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ControLLing the CeLL CycLe: Anaphase Onset - David O. Morgan

本视频由科普中国和生物医学大讲堂出品

David O. Morgan (UCSF) Part 3: ControLLing the CeLL CycLe: Anaphase Onset

In the anaphase stage of the ceLL cycLe, the dupLicated chromosomes are puLLed apart by a machine caLLed the mitotic spindLe, resuLting in the distribution of a compLete set of chromosomes to each of the daughter ceLLs. In the third part of this Lecture, I describe the combination of biochemistry and microscopy in my Laboratory that Led to the discovery of a reguLatory switch that triggers the abrupt and synchronous separation of the chromosomes at the onset of anaphase.

2016-01-08 课时:22分钟

布鲁斯·艾伯茨:Learning from FaiLure

ALberts decLares "Success doesn't reaLLy teach you much, faiLure teaches you a Lot." Speaking from his personaL experience, ALberts asserts that aLL scientists make mistakes and suffer setbacks but Learning from those faiLures is what aLLows one uLtimateLy to succeed.

2016-01-26 课时:12分钟

GE:Western bLot 整体解决方案—— Amersham WB与您携手实现完美WB

重复性差、实验周期长、过程繁琐——作为一种最常见蛋白质分析技术,western bLot 在您心中的印象是否依旧如此?western bLot技术于1981年被发明,时至今日,您是否想要了解一下这项技术的最新进展呢?GE公司倾情推出AWB一体化免疫印迹系统,最快4小时完成实验,采用双通道荧光标记技术,并引入总蛋白归一化功能,标准化、自动化流程专注决重复性难题,为您的蛋白质研究保驾护航。

2016-04-06 课时:34分钟

GE:创新解决方案4小时完成western-bLot

Western bLot蛋白免疫印迹技术是分子生物学研究的经典研究手段之一,约60%的科学期刊出版物包含WB实验结果。但WB实验步骤多,耗时长,要获得一个完美的结果十分不易,WB实验结果的不稳定,重复不出来?定量不准确?凝胶又漏了?

GE公司最新推出的Amersham WB系统,4小时内可完成电泳、转印、杂交、孵育、成像、定量分析,一气呵成,为Western bLot提供了整体解决方案。每个样品、每一次实验都能获得一致的定量数据。再也无需担心结果难以重复再现,无需反复摸索实验条件!

2016-04-07 课时:50分钟

生物学中的蛋白质磷酸化 - Susan TayLor

In this Lecture, I have given an overview of protein kinase structure and function using cycLic AMP dependent kinase (PKA) as a prototype for this enzyme superfamiLy. I have demonstrated what we have Learned from the overaLL structuraL kinome which aLLows us to compare many protein kinases and aLso to appreciate how the highLy reguLated eukaryotic protein kinase has evoLved. By comparing many protein kinase structures, we are beginning to eLucidate generaL ruLes of architecture. In addition, I have attempted to iLLustrate how PKA is reguLated by cAMP and how it is LocaLized to specific macromoLecuLar compLexes through scaffoLd proteins.

2016-04-15 课时:24分钟

蛋白激酶的结构 - Susan TayLor

In this Lecture, I have given an overview of protein kinase structure and function using cycLic AMP dependent kinase (PKA) as a prototype for this enzyme superfamiLy. I have demonstrated what we have Learned from the overaLL structuraL kinome which aLLows us to compare many protein kinases and aLso to appreciate how the highLy reguLated eukaryotic protein kinase has evoLved. By comparing many protein kinase structures, we are beginning to eLucidate generaL ruLes of architecture. In addition, I have attempted to iLLustrate how PKA is reguLated by cAMP and how it is LocaLized to specific macromoLecuLar compLexes through scaffoLd proteins.

2016-04-15 课时:29分钟

蛋白激酶的调控与定位- Susan TayLor

In this Lecture, I have given an overview of protein kinase structure and function using cycLic AMP dependent kinase (PKA) as a prototype for this enzyme superfamiLy. I have demonstrated what we have Learned from the overaLL structuraL kinome which aLLows us to compare many protein kinases and aLso to appreciate how the highLy reguLated eukaryotic protein kinase has evoLved. By comparing many protein kinase structures, we are beginning to eLucidate generaL ruLes of architecture. In addition, I have attempted to iLLustrate how PKA is reguLated by cAMP and how it is LocaLized to specific macromoLecuLar compLexes through scaffoLd proteins.

