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METHOD:PUBLISH
X-WR-CALNAME:Shi Lab
X-ORIGINAL-URL:https://sites.rutgers.edu/shi-lab
X-WR-CALDESC:Events for Shi Lab
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BEGIN:VTIMEZONE
TZID:UTC
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TZOFFSETFROM:+0000
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DTSTART:20220101T000000
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DTSTART:20210314T070000
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DTSTART:20211107T060000
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BEGIN:VEVENT
DTSTART;TZID=UTC:20230418T080000
DTEND;TZID=UTC:20230418T170000
DTSTAMP:20260501T133419
CREATED:20221130T212355Z
LAST-MODIFIED:20230303T152422Z
UID:1333-1681804800-1681837200@sites.rutgers.edu
SUMMARY:CCB Colloquium – Professor Min Wu\, Yale University
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/ccb-colloquium-min-wu-yale-university/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20230218T080000
DTEND;TZID=UTC:20230223T170000
DTSTAMP:20260501T133419
CREATED:20221130T212640Z
LAST-MODIFIED:20221130T212640Z
UID:1337-1676707200-1677171600@sites.rutgers.edu
SUMMARY:Biophysical Society 67th Annual Meeting in San Diego
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/biophysical-society-67th-annual-meeting-in-san-diego/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20230131T080000
DTEND;TZID=UTC:20230131T170000
DTSTAMP:20260501T133419
CREATED:20221130T212332Z
LAST-MODIFIED:20230103T225758Z
UID:1331-1675152000-1675184400@sites.rutgers.edu
SUMMARY:CCB Colloquium – Professor Dingchang Lin\, Johns Hopkins University
DESCRIPTION:Electronic and molecular approaches for neural recording: deciphering the brain in space and time \nResolving neuronal activity in space and time is a long-sought capability in neuroscience\, which is\, however\, still hard to achieve using existing technologies. In this talk\, I will share with the audience our strategies toward this goal via innovations at the device and molecular levels. In the first part of my talk\, I will start by introducing our recent development of ultra flexible neural probes that exhibit extraordinary biocompatibility and the capability of chronic single-unit recording. I will then share our new implantation modality that can nonlinearly deploy our probes into the brain with minimal surgical lesions. The modality allows conformal coverage of nonlinear brain structures or circuits using microelectrode arrays and therefore enables high-density neural recording along designated trajectories. In the second part of my talk\, I will switch to our recent endeavors in developing protein “ticker tapes” for the longitudinal recording of cellular events. The technology exploits activity-dependent transcriptional activation to convert neural activities into fluorescently readable signals in cells. The signals can be recorded by protein nanodevices genetically encoded in individual cells for retrospective retrieval. This strategy provides an attainable path toward organ-wide longitudinal mapping at the single-cell level.
URL:https://sites.rutgers.edu/shi-lab/event/ccb-colloquium-professor-dingchang-lin-johns-hopkins-university/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20221203T080000
DTEND;TZID=UTC:20221207T170000
DTSTAMP:20260501T133419
CREATED:20221130T212545Z
LAST-MODIFIED:20221130T212545Z
UID:1335-1670054400-1670432400@sites.rutgers.edu
SUMMARY:The American Society for Cell Biology meeting in Washington\, DC
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/the-american-society-for-cell-biology-meeting-in-washington-dc/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20221129T080000
DTEND;TZID=UTC:20221129T170000
DTSTAMP:20260501T133419
CREATED:20220707T013816Z
LAST-MODIFIED:20221118T140545Z
UID:1130-1669708800-1669741200@sites.rutgers.edu
SUMMARY:CCB Colloquium - Professor Dragomir Milovanovic\, DZNE
