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X-WR-CALDESC:Events for The Advanced Science Research Center
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BEGIN:VEVENT
DTSTART;TZID=America/New_York:20251118T163000
DTEND;TZID=America/New_York:20251118T183000
DTSTAMP:20260916T175816
CREATED:20251110T213328Z
LAST-MODIFIED:20251118T224647Z
UID:10001538-1763483400-1763490600@asrc.gc.cuny.edu
SUMMARY:The Brain and The Environment Family Night
DESCRIPTION:Join us for The Brain and The Environment Family Night at the CUNY ASRC on Nov. 18 from 4:30 to 6:30 p.m. This fun and educational evening will explore how the environment affects the brain through hands-on science activities for all ages. Guests will have the opportunity to see live EEG demonstrations where you can see your brain activity in real time\, meet our leading science researchers\, tour the research facilities\, and enjoy light food and drinks. \nRSVP today at https://forms.gle/E2htnPbQEwsZTtir9 \n 
URL:https://asrc.gc.cuny.edu/event/the-brain-and-the-environment-family-night/
LOCATION:Advanced Science Research Center (ASRC)\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Environmental Sciences,Nanoscience,Neuroscience,Photonics,Structural Biology
ATTACH;FMTTYPE=image/jpeg:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/the-brain-and-the-environment-family-night/TAYB8682_1280x720.jpg
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20251119T120000
DTEND;TZID=America/New_York:20251119T130000
DTSTAMP:20260916T175817
CREATED:20250821T165935Z
LAST-MODIFIED:20251114T175151Z
UID:10001515-1763553600-1763557200@asrc.gc.cuny.edu
SUMMARY:Fall '25 Biochem Seminar: Professor Olga Boudker
DESCRIPTION:Dynamics and Evolution of Glutamate Transporters \nGlutamate transporters in the human brain remove the neurotransmitter glutamate from the synaptic cleft\, enabling repeated cycles of neurotransmission and preventing glutamate-induced excitotoxicity. These transporters are ancient proteins that\, in prokaryotes\, serve to import amino acids as nutrient sources from the environment. Across evolution\, glutamate transporters have diversified to meet distinct physiological demands\, adapting to use different ion gradients as energy sources\, to recognize various amino acid substrates\, and to operate at different kinetic rates. I will discuss our recent insights into the structural and dynamic bases of these adaptations and how they inform strategies for developing improved therapeutics targeting neurotransmitter transporters. \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-olga-boudker/
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-olga-boudker/20251119_boudker_flyer.pdf
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20251203T120000
DTEND;TZID=America/New_York:20251203T130000
DTSTAMP:20260916T175817
CREATED:20250821T170041Z
LAST-MODIFIED:20251125T063343Z
UID:10001516-1764763200-1764766800@asrc.gc.cuny.edu
SUMMARY:Fall '25 Biochem Seminar: Associate Professor Rupal Gupta
DESCRIPTION:Structure\, Dynamics and Assembly of Human Antimicrobial Protein\n\nAntimicrobial proteins in humans sequester zinc to curtail infection. Although well established as key components of the immune response\, the mechanisms of action of these proteins\, such as S100A12\, in the inflammatory pathway is not well understood. In this talk\, I will present our work on biophysical characterization of S100A12 using NMR spectroscopy\, together with cellular studies evaluating the origin of inflammatory signals triggered by the protein. In particular\, I will focus on the roles of Ca(II) and Zn(II) towards modulating the structure and internal dynamics of S100A12 that afford its biological functions. Based on our studies\, we propose a generalized model describing the molecular events that enable S100A12 and related antimicrobial proteins to regulate infection and inflammation during immune response.\nPlease use this link to access Zoom. \nPlease contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu for any questions.
