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BEGIN:VEVENT
DTSTART;TZID=UTC:20240210T080000
DTEND;TZID=UTC:20240214T170000
DTSTAMP:20260401T162758
CREATED:20230728T161927Z
LAST-MODIFIED:20230728T161927Z
UID:1545-1707552000-1707930000@sites.rutgers.edu
SUMMARY:Biophysical Society 68th Annual Meeting in Philadelphia
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/biophysical-society-68th-annual-meeting-in-philadelphia/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20240123T110000
DTEND;TZID=UTC:20240123T123000
DTSTAMP:20260401T162758
CREATED:20230728T161447Z
LAST-MODIFIED:20230921T170426Z
UID:1536-1706007600-1706013000@sites.rutgers.edu
SUMMARY:CCB Colloquium – Professor Jim Shorter\, University of Pennsylvania
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/ccb-colloquium-professor-jim-shorter-university-of-pennsylvania/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20240116T110000
DTEND;TZID=America/New_York:20240116T123000
DTSTAMP:20260401T162758
CREATED:20230728T161601Z
LAST-MODIFIED:20230921T170302Z
UID:1538-1705402800-1705408200@sites.rutgers.edu
SUMMARY:CCB Colloquium – Professor Qiang Cui\, Boston University
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/ccb-colloquium-professor-qiang-cui-boston-university/
LOCATION:CCB 1303 Auditorium
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20231202T080000
DTEND;TZID=UTC:20231206T170000
DTSTAMP:20260401T162758
CREATED:20230728T161808Z
LAST-MODIFIED:20230728T161825Z
UID:1542-1701504000-1701882000@sites.rutgers.edu
SUMMARY:The American Society for Cell Biology meeting in Boston
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/the-american-society-for-cell-biology-meeting-in-boston-ma/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20231019T110000
DTEND;TZID=America/New_York:20231019T120000
DTSTAMP:20260401T162758
CREATED:20230728T161658Z
LAST-MODIFIED:20230921T170101Z
UID:1540-1697713200-1697716800@sites.rutgers.edu
SUMMARY:Special Seminar – Dr. Harry McNamara\, Princeton University
DESCRIPTION:Symmetry breaking and self-organization of a body axis from mouse embryonic stem cells  \nAbstract:  \nDuring development\, the embryo must break symmetry to form body axes and patterned tissue structures. Recent discoveries have revealed that stem cell aggregates can recapitulate developmental patterning and morphogenesis in vitro; however\, it remains largely unknown how these ‘stembryos’ break symmetry in the absence of extrinsic patterning cues. The gastruloid is a stembryo model which self-organizes an anterior-posterior body axis in response to transient\, spatially uniform stimulation of Wnt signaling activity. It has been proposed that a reaction-diffusion Turing instability polarizes Wnt activity in the gastruloid\, thereby defining a posterior organizer. \nWe use synthetic “signal-recording” gene circuits to trace fate information encoded by signaling dynamics in the mouse gastruloid. We find that an ordered sequence of BMP\, Nodal\, and Wnt signaling states predict cells’ future position along the anterior-posterior (A-P) axis even before any of these morphogen signals are themselves polarized. Our data demonstrate A-P axial polarization does not require a biochemical Turing instability\, but instead proceeds through a cell sorting mechanism which resoles early signaling variability into spatially separated anterior and posterior domains. Our study reveals how stem cells can self-organize a body axis without extrinsic patterning cues.
URL:https://sites.rutgers.edu/shi-lab/event/special-seminar-dr-harry-mcnamara-princeton-university/
LOCATION:CCB 3217
ATTACH;FMTTYPE=image/jpeg:https://sites.rutgers.edu/shi-lab/wp-content/uploads/sites/378/2023/07/headshot_cropped_upright-scaled-e1694637880814.jpg
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20230928T110000
DTEND;TZID=America/New_York:20230928T120000
DTSTAMP:20260401T162758
CREATED:20230919T162649Z
LAST-MODIFIED:20230925T141038Z
UID:1577-1695898800-1695902400@sites.rutgers.edu
SUMMARY:Special Seminar – Dr. Charles Cox\, Victor Chang Cardiac Research Institute\, Australia
DESCRIPTION:Discovery and characterization of a novel family of PIEZO channel auxiliary subunits \nPIEZO channels are critical cellular sensors of mechanical forces. Native PIEZO1 channels can display nonuniform subcellular localization and exhibit different gating kinetics—principally\, slower inactivation in many cell types when compared with heterologous expression systems. These observations could be explained by differences in lipid composition\, curvature-dependent sorting or protein-protein interactions. Despite their large size\, ubiquitous expression\, and irreplaceable roles in an ever-growing list of physiological processes\, few PIEZO channel-binding proteins have emerged. Recently using affinity capture mass spectrometry in conjunction with fibroblast cell lines edited using CRISPR/Cas9 we found that MyoD family inhibitor proteins (MDFIC and MDFI)\, interact with both PIEZO1 and PIEZO2 channels. We confirmed using co-immunoprecipitation that these transcriptional regulators\, bind to PIEZO1/2 channels and patch-clamp electrophysiology revealed they regulate channel inactivation. Using single-particle cryo-electron microscopy\, we mapped the interaction site in MDFIC to a lipidated\, C-terminal helix that inserts laterally into the PIEZO1 pore module. These PIEZO interacting proteins fit all the criteria for auxiliary subunits\, contribute to explaining the vastly different gating kinetics of endogenous PIEZO channels observed in many cell types\, shine light on mechanisms potentially involved in human lymphatic vascular disease and pave the way for novel mechano-signaling pathways directly linking PIEZO channels to transcription. \nLocation: CCB-3217 \nZoom Registration