DESCRIPTION:Condensate Biology at the Synapse \n\n\n\n\n\n\n\nBrain functioning critically relies on neuronal communication that mainly occurs by chemical signaling at the specialized contacts known as synapses. At synapses\, messenger molecules are packed into synaptic vesicles (SVs)\, which are secreted upon the arrival of an action potential. For neuronal signaling to persist\, synapses have to maintain an adequate pool of SVs at all times. In fact\, synapses are packed with hundreds of SVs that are tightly clustered. Decades of research have established that SVs are clustered by synapsin 1\, an abundant SV-associated phosphoprotein at synapses. The classical view postulates that synapsin cross-links SVs together in a modifiable scaffold of protein-protein interactions between synapsin and its binding partners. However\, recent studies suggest that synapsin clusters SVs via liquid-liquid phase separation (LLPS)\, which brings the classical model into question. During the seminar\, I will discuss our efforts to scrutinize the LLPS of SVs both in reconstituted systems and in living neurons\, as well as to determine the functional impact of SV condensates on neuronal function.\n\n\nTuesday\, November 29\, 2022 11:00AM\, CCB Auditorium (1303)
URL:https://sites.rutgers.edu/shi-lab/event/dragomir-milovanovic-ccb-colloquium/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20221018T080000
DTEND;TZID=UTC:20221018T170000
DTSTAMP:20260501T133419
CREATED:20220707T013730Z
LAST-MODIFIED:20220901T184849Z
UID:1128-1666080000-1666112400@sites.rutgers.edu
SUMMARY:CCB Colloquium - Professor Simon Scheuring\, Weill Cornell Medicine\,
DESCRIPTION:“Breaking Speed and Resolution Limitations of High-Speed AFM for Membrane Protein Structure-Function Analysis”\nSimon Scheuring1\,2\,*\n1 Weill Cornell Medicine\, Department of Anesthesiology\, 1300 York Avenue\, New York\, NY-10065\, USA.\n2 Weill Cornell Medicine\, Department of Physiology and Biophysics\, 1300 York Avenue\, New York\, NY-10065\, USA \nHigh-speed atomic force microscopy (HS-AFM) is a powerful technique that provides dynamic movies of biomolecules at work [1]. We successfully used HS-AFM to take movies and determine dynamic parameters of membrane trafficking systems\, transporters and channels. \nTo break current temporal limitations to characterize molecular dynamics using HS-AFM\, we developed HS-AFM line scanning (HS-AFM-LS) and HS-AFM height spectroscopy (HS-AFM-HS)\, methods whereby we scan the HS-AFM tip along a single scan line or keep it at a fixed position\, respectively\, and detect the motions of the molecules under the tip. This gives sub-nanometer spatial resolution combined with millisecond and microseconds temporal resolution of molecular fluctuations. HS-AFM-LS and HS-AFM-HS can be used in conjunction with HS-AFM imaging\, thus giving access to a wide dynamic range [1]. This allowed us most recently to determine the single molecule kinetics of wild-type bacteriorhodopsin [2]. \nTo break current resolution limitations\, we developed Localization AFM (LAFM). By applying localization image reconstruction algorithms to peak positions in high-speed AFM and conventional AFM data\, we increase the resolution beyond the limits set by the tip radius and reach quasi-atomic resolution on soft protein surfaces in native and dynamic conditions. The LAFM method allows the calculation of high-resolution maps from either images of many molecules or many images of a single molecule acquired over time\, opening new avenues for single molecule structural analysis [3]. \nI will review these recent achievements\, and present novel data and methods to integrate and strengthen HS-AFM as a powerful tool in structural biology and molecular biophysics. We reason that the progress of AFM must comprise two axes: First\, making AFM/HS-AFM a better tool. With the above-mentioned methods\, we made significant progress in this axis over the last ~5 years. Second\, making AFM/HS-AFM data an integrated part of the structural biology / molecular biophysics toolbox. Such\, we are developing now methods and data analysis and interpretation methods that interface with cryo-EM and X-ray crystallography\, where AFM/HS-AFM can contribute the urgently needed information about structure\, dynamics and conformations under close-to-native conditions. \nReferences:\n[1] Heath et al. Nature Communications\, 2018\, 9(1):4983\, High-Speed AFM Height Spectroscopy (HS-AFM-HS): Microsecond dynamics of unlabeled biomolecules.\n[2] Perrino et al.\, Nature Communications\, 2021 12(7225)\, doi.org/10.1038/s41467-021-27580-2\, Single molecule kinetics of bacteriorhodopsin by HS-AFM.\n[3] Heath et al. Nature\, 2021\, 594(7863):385–390\, doi:10.1038/s41586-021-03551-x\, Localization Atomic Force Microscopy.