URL:https://asrc.gc.cuny.edu/event/fall-25-biochem-seminar-associate-professor-rupal-gupta/
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-professor-rupal-gupta/20250903_rojas_flyer.pdf
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20251216T163000
DTEND;TZID=America/New_York:20251216T183000
DTSTAMP:20260916T175817
CREATED:20251118T224251Z
LAST-MODIFIED:20251119T165928Z
UID:10001540-1765902600-1765909800@asrc.gc.cuny.edu
SUMMARY:Alumni and Friends Community Science Night
DESCRIPTION:Join us on Tuesday\, Dec. 16 to reconnect and learn all about what’s happening at the CUNY ASRC! All are welcome — especially former and current students\, interns\, summer researchers\, and their friends and family. The night will include fun science activities for all ages and an updated tour of the the CUNY ASRC’s state-of-the-art research facilities. \nHere is the RSVP form: https://bit.ly/3JGRh5V \n \n\nDownload and share flyer
URL:https://asrc.gc.cuny.edu/event/alumni-and-friends-community-science-night/
LOCATION:Advanced Science Research Center (ASRC)\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Environmental Sciences,Nanoscience,Neuroscience,Photonics,Structural Biology
ATTACH;FMTTYPE=image/jpeg:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/alumni-and-friends-community-science-night/TAYB7879_1280x720.jpg
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260113T123000
DTEND;TZID=America/New_York:20260113T133000
DTSTAMP:20260916T175817
CREATED:20260107T214617Z
LAST-MODIFIED:20260107T215450Z
UID:10001546-1768307400-1768311000@asrc.gc.cuny.edu
SUMMARY:Bluesky Training for Academics
DESCRIPTION:Join us for a practical\, beginner-friendly workshop on how academics can use Bluesky to share research\, build a public profile\, and connect with scholarly and professional communities. We’ll cover everything from account setup and posting basics to best practices for engagement\, visibility\, and credibility. Participants will also learn strategies for promoting publications\, events\, teaching\, and public scholarship in a way that feels authentic and manageable. This training will be held live on Zoom and includes time for questions.
URL:https://asrc.gc.cuny.edu/event/bluesky-training-for-academics/
LOCATION:Advanced Science Research Center (ASRC)\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Environmental Sciences,Nanoscience,Neuroscience,Photonics,Structural Biology
ATTACH;FMTTYPE=image/jpeg:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/bluesky-training-for-academics/GettyImages-1311107708_1280x852.jpg
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260128T120000
DTEND;TZID=America/New_York:20260128T130000
DTSTAMP:20260916T175817
CREATED:20260122T161031Z
LAST-MODIFIED:20260122T161031Z
UID:10001549-1769601600-1769605200@asrc.gc.cuny.edu
SUMMARY:Spring '26 Biochem Seminar: Christine Mayr
DESCRIPTION:Structure\, Dynamics and Assembly of Human Antimicrobial Protein \nMore than 2\,700 human mRNA 3′UTRs have hundreds of highly conserved (HC) nucleotides\, but their biological roles are unclear. A large fraction of mRNAs with highly conserved 3′UTRs\nencodes proteins with long intrinsically disordered regions (IDRs). For the tested candidates\, we observed that these proteins are only fully active when translated from mRNA templates that include their 3′UTRs\, raising the possibility of functional interactions between 3′UTRs and IDRs. Rather than affecting protein abundance or localization\, we find that highly conserved 3′UTRs directly control protein activity through protein folding of IDR-containing proteins. Presence of the 3′UTR is required to prevent interference of hydrophobic clusters in the IDR with the folding of the structured domains of the mRNA-encoded protein. In addition to folding of individual proteins\, we also observed that for some transcription factors 3′UTR-3′UTR interactions determine the co-folding of the mRNA-encoded proteins\, thus generating stable heterodimers. Taken together\, our work indicates that highly conserved 3′UTRs regulate protein activity in an abundance-independent manner\, by controlling different co-translational protein folding pathways. \nPlease use this link to access Zoom.