URL:https://sites.rutgers.edu/shi-lab/event/special-seminar-dr-charles-cox-victor-chang-cardiac-research-institute-australia/
LOCATION:CCB 3217
ATTACH;FMTTYPE=image/png:https://sites.rutgers.edu/shi-lab/wp-content/uploads/sites/378/2023/09/cdc-e1695245780532.png
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20230921T110000
DTEND;TZID=America/New_York:20230921T120000
DTSTAMP:20260401T162758
CREATED:20230913T203928Z
LAST-MODIFIED:20230921T165945Z
UID:1569-1695294000-1695297600@sites.rutgers.edu
SUMMARY:Special Seminar – Professor Neha Jain\, Indian Institute of Technology
DESCRIPTION:Modulation of amyloid assembly by chaperone-like proteins \nSoluble proteins have an inherent propensity to undergo altered protein folding\, forming cross-B sheet-rich structures called amyloids. Amyloid fibrils have gained significant attention due to their involvement in neurodegenerative disorders. Parkinson’s disease (PD) is one of the most common movement disorders and the fastest-growing age-related neurological disorder. It is characterized by progressive loss of dopaminergic neurons in substantia nigra due to the accumulation of a-synuclein amyloid fibrils leading to the formation of Lewy bodies. Co-aggregation of a-synuclein with other amyloidogenic proteins such as amyloid-B\, Tau\, and IAPP contributes to the pathophysiology and severity of PD\, suggesting that PD progression is associated with other neurological disorders such as Alzheimer’s and Huntington’s and non-neurological diseases such as Type 2 diabetes and systemic diseases where amyloid deposits can be found in multiple organs including liver\, kidney\, and heart. An intricate machinery of chaperones and chaperone-like proteins keeps a check on protein aggregation and amyloid formation. However\, these guardians lose their properties with age\, and proteins such as a-synuclein accumulate in cells. Understanding the role of chaperone-like proteins as amyloid modulators will help in the early diagnosis of disease and present a novel approach to mitigate amyloid burden in neurodegenerative disease. Using bioinformatics tools\, we have rationally identified human B-sheet rich proteins that have the potential to act as chaperone-like proteins to inhibit amyloid assembly. These proteins possess remarkable structural similarity\, with 50-60% of the structure contributed by B-sheets. We speculated that the B-sheet-rich regions in the proteins may present a scaffold to the growing chain of aggregates\, which is incompetent for maturing into amyloid fibrils. We have taken a multi-disciplinary approach involving microbiology\, biochemistry\, biophysics\, molecular and cellular biology tools to decipher the mechanism of amyloid inhibition by chaperone-like proteins. We demonstrated that sub-stoichiometric ratios of CLP drive a-synuclein into soluble off-pathway aggregates incompetent of making amyloids under in vitro conditions. We believe that unraveling the potential of chaperone-like proteins to alleviate amyloid burden will pave the way for future therapeutics to treat neurodegenerative diseases. \nLocation CCB-3217
URL:https://sites.rutgers.edu/shi-lab/event/special-seminar-professor-neha-jain-indian-institute-of-technology/
LOCATION:CCB 3217
ATTACH;FMTTYPE=image/jpeg:https://sites.rutgers.edu/shi-lab/wp-content/uploads/sites/378/2023/09/Neha-Jain-professional-headshot-scaled-e1694637737488.jpg
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20230919T080000
DTEND;TZID=UTC:20230919T170000
DTSTAMP:20260401T162758
CREATED:20230913T203520Z
LAST-MODIFIED:20230913T204132Z
UID:1562-1695110400-1695142800@sites.rutgers.edu
SUMMARY:CCB Colloquium – Professor Xiaoyang Su\, Rutgers Medical School and Cancer Institute of New Jersey
