课题基金 / 基金详情

GORDON CONFERENCE:HORMONAL & NEURAL PEPTIDE BIOSYNTHESIS

GORDON CONFERENCE:HORMONAL & NEURAL PEPTIDE BIOSYNTHESIS
戈登会议:荷尔蒙
批准号:
6159568
负责人:
ROBERTA S. FULLER
金额:
$0.5万
依托单位:
依托单位国家:
美国
项目类别:
财政年份:
2000
资助国家:
美国
项目状态:
已结题
起止时间:
2000-07-01 至 2001-06-30

项目摘要

项目成果

ROBERTA S. FULLER的其他基金

相关文献

中文摘要
翻译
描述(取自应用程序) 生物活性多肽作为信号分子具有不同的功能,在 神经和内分泌生理学以及在形态发生和发育过程中。这个 从较大的前体蛋白中产生小肽 分泌途径的传递,有时来自胞质前体, 涉及多个翻译后修改,包括Endo-and 外源蛋白分解、氧化裂解(C-末端“酰胺化”)、乙酰化和 内酯形成等。在过去的二十年里,活跃的地区 研究已经从识别多肽前体转移到, 多蛋白等对加工过程中涉及的酶的鉴定 酶的特异性、作用机制和结构的反应和研究 酵素。加工酶对底物前体的作用 分泌途径的管腔结构域清楚地表明,对 两者的分拣、运输和本地化的机制和调控 可溶性和膜蛋白是理解生物合成的关键。 信号肽。对编码加工酶的基因的获取使它成为 有可能启动遗传学方法来开始阐明 这些酶在哺乳动物中的生理作用。这些研究得到了补充 通过简单的真核系统:单细胞真核生物,如酵母和 原生动物和无脊椎后生动物,如果蝇和线虫。 类似的加工反应继续对 菲尔德。 这是第四个戈登研究项目的部分资助申请 激素和神经肽生物合成会议将于7月16-21日举行, 2000年,在密歇根州新伦敦的科尔比-索耶学院学习。在传统上, 此前的三次会议,本次会议将是多学科的,带来 来自不同领域的科学家汇聚一堂,从酶学到结构学 从生物学到细胞生物学,从神经生物学到遗传学和生理学。在 与此同时,会议主题和演讲者将被选为准确关注的焦点 多肽合成和分泌中的重要和当前问题 激素、神经肽及相关分子。美国国立卫生研究院被要求提供资金 支持10名初级教员、研究员和 将在会议期间发表平台演讲的学生。至少6个 此支持的接受者将从参加会议的申请者中选择 已经提交了摘要,并要求考虑将其作为平台 说吧。奖项的获奖者将由副主席与 与组委会成员进行交流。如果没有单独的资金来源, 我们将无法为这个奖项计划提供财政支持。
英文摘要
DESCRIPTION (taken from the application) Bioactive peptides serve diverse functions as signaling molecules, both in neural and endocrine physiology and during morphogenesis and development. The generation of small peptides from larger precursor proteins during their transit of the secretory pathway, or sometimes from cytosolic precursors, involves multiple post-translational modifications that include endo- and exo-proteolysis, oxidative cleavage (C-terminal "amidation"), acetylation, and lactone formation, among others. In the past two decades, active areas of research have moved from the identification of peptide precursors, polyproteins, etc., to the identification of the enzymes involved in processing reactions and studies of the specificity, mechanism and structures of the enzymes. The action of processing enzymes on substrate precursors within the lumenal domain of the secretory pathway has made it clear that understanding mechanisms and regulation of sorting, transport and localization of both soluble and membrane proteins is crucial to understanding the biosynthesis of signaling peptides. Access to the genes encoding processing enzymes has made it possible to initiate genetic approaches to begin to elucidate the precise physiological roles of these enzymes in mammals. These studies are complemented by simple eukaryotic systems: unicellular eukaryotes such as yeast and protozoans and invertebrate metazoans such as Drosophila and C. elegans. Analogous processing reactions continue to be of comparative interest to the field. This is an application for partial support for the fourth Gordon Research Conference on Hormonal and Neural Peptide Biosynthesis, to be held July 16-21, 2000, at Colby-Sawyer College in New London, NH. In the tradition of the previous three meetings, this meeting will be multi-disciplinary, bringing together scientists from diverse fields, ranging from enzymology and structural biology to cell biology and neurobiology to genetics and physiology. At the same time, the session topics and speakers will be chosen to focus precisely on the vital and current issues in the synthesis and secretion of peptide hormones, neuropeptides and related molecules. NIH funding is requested to support the travel, registration and lodging of 10 junior faculty, fellows and students who will give platform presentations during the meeting. At least 6 recipients of this support will be chosen from applicants to the meeting who have submitted abstracts and requested that they be considered for a platform talk. Recipients of the awards will be chosen by the Vice Chair in conjunction with members of the organizing committee. Without a separate source of funding, we would be unable to provide financial support for this Awards program.
期刊论文(0)
专著(0)
科研奖励(0)
会议论文
Nikon TiE Motorized Microscope System For 3D Image Acquisition, Deconvolution, Li
GOLGI TARGETING AND RETENTION OF YEAST KEX2 PROTEASE
Golgi Targeting and Retention of Yeast Kex2 Protease
Golgi Targeting and Retention of Yeast Kex2 Protease