URL:https://asrc.gc.cuny.edu/event/spring-26-biochem-seminar-christine-mayr/
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/spring-26-biochem-seminar-christine-mayr/20260128_mayr_flyer_new_zoom_link.pdf
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260128T123000
DTEND;TZID=America/New_York:20260128T133000
DTSTAMP:20260916T175817
CREATED:20260114T195118Z
LAST-MODIFIED:20260114T195252Z
UID:10001548-1769603400-1769607000@asrc.gc.cuny.edu
SUMMARY:LinkedIn Training for Academics
DESCRIPTION:Join us for a practical\, beginner-friendly workshop on how academics can use LinkedIn to showcase their expertise\, expand professional networks\, and increase the visibility of their research and teaching. This session will cover optimizing profiles for academic and public-facing work\, understanding how the platform’s algorithm works\, and crafting posts that highlight publications\, projects\, events\, and career milestones without feeling self-promotional. Participants will also learn strategies for engaging with scholarly\, nonprofit\, and industry communities; building credibility over time; and using LinkedIn in ways that support public scholarship\, career development\, and institutional visibility. The training will be held live on Zoom and includes time for questions and real-world examples. \nRegister to attend at https://bit.ly/4pD08nK
URL:https://asrc.gc.cuny.edu/event/linkedin-training-for-academics/
LOCATION:Advanced Science Research Center (ASRC)\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Environmental Sciences,Nanoscience,Neuroscience,Photonics,Structural Biology
ATTACH;FMTTYPE=image/jpeg:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/bluesky-training-for-academics/GettyImages-1311107708_1280x852.jpg
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260218T120000
DTEND;TZID=America/New_York:20260218T130000
DTSTAMP:20260916T175817
CREATED:20260122T195707Z
LAST-MODIFIED:20260209T142433Z
UID:10001550-1771416000-1771419600@asrc.gc.cuny.edu
SUMMARY:Spring '26 Biochem Seminar: Edward P. O'Brien\, Jr.
DESCRIPTION:How a novel class of protein misfolding is associated with changes in enzyme activity\, proteostasis\, aging\, and disease \nUtilizing simulations\, experimental data\, and data science\, my lab predicted the existence of a previously undiscovered\, widespread class of protein misfolding that can result in soluble\, loss-of-function states\, some of which evade the proteostasis network. This class of misfolding involves structural changes in geometric motifs called non-covalent lasso entanglements\, which are found in 70% of the native structures of globular proteins. In this talk\, I will synthesize six lines of evidence: (1) proteome-wide and atomistic simulations establish the prevalence and physical plausibility of self-entanglement; (2) translation-speed changes from synonymous mutations can re-partition folding trajectories into slowly interconverting\, near-native entangled ensembles with reduced catalytic efficiency; (3) native-like surfaces coupled to these topological barriers explain how some misfolded states bypass chaperones; that these misfolded states are associated with (4) increased nascent protein degradation through the ubiquitin-proteasome pathway in human fibroblast cells\, (5) with structural changes in proteins that occur during yeast mother cell aging\, and (6) with a higher likelihood of harboring pathogenic mutations in human diseases. Taken together\, simulations and experiments areconverging on a unified picture in which entanglement misfolding is common\, biologically consequential\, and measurable. \nPlease use this link to access Zoom. \nPlease contact Hyacinth Camillieri at hcamillieri@gc.cuny.edu if you have any questions.