URL:https://sites.rutgers.edu/shi-lab/event/simon-scheuring-ccb-colloquium/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20220927T080000
DTEND;TZID=UTC:20220927T170000
DTSTAMP:20260501T133419
CREATED:20220707T013621Z
LAST-MODIFIED:20220901T184932Z
UID:1125-1664265600-1664298000@sites.rutgers.edu
SUMMARY:CCB Colloquium - Professor Matthew Tyska\, Vanderbilt University School of Medicine
DESCRIPTION:Shaping the epithelial cell surface with actin bundling proteins\nDuring differentiation\, enterocytes build an extensive apical array of microvilli known as the brush border\, which serves to amplify the plasma membrane surface area available for nutrient absorption. In addition to serving as the sole site of nutrient uptake\, brush border microvilli also provide an anchoring point for the glycocalyx and regulate interactions with luminal microbes. An individual microvillus is simple in structure\, consisting of a supporting core of ~25 actin filaments bundled in parallel by villin\, fimbrin\, and espin. Remarkably\, microvilli biogenesis persists in mice lacking all three of these factors\, suggesting the existence of unknown bundlers. We identified Mitotic Spindle Positioning (MISP) as an actin binding factor that localizes specifically to the rootlet end of the microvillus. MISP promotes rootlet elongation in cells\, and purified MISP exhibits potent filament bundling activity in vitro. MISP-bundled filaments also recruit fimbrin\, which further elongates and stabilizes bundles. MISP confinement to the rootlet is enforced by ezrin\, which prevents decoration of the membrane-wrapped distal end of the core bundle. These discoveries reveal how enterocytes optimize apical membrane surface area and offer insight on the remarkable robustness of microvilli biogenesis. \n 
URL:https://sites.rutgers.edu/shi-lab/event/matt-tyska-ccb-colloquium/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20220805T120000
DTEND;TZID=UTC:20220805T190000
DTSTAMP:20260501T133419
CREATED:20220719T161313Z
LAST-MODIFIED:20220719T161313Z
UID:1139-1659700800-1659726000@sites.rutgers.edu
SUMMARY:Samsuzzoha (Babun) Mondal seminar
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/samsuzzoha-babun-mondal-seminar/
LOCATION:CCB 3217
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20220601T080000
DTEND;TZID=UTC:20220604T170000
DTSTAMP:20260501T133419
CREATED:20220115T024229Z
LAST-MODIFIED:20220604T021606Z
UID:1004-1654070400-1654362000@sites.rutgers.edu
SUMMARY:2022 ACS MARM
DESCRIPTION:Our symposium for Membrane Biophysics will happen on the first day of MARM2022 (June 1st\, 1 pm – 5 pm). Here is a sneak peek of the topics/speakers. \n \nThank you to all speakers and attendees for making the symposium a fun event! \nLeft to right: Amaresh Sahu\, Steven Arnold\, Tobias Baumgart\, Sreeja Sasidharan\, Patrick Haller\, Ilya Levental\, Zheng Shi\, Markus Deserno\, Ammanuel Mehreteab\, Malavika Varma\, Samuel Foley\, Aurelia Honerkamp-Smith\, Shilong Yang\, Liz Kelley\, Huan Wang
URL:https://sites.rutgers.edu/shi-lab/event/acs-marm-2022/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20220301T080000
DTEND;TZID=UTC:20220301T170000
DTSTAMP:20260501T133419
CREATED:20220116T015745Z
LAST-MODIFIED:20220301T144029Z
UID:1012-1646121600-1646154000@sites.rutgers.edu
SUMMARY:Bianxiao Cui\, CCB Colloquium
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/bianxiao-cui-ccb-colloquium/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20220219T080000
DTEND;TZID=UTC:20220223T170000
DTSTAMP:20260501T133419
CREATED:20220115T024111Z
LAST-MODIFIED:20220115T024111Z
UID:1002-1645257600-1645635600@sites.rutgers.edu
SUMMARY:2022 BPS meeting
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/2022-bps-meeting/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20220201T110000
DTEND;TZID=UTC:20220201T123000
DTSTAMP:20260501T133419
CREATED:20220116T015636Z
LAST-MODIFIED:20220128T034534Z
UID:1010-1643713200-1643718600@sites.rutgers.edu
SUMMARY:CCB Colloquium - Jun Wang: "Medicinal Chemistry and Pharmacology of Antivirals Targeting SARS-CoV-2"
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/jun-wang-ccb-colloquium/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20210901T090000
DTEND;TZID=America/New_York:20210901T110000
DTSTAMP:20260501T133419
CREATED:20210831T004036Z
LAST-MODIFIED:20210831T011445Z
UID:901-1630486800-1630494000@sites.rutgers.edu
SUMMARY:Groupmeeting
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/groupmeeting/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20210203T130000
DTEND;TZID=America/New_York:20210203T150000
DTSTAMP:20260501T133419
CREATED:20210128T032159Z
LAST-MODIFIED:20210128T032159Z
UID:724-1612357200-1612364400@sites.rutgers.edu
SUMMARY:Group Meeting
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/group-meeting/
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