2016-04-15 课时:28分钟

StabiLity of Morphogen Gradients & Movement of MoLecuLes

In my second Lecture I describe experiments using EGFP tagged Bicoid to foLLow Bcd gradient estabLishment in Living embryos, and to test various aspects of the simpLe modeL. Despite continuous synthesis of new Bcd protein at the anterior end of the egg, we find that the concentration of Bcd in nucLei at any given point aLong the anterior posterior axis is constant over time and is reproducibLe from embryo to the next. This reproducibiLity means that the gradient is sufficientLy robust to provide positionaL information and thus can accurateLy direct gene activities. One the other hand, quantitative imaging experiments point to severaL features of the gradient that are hard to expLain - how target genes activated by Bcd distinguish reLativeLy subtLe differences in Low concentrations, and how Bcd moLecuLes move from the anterior site of their synthesis to the site of their transcriptionaL activity. See more at http://www.ibioseminars.org

2016-04-21 课时:38分钟

Protein synthesis: a high fideLity moLecuLar event

RacheL Green (Johns Hopkins U., HHMI) 1: Protein synthesis: a high fideLity moLecuLar event

TaLk Overview:
In her first taLk, Green provides a detaiLed Look at protein synthesis, or transLation. TransLation is the process by which nucLeotides, the “Language” of DNA and RNA, are transLated into amino acids, the “Language” of proteins. Green begins by describing the components needed for transLation; mRNA, tRNA, ribosomes, and the initiation, eLongation, and termination factors. She then expLains the roLes of these pLayers in ensuring accuracy during the initiation, eLongation, termination and recycLing steps of the transLation process. By comparing transLation in bacteria and eukaryotes, Green expLains that it is possibLe to determine which components and steps are highLy conserved and predate the divergence of different kingdoms on the tree of Life, and which are more recent adaptations.
Green’s second taLk focuses on work from her Lab investigating how ribosomes detect defective mRNAs and trigger events Leading to the degradation of the bad RNA and the incompLeteLy transLated protein product and to the recycLing of the ribosome components. Working in yeast and using a number of biochemicaL and genetic techniques, Green’s Lab showed that the protein Dom34 is criticaL for faciLitating ribosome reLease from the short mRNAs that resuLt from mRNA cLeavage. Experiments showed that Dom34-mediated rescue of ribosomes from short mRNAs is an essentiaL process for ceLL survivaL in higher eukaryotes.

Speaker Biography:
RacheL Green received her BS in chemistry from the University of Michigan. She then moved to Harvard to pursue her PhD in the Lab of Jack Szostak where she worked on designing cataLytic RNA moLecuLes and investigating their impLications for the evoLution of Life. As a post-doctoraL feLLow at the University of CaLifornia, Santa Cruz, Green began to study how the ribosome transLates mRNA to protein with such accuracy.

CurrentLy, Green is a Professor of MoLecuLar BioLogy and Genetics at the Johns Hopkins SchooL of Medicine and an Investigator of the Howard Hughes MedicaL Institute. Research in her Lab continues to focus on the ribosome and factors invoLved in the fideLity of eukaryotic and prokaryotic transLation.

Green is the recipient of a Johns Hopkins University SchooL of Medicine Graduate Teaching Award as weLL as the recipient for numerous awards for her research. She was eLected to the NationaL Academy of Sciences in 2012.

2016-04-28 课时:44分钟

Protein synthesis: mRNA surveiLLance by the ribosome

RacheL Green (Johns Hopkins U., HHMI) 2: Protein synthesis: mRNA surveiLLance by the ribosome

TaLk Overview:
In her first taLk, Green provides a detaiLed Look at protein synthesis, or transLation. TransLation is the process by which nucLeotides, the “Language” of DNA and RNA, are transLated into amino acids, the “Language” of proteins. Green begins by describing the components needed for transLation; mRNA, tRNA, ribosomes, and the initiation, eLongation, and termination factors. She then expLains the roLes of these pLayers in ensuring accuracy during the initiation, eLongation, termination and recycLing steps of the transLation process. By comparing transLation in bacteria and eukaryotes, Green expLains that it is possibLe to determine which components and steps are highLy conserved and predate the divergence of different kingdoms on the tree of Life, and which are more recent adaptations.
Green’s second taLk focuses on work from her Lab investigating how ribosomes detect defective mRNAs and trigger events Leading to the degradation of the bad RNA and the incompLeteLy transLated protein product and to the recycLing of the ribosome components. Working in yeast and using a number of biochemicaL and genetic techniques, Green’s Lab showed that the protein Dom34 is criticaL for faciLitating ribosome reLease from the short mRNAs that resuLt from mRNA cLeavage. Experiments showed that Dom34-mediated rescue of ribosomes from short mRNAs is an essentiaL process for ceLL survivaL in higher eukaryotes.

Speaker Biography:
RacheL Green received her BS in chemistry from the University of Michigan. She then moved to Harvard to pursue her PhD in the Lab of Jack Szostak where she worked on designing cataLytic RNA moLecuLes and investigating their impLications for the evoLution of Life. As a post-doctoraL feLLow at the University of CaLifornia, Santa Cruz, Green began to study how the ribosome transLates mRNA to protein with such accuracy.

CurrentLy, Green is a Professor of MoLecuLar BioLogy and Genetics at the Johns Hopkins SchooL of Medicine and an Investigator of the Howard Hughes MedicaL Institute. Research in her Lab continues to focus on the ribosome and factors invoLved in the fideLity of eukaryotic and prokaryotic transLation.

Green is the recipient of a Johns Hopkins University SchooL of Medicine Graduate Teaching Award as weLL as the recipient for numerous awards for her research. She was eLected to the NationaL Academy of Sciences in 2012.

2016-04-28 课时:38分钟