URL:https://asrc.gc.cuny.edu/event/spring-26-biochem-seminar-edward-p-obrien-jr/
LOCATION:ASRC Auditorium\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Structural Biology
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260304T120000
DTEND;TZID=America/New_York:20260304T130000
DTSTAMP:20260916T175817
CREATED:20260122T195846Z
LAST-MODIFIED:20260219T155919Z
UID:10001551-1772625600-1772629200@asrc.gc.cuny.edu
SUMMARY:Spring '26 Biochem Seminar: Neil L. Kelleher
DESCRIPTION:Digitizing Proteoform Biology with Single Molecule & Single Cell Mass Spectrometry \nSince the completion of the Human Genome Project\, much has been made of the need to bridge the gap from genes and traits. As a key nexus for the many interacting ‘-omes’ (genome\,\ntranscriptome\, proteome\, metabolome\, etc.)\, the proteome should offer a tight link between genotype and phenotype. Proteoforms\, or all of the precise molecular forms of a protein\, capture all sources of variability in protein composition (i.e.\, SNPs\, isoforms\, posttranslational modifications)\, and thus provide crucial insights into regulation and function. Now\, “single ion” mass spectrometry is poised to convert genes to proteoform signatures at a far faster rate. Recently we developed proteoform imaging mass spectrometry (PiMS)\, with individual ion mass spectrometry. This platform has been extended now to single-cell Proteoform imaging Mass Spectrometry (scPiMS)\, boosting cell processing rates by >20-fold in the field while detecting proteoforms from single cells. \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/spring-26-biochem-seminar-neil-l-kelleher/
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/spring-26-biochem-seminar-neil-l-kelleher/20260304_kelleher_flyer.pdf
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260311T120000
DTEND;TZID=America/New_York:20260311T130000
DTSTAMP:20260916T175817
CREATED:20260122T195948Z
LAST-MODIFIED:20260305T220731Z
UID:10001552-1773230400-1773234000@asrc.gc.cuny.edu
SUMMARY:Spring '26 Biochem Seminar: James Fraser
DESCRIPTION:Statistical Structural Biology \nIn a post-“structure prediction is solved” world\, our lab is obsessed with the concept of statistical structural biology. We collect large datasets (X-ray fragment screens from 1000s of individual crystals) and use new statistical approaches to identify small molecule binders. This inspires new inhibitors\, allosteric modulators\, and enzyme design strategies. We also examine how experimental information encodes statistical distributions of conformations. This inspires software (e.g. qFit) that reveals hidden conformations\, new guidance frameworks for diffusion models that reveals memorization\, and experiments to extract even more information. These two aspects are synergistic in examining many aspects of biology. A current focus is the promiscuity of ligand binding in drug metabolism proteins\, as part of the OpenADMET. \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/spring-26-biochem-seminar-series-james-fraser/
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/spring-26-biochem-seminar-series-james-fraser/20260311_fraser_flyer-1.pdf
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260325T120000
DTEND;TZID=America/New_York:20260325T130000
DTSTAMP:20260916T175817
CREATED:20260122T200053Z
LAST-MODIFIED:20260312T185612Z
UID:10001553-1774440000-1774443600@asrc.gc.cuny.edu
SUMMARY:Spring '26 Biochem Seminar: Margaret Stratton
DESCRIPTION:Tuning a Master Kinase: How CaMKII variants are deployed and degraded \nCa²⁺/calmodulin-dependent protein kinase II (CaMKII) is a central signaling enzyme that regulates neuronal plasticity\, fertilization\, and cardiac function. Although its catalytic and oligomerization domains are highly conserved\, extensive alternative splicing within a variable linker region generates numerous CaMKII proteoforms whose functional roles remain unclear. Transcript sequencing of human hippocampus reveals three CaMKIIα splice variants in human hippocampal tissue. Biochemical and cellular analyses show that linker composition tunes CaMKII activation by Ca²⁺/calmodulin\, with electrostatic effects that modulate regulatory segment accessibility. In addition to activation control\, CaMKII signaling is regulated by selective degradation: activated CaMKII is targeted by the ubiquitin–proteasome system. Together\, these results reveal how alternative splicing and ubiquitin-dependent turnover cooperate to tune the activity of this master kinase. \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/spring-26-biochem-seminar-margaret-stratton/
