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DTSTART;TZID=America/New_York:20250903T120000
DTEND;TZID=America/New_York:20250903T130000
DTSTAMP:20260522T180041
CREATED:20250821T165224Z
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UID:10001508-1756900800-1756904400@asrc.gc.cuny.edu
SUMMARY:Fall '25 Biochem Seminar: Assistant Professor Enrique R. Rojas
DESCRIPTION:Smart Bacterial Materials\n \nOne of the most common cellular morphologies across nature is the cylinder\, rod\, or bacillus. To achieve this shape\, cells usually reinforce the circumference of the cell to avoid cell widening while allowing elongation. However\, it is not known – in any system – how cells homeostatically specify cell width. I will show\, first\, how the cell wall of Gram-positive bacteria like Bacillus subtilisexhibit extraordinary non-linear mechanical properties\, including both stress-stiffening and stress-softening in different regimes of intracellular pressure. I will next explain how the cell exploits these properties to adaptively execute cell width homeostasis. Our preliminary studies in plant roots reveal that this generic strategy may appear convergently across many systems. \n  \nPlease use this link to access the Zoom meeting. \nFor any questions\, please contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu.
URL:https://asrc.gc.cuny.edu/event/fall-25-biochem-seminar-assistant-professor-enrique-r-rojas/
LOCATION:ASRC Auditorium\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Structural Biology
ATTACH;FMTTYPE=application/pdf:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/fall-25-biochem-seminar-assistant-professor-enrique-r-rojas/20250903_rojas_flyer.pdf
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DTSTART;TZID=America/New_York:20250910T120000
DTEND;TZID=America/New_York:20250910T130000
DTSTAMP:20260522T180041
CREATED:20250821T165341Z
LAST-MODIFIED:20250904T160138Z
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SUMMARY:Fall '25 Biochem Seminar: Associate Editor Antonio Cerullo
DESCRIPTION:Publishing in Structural Biology\, Biochemistry\, and Biophysics \nScientific progress and publishing are fundamentally intertwined. Therefore\, scientists must master both the pipette and the pen. Antonio Cerullo (CUNY ASRC – Ph.D. in Biochemistry ’23) shares his professional and personal experiences transitioning from bench science to an editorial career. Points of discussion include\, but are not limited to\, the benefits and challenges of working in publishing\, insights into writing successful manuscripts\, trends in biochemistry and biophysics\, navigating peer review\, and how to leverage your scientific background into diverse opportunities. Ultimately\, he seeks to educate scientists of all levels about the publication process and to improve engagement with this critical aspect of science. \n  \n\n\n\nPlease use this link to access Zoom. \nFor any questions\, please contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu.
URL:https://asrc.gc.cuny.edu/event/fall-25-biochem-seminar-associate-editor-antonio-cerullo/
LOCATION:ASRC Auditorium\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Structural Biology
ATTACH;FMTTYPE=application/pdf:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/fall-25-biochem-seminar-associate-editor-antonio-cerullo/20250910_cerullo_flyer.pdf
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DTSTART;TZID=America/New_York:20250917T120000
DTEND;TZID=America/New_York:20250917T130000
DTSTAMP:20260522T180041
CREATED:20250821T165504Z
LAST-MODIFIED:20250912T131702Z
UID:10001510-1758110400-1758114000@asrc.gc.cuny.edu
SUMMARY:Fall '25 Biochem Seminar: Professor Tarun Kapoor
DESCRIPTION:Chemical activators of VCP\, an unfoldase required for proteostasis \nI will discuss our recent efforts to identify and characterize chemical activators of ATPase mechanoenzymes. The loss of function of AAA (ATPases associated with diverse cellular activities) mechanoenzymes has been linked to diseases\, and chemical probes that activate these proteins can be powerful tools to probe function and test therapeutic hypotheses. Unlike an inhibitor that can bind a single conformational state of an enzyme to block activity\, activator binding must be permissive to different conformational states needed for function. However\, we do not know how any of the ~100 AAA proteins expressed in humans can be activated by drug-like small molecules. We have focused on VCP\, an AAA unfoldase with essential roles in protein turnover and quality control. Loss-of-function mutations in VCP have been linked to degenerative diseases in multiple organs and tissues. We have identified and optimized compounds that stimulate VCP’s activity and have determined cryo-EM structures (~2.9-3.5 Å resolution) of activator-VCP complexes in apo and ADP-bound states. In ongoing work\, structure-guided design has led to more potent VCP activators that may stimulate autophagy\, a lysosomal degradation pathway critical for disposing harmful cellular materials. Together\, our findings uncover a druggable allosteric site that can also be occupied by VCP’s C-terminal tail to control activity\, suggesting a mechanism of small molecule mimicry of mechanoenzyme regulation. \n  \nPlease use this link to access Zoom. \nFor any questions\, please contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu.
URL:https://asrc.gc.cuny.edu/event/fall-25-biochem-seminar-professor-tarun-kapoor/
LOCATION:ASRC Auditorium\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Structural Biology
ATTACH;FMTTYPE=application/pdf:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/fall-25-biochem-seminar-professor-tarun-kapoor/20250917_kapoor_flyer.pdf
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