL 2014 Molecular Chaperones & Stress Response Conference
CSHL 2014 分子伴侣
基本信息
- 批准号:8651595
- 负责人:
- 金额:$ 3.01万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 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:
- 关键词:AffectAgingAging-Related ProcessAlzheimer&aposs DiseaseAmino AcidsAmyloidosisAnimal ModelAreaAttentionBasic ScienceBiogenesisBiomedical ResearchBusinessesCell physiologyCellsCharacteristicsCommunicable DiseasesComplexDataDegradation PathwayDevelopmentDiabetes MellitusDisciplineDiseaseEnsureEnvironmentEquilibriumEvaluationExplosionFacultyFailureFeedbackFinancial SupportFosteringFutureGeneral PopulationGoalsHealthHeart DiseasesHeat shock proteinsHeat-Shock ResponseHomeostasisHormonesHumanitiesInternationalInvestmentsKnowledgeLaboratoriesLifeMalignant NeoplasmsMeasuresMetabolic DiseasesMetabolismMethodsMolecular ChaperonesMolecular MachinesNeurodegenerative DisordersOralOrganismParkinson DiseaseParticipantPathway AnalysisPathway interactionsPeptide HydrolasesPhysiologyPlayPolymersPostdoctoral FellowPrion DiseasesProcessProtein BiosynthesisProteinsQuality ControlQuestionnairesRecording of previous eventsResearch InstituteResearch PersonnelRibosomesRoleScheduleScienceScientistSignal TransductionSlideStressThinkingTimeTranslatingWorkabstractingage relatedbasebiological adaptation to stresscell typeclinically relevantgraduate studentimprovedin vivoinsightinterestlecturesmeetingsnormal agingnovelnovel strategiespolypeptidepostersprotein aggregateprotein aggregationprotein degradationprotein foldingprotein functionprotein misfoldingrepairedrepositoryresponsesuccesssymposium
项目摘要
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):该提案是为了在2014年4月29日至5月3日在冷春港实验室举行的有关分子伴侣和压力响应会议的部分财政支持的请求。这次会议是最重要的国际格式。在该领域的新结果介绍,并由该领域的每个主要实验室的代表参加。关于如何在体内获取和维持蛋白质折叠状态的新信息的爆炸以及该过程参与越来越多的疾病状态,并且在正常衰老中保证了这次会议的兴奋。由于最近确定了新的和新兴的分子机器及其作用机理的发展,将有两个专门用于蛋白质折叠机的机械洞察力。此外,越来越清楚的是,这些机器不能孤立地工作,而是在折叠机器网络中精心策划的。因此,我们将首次举办一个专门用于蛋白质折叠网络评估的会话。蛋白质错误折叠和疾病将在会议上大量代表,并在其自己的会议上将主要显示并讨论引起蛋白质错误折叠疾病的传播的新兴原则。细胞使用的各种蛋白质质量控制策略将代表蛋白质折叠应力期间分泌途径的完整性,以及在细胞内空间质量控制方面的一个新的新兴主题。热休克蛋白和分子伴侣的领域迅速发展,不仅从基本科学中的传统科学学科中引起了人们的兴趣,而且还来自许多生物医学研究领域,包括神经退行性疾病,感染性疾病,癌症,心脏病,心脏病和衰老。会议将包括九次讲座和三个海报会议。提议的会话包括: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。每个会议将由八到九个口头演讲组成,并由受邀发言人主持。每个会话最多将预先启动两个扬声器,其余的将从提交的摘要中选择。谈话的平衡使会议能够通过领先的科学家进行演讲,对令人兴奋的新发展做出反应,以鼓励各种参与并认可新的调查人员。
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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DAVID J. STEWART其他文献
DAVID J. STEWART的其他文献
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