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/spring-26-biochem-seminar-margaret-stratton/20260325_stratton_flyer.pdf
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260415T120000
DTEND;TZID=America/New_York:20260415T130000
DTSTAMP:20260916T175817
CREATED:20260122T200230Z
LAST-MODIFIED:20260408T152158Z
UID:10001554-1776254400-1776258000@asrc.gc.cuny.edu
SUMMARY:Spring '26 Biochem Seminar: Pratyush Tiwary
DESCRIPTION:AI augmented molecular simulations for predicting protein and RNA structural ensembles\nAI is now everywhere in chemistry\, from structure prediction to molecule generation to automated synthesis. The excitement is real\, but so is the unease about what is genuinely predictive and what is closer to impressive memorization. In this colloquium I will take a statistical physicist’s perspective and use examples from my group’s work to argue for cautious\, but clear\, enthusiasm for AI in chemistry and allied fields. I will show how we combine generative AI with statistical mechanics to learn Boltzmann weighted ensembles from limited training data\, and then extrapolate across temperature\, pressure\, and other thermodynamic conditions reducing the need for explicit\, expensive simulations or experiments. I will highlight the breadth of these methods through applications that include nucleation of crystal polymorphs under nanoconfinement\, prediction of protein and RNA structural ensembles\, and conformation selective drug discovery efforts aimed at Alzheimer’s disease and hypertension. Time permitting\, I will discuss briefly what I think are the biggest challenges facing chemistry research and education as we proceed with the perhaps inevitable adoption of AI. \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/spring-26-biochem-seminar-pratyush-tiwary/
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/spring-26-biochem-seminar-pratyush-tiwary/20260415_tiwary_flyer.pdf
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260429T120000
DTEND;TZID=America/New_York:20260429T130000
DTSTAMP:20260916T175817
CREATED:20260122T200333Z
LAST-MODIFIED:20260416T195618Z
UID:10001555-1777464000-1777467600@asrc.gc.cuny.edu
SUMMARY:Spring '26 Biochem Seminar: Abhishek Singharoy
DESCRIPTION:Inverting Biophysics: From Function to Ensembles \nMost of computational biology is predicated upon the sequence → structure → function → phenotype paradigm. Thanks to artificial intelligence and the availability of data at various scales\, researchers have been trying to bridge gaps between the different tiers of this process\, starting from the age-old genotype–phenotype modeling to CASP and Alphafold’s sequence-structure up to recent attempts to go from sequence to ensemble. However\, physical causality is often missing in the traditional bioinformatic models\, thus far sidelining the AIdriven advances only to predictions of the forward direction. The lecture will introduce physical ideas to conceive generative models that backmap phenotypes down to an ensemble of structures and sequences. For example\, leveraging our work on modeling the diffusion of charge carriers in bioenergetic membranes\, we computed the mechanism of chemokine binding to the Oxford CovidVaccine. With AstraZenaca\, we computationally redesigned the adenovirus vector to prevent potential clotting disorders. Using Google’s inception network algorithm\, we invert this immune recognition function into a generalizable learning strategy of electrostatic structures across proteins. We are now using this electrostatic network to study disease association in patients\, as well as design peptide therapeutics\, and search of hidden toxins\, covering the entire human proteome\, generalizing the molecular function-to-ensemble paradigm. \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/spring-26-biochem-seminar-abhishek-singharoy/
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/spring-26-biochem-seminar-abhishek-singharoy/20260429_singharoy_flyer.pdf
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260902T120000
DTEND;TZID=America/New_York:20260902T130000
DTSTAMP:20260916T175817
CREATED:20260827T172341Z
LAST-MODIFIED:20260827T172341Z
UID:10001578-1788350400-1788354000@asrc.gc.cuny.edu
SUMMARY:Fall '26 Biochem Seminar: Pranam Chatterjee
