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Research Clusters
PostDoctoral Research
Graduate Research
Molecular Cell & Developmental Biology
225 Sinsheimer Laboratories
Phone: 831.459.4986
Fax: 831.459.3139
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MCDB POSTDOCTORAL RESEARCH
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
| Post Doctorate Researcher |
Lab |
Email |
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| Ermolenko, Dmitri |
Noller |
dmitri@biology.ucsc.edu |
| Both ribosomal subunits contain three binding sites for tRNA: the A, P and E sites. During translocation, following the formation of a new peptide bond, peptidyl-tRNA moves from the A to P and deacylated-tRNA from the P to E site, respectively. Translocation is catalyzed by elongation factor EF-G. The mechanism of ribosomal translocation remains obscure. I study a sequence of structural rearrangements of the ribosome and EF-G during translocation using biochemical methods and fluorescence resonance energy transfer (FRET)". |
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| Grate, Leslie |
Ares |
lesliegrate@comcast.net |
| As a computational biologist I study structural RNA's, splicing and alternate splicing in the Ares lab. We use our custom designed splicing-specific microarrays for mouse (and yeast) to detect specific splicing events that are tissue specific and/or perturbed by treatments and disease. I also work on structural RNA's in Malaria. |
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| Korostelev, Andrei |
Noller |
andrei@biology.ucsc.edu |
| Elucidation of the structure and mechanism of the ribosome, protein-synthesis machine. I apply crystallography in order to determine the structure of this complicated assembly of proteins and ribonucleic acids. The aim is to solve the structures of the ribosome in different conformations and in different functional states. |
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| Laurberg, Martin |
Noller |
martin@biology.ucsc.edu |
I work on solving crystal structures of the ribosome captured in different
functional states. We want to explain ribosomal functions in atomic detail
and ultimately reconstruct a 'movie' of protein translation as it occurs
on the ribosome. |
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| McCusker, Derek |
Kellogg |
mccusker@biology.ucsc.edu |
| Polarisation of the actin cytoskeleton occurs early in the budding yeast cell cycle and precedes bud emergence. Cyclin dependent kinase (Cdk1) activity somehow triggers activation of the essential GTPase Cdc42 which in turn orients the actin cytoskeleton and secretory apparatus towards the incipient bud. I am interested in how these temporal and spatial aspects of cell growth are coordinated with cell division. I have been working on how the Cdc42 GTPase module is regulated during the cell cycle. This involves purifying and identifying the components of the module, then analysing how these components are targeted to sites of growth using a combination of mass spectrometry, live cell imaging and electron microscopy. |
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| Siriaco, Giorgia |
Tamkun |
siriaco@biology.ucsc.edu |
| The Drosophila ISWI protein functions as the ATPase subunit of multiple chromatin-remodeling complexes. These complexes have been implicated in a wide variety of biological processes, such as DNA replication, chromatin assembly and transcription. Our studies have revealed that ISWI functions as a global repressor of transcription. In addition, it is required to maintain a compact, highly organized structure in vivo. Our recent results suggest that ISWI mediates chromatin compaction by facilitating histone H1 association with chromatin. |
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| Staple, David |
Noller |
dwstaple@biology.ucsc.edu |
| I am interested in the dynamic motions of the ribosome and how they govern translation. Currently, I study the movement of tRNA and the L1 stalk, a protrusion composed of three rRNA helices and ribosomal protein L1, using Fšrster resonance energy transfer (FRET). The objective of my research is to characterize the movement of the L1 stalk, and to decipher its role in regulating the tRNA entry into, and escape from, the E-site. |
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| Zhu, Jianyu |
Noller |
jzhu@biology.ucsc.edu |
| Currently I am focusing on the ribosome helicase activity to unfold the mRNA structure during translation process. mRNAs with different structure were prepared and cocrystallized with ribosome. The fine details of the interactions will be revealed by combinations of biochemical assays and x-ray crystal diffraction. |
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