DESCRIPTION:LC-MS Metabolomics Reveals the Role of SLC45A4 in GABA de novo Synthesis \nAffiliations: 1Departments of Medicine\, Division of Endocrinology\, Robert Wood Johnson Medical School\, Rutgers University; 2Metabolomics Shared Resource\, Rutgers Cancer Institute of New Jersey\, New Brunswick\, NJ 08901\, USA \nSolute carrier (SLC) proteins are membrane transporters that govern the cross-membrane exchanges of glucose\, amino acids\, inorganic ions\, and other small molecule metabolites. Many SLC genes have been shown to be causes of Mendelian diseases in humans\, and a number of SLC transporters are important drug targets. However\, due to myriad technical difficulties\, a large fraction of SLC family members are still orphan transporters without known substrates\, which represents both a significant knowledge gap and a huge opportunity for new drug development.  In order to systematically deorphanize SLC transporters\, we developed a workflow for transcriptomic-metabolomic association analysis. Using this approach\, we identified an uncharacterized gene\, SLC45A4\, that is the single greatest  determinant of  y-aminobutyric acid (GABA) levels in human cancer cells. GABA\, which is mostly known as an inhibitory neurotransmitter in the mammalian central nervous system\, functions in peripheral tissues to regulate cell proliferation\, differentiation\, and migration. Using mass spectrometry and stable isotope tracing\, we found that SLC45A4 increases cellular GABA levels not by promoting GABA uptake but by facilitating GABA de novo synthesis\, suggesting an entirely new regulatory mechanism of GABA synthesis. \nLocation CCB Auditorium (Room 1303)
URL:https://sites.rutgers.edu/shi-lab/event/ccb-colloquium-professor-xiaoyang-su-rutgers-medical-school-and-cancer-institute-of-new-jersey/
ATTACH;FMTTYPE=image/jpeg:https://sites.rutgers.edu/shi-lab/wp-content/uploads/sites/378/2023/09/Photo_Su-scaled-e1694637682660.jpg
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20230914T083000
DTEND;TZID=UTC:20230914T170000
DTSTAMP:20260401T162758
CREATED:20230728T165058Z
LAST-MODIFIED:20230728T165058Z
UID:1549-1694680200-1694710800@sites.rutgers.edu
SUMMARY:Rutgers-Princeton Biomolecular Condensates Day
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/rutgers-princeton-biomolecular-condensates-day/
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20230912T080000
DTEND;TZID=UTC:20230912T170000
DTSTAMP:20260401T162758
CREATED:20230913T203718Z
LAST-MODIFIED:20230913T204721Z
UID:1564-1694505600-1694538000@sites.rutgers.edu
SUMMARY:CCB Colloquium – Professor Keith Mickolajczyk\, RWJ Medical School
DESCRIPTION:Single-molecule biophysical approaches to studying the mechanisms of motor proteins\n \nRibosomes are molecular machines made of protein and RNA that translate mRNA into proteins. The biogenesis of new ribosomes is the most energetically costly process in the cell\, accounting for ~60% of all ATP consumed. New ribosomes begin as rRNA\, and are sequentially matured through a complicated multi-step process that involves hundreds of protein factors\, including motor proteins (force-producing enzymes) from the AAA (ATPase associated with diverse cellular activities) and helicase-2 (SF2) superfamilies. Dysregulation of ribosome biogenesis is linked to genetic diseases (ribosomopathies)\, and its upregulation is a hallmark of proliferative cancers. Nonetheless\, the molecular mechanisms underlying ribosome maturation – how motor proteins sequentially convert ribosomal precursors into mature particles – remain poorly understood. Filling this gap in knowledge is essential for understanding ribosomal biology in health and disease\, and for exploring new classes of ribosome biogenesis-targeting chemotherapeutics. \nIn the Mickolajczyk Lab we develop and apply state-of-the-art single-molecule biophysical techniques including optical tweezers\, magnetic tweezers\, FRET\, and label-free imaging to study how AAA and SF2 motor proteins drive ribosome biogenesis. We directly measure how these motors convert the energy from ATP hydrolysis into mechanical work\, and how those forces are then used to change the structure and composition of ribosomal precursors. We further explore how disease-causing mutations in ribosomal proteins alter this fundamental enzymology\, with the ultimate goal of guiding new molecular therapies for ribosomopathies and proliferative cancers.
URL:https://sites.rutgers.edu/shi-lab/event/ccb-colloquium-professor-keith-mickolajczyk-rwj-medical-school/
ATTACH;FMTTYPE=image/jpeg:https://sites.rutgers.edu/shi-lab/wp-content/uploads/sites/378/2023/09/Mickolajczyk_Keith-J-scaled-e1694638036900.jpg
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20230418T080000
DTEND;TZID=UTC:20230418T170000
DTSTAMP:20260401T162759
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:20260401T162759
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:20260401T162759
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:20260401T162759
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:20260401T162759
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:20260401T162759
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:20260401T162759
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:20260401T162759
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:20260401T162759
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:20260401T162759
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:20260401T162759
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:20260401T162759
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:20260401T162759
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:20260401T162759
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/
END:VEVENT
END:VCALENDAR