Controlling the Cell Cycle: Introduction - 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 1: Controlling the Cell Cycle: Introduction
Cells reproduce by duplicating their chromosomes and other components and then distributing them into a pair of genetically identical daughter cells. This series of events is called the cell cycle. In the first part of this lecture, I provide a general overview of the cell-cycle control system, a complex regulatory network that guides the cell through the steps of cell division. I briefly describe the major components of this regulatory system and how they fit together to form a series of biochemical switches that trigger cell-cycle events at the correct time and in the correct order.
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Controlling the Cell Cycle: Cdk Substrates - 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 2: Controlling the Cell Cycle: Cdk Substrates
Cyclin-dependent kinases (Cdks) are the central components of the control system that initiates the events of the cell cycle. In the second part of this lecture, I discuss my laboratory's efforts to address the problem of how the Cdks trigger cell-cycle events. I describe our methods for identifying the protein substrates of the Cdks, and I discuss how these studies have led to important clues about how Cdks find their correct targets in the cell and how phosphorylation of those targets governs their function.
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.
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
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.
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.
Introducing the EnSight™ Multimode Plate Reader from PerkinElmer
PerkinElmer's EnSight Multimode Plate Reader is the first benchtop system to offer well-imaging alongside label-free and labeled detection technologies - for a whole new perspective on your research. For more information, please visit the EnSight website - http://bit.ly/T4IDPh
PKI Mantra Intro 2015
The Mantra™ quantitative pathology workstation lets you visualize, quantify, and phenotype multiple types of immune cells simultaneously in intact FFPE tissue sections for cancer immunology research. Mantra allows you to maintain tissue morphology to help better understand the types and roles of cells within the tumor and tumor microenvironment. The system comes with powerful inForm® Tissue Finder™ advanced image analysis software that features user-trainable algorithms for automatic recognition of specific tissue and cell types, as well as per-cell analysis of biomarker expression and phenotyping to differentiate among cell types. Pathology Views™ creates familiar-looking brightfield (H&E, DAB, hematoxylin) renderings from original multi-label fluorescence images. PerkinElmer’s cancer immunology workflow has been validated using Opal™ reagent kits. Opal methodology enables specific staining of multiple tissue biomarkers reaching up to 6-plex and beyond in a single tissue section. Learn more: http://www.perkinelmer.com/catalog/pr...
Introducing the Opera Phenix™ High Content Screening System
Introducing Opera Phenix™, a next-generation, confocal, high content screening system designed for high-throughput, phenotypic screening and assays using complex disease models, such as primary cells and microtissues. Find out more at http://bit.ly/1eZM4Ok.
Metalloproteins and the Environment
B12定位在CH3转移cfesp如何？摆动夹紧动作B12 17 Å.复杂我们守在这里 。你为什么需要140（或220）为转移甲基？在一部分，以形成一个稳定的框架，以允许这些大；构象变化是催化的关键。