DESCRIPTION:Designing Programmable Biologics with Generative Sequence Models \nIn this talk\, I will share how my lab develops discrete generative models to design functional biologics for disease and bioremediation. Our work has centered on language models that de novo design peptides to bind and modulate undruggable targets\, with experimental validation across rare neurodegenerative disorders\, pediatric cancers\, and viral infections. Because therapeutic design depends on clinically-viable properties beyond binding (solubility\, half-life\, non-toxicity)\, we have developed discrete diffusion algorithms to generate peptides\, proteins\, mRNAs\, and heavy metal sequestrants that are Pareto-optimal across these properties. We have extended these frameworks to discrete flow matching models that generate isoform-specific\, domain- and motif-resolved binders under competing therapeutic objectives\, enabling the design of potent inhibitors and CAR T cell ligands. Finally\, we have recently pioneered Schrödinger Bridge Matching\, a new class of generative models that capture both biological states and the trajectories connecting them\, from protein folding to drug-induced cell-state transitions\, establishing a unified\, programmable framework for molecular modeling and design. \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-26-biochem-seminar-pranam-chatterjee/
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-26-biochem-seminar-pranam-chatterjee/20260902_chatterjee_flyer.pdf
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260916T120000
DTEND;TZID=America/New_York:20260916T130000
DTSTAMP:20260916T175817
CREATED:20260910T140729Z
LAST-MODIFIED:20260910T140729Z
UID:10001580-1789560000-1789563600@asrc.gc.cuny.edu
SUMMARY:Fall '26 Biochem Seminar: Crina Nimigean
DESCRIPTION:Mechanism of Lipid Modulation in Ion Channels \nMembrane proteins are continuously exposed to the complex lipid environment of cellular membranes\, yet how specific lipids regulate their function remains poorly understood. In this talk\, I will discuss two examples illustrating how membrane lipids tune ion-channel activity through defined structural mechanisms. First\, I will describe how lipids regulate temperature sensitivity in SthK\, a\nbacterial ion channel that is activated by cold temperatures. We find that a functionally important\, state-dependent intersubunit salt bridge acts as a temperature sensor\, while lipid binding tunes temperature sensitivity by modulating the strength of this interaction. These findings suggest a general mechanism by which thermosensitivity can emerge from the interplay between protein energetics and the membrane environment. Second\, I will discuss regulation of rod photoreceptor cyclic nucleotide-gated (CNG) channels by the signaling lipid PI(4\,5)P2 (PIP2). Although PIP2 was known to inhibit CNG channels\, its very low abundance in rod outer segments raised questions about the physiological relevance of this effect. We show that\nPIP2 potently inhibits CNG channels at physiologically relevant concentrations (<0.2 mol%) and identify its binding site and mechanism of action. PIP2 binds to an allosteric site that stabilizes the closed channel and impedes conformational changes required for opening. Identification of this regulatory site also reveals a potential target for pharmacological modulation of CNG channels.\nTogether\, these studies demonstrate how specific lipid–protein interactions can reshape the energetic landscape of ion channels to control physiologically important aspects of their function. \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-26-biochem-seminar-crina-nimigean/
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-26-biochem-seminar-crina-nimigean/20260916_nimigean_flyer.pdf
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/New_York:20260922T100000
DTEND;TZID=America/New_York:20260922T140000
DTSTAMP:20260916T175817
CREATED:20260902T214646Z
LAST-MODIFIED:20260902T215228Z
UID:10001579-1790071200-1790085600@asrc.gc.cuny.edu
SUMMARY:FloodNet Community Session: Building Community Together – Lessons from 2023 to Now
DESCRIPTION:Join us for the launch of At the Intersection of Science\, Policy\, and Community: The FloodNet NYC Community Engagement Strategy\, a public-facing guide that shares the community engagement approaches\, tools\, and lessons developed through FloodNet NYC.  \nGrounded in community-based participatory research (CBPR)\, the guide highlights practical strategies for building meaningful collaborations across science\, policy\, and communities through outreach\, education\, and action. This event will bring together community partners\, community-engaged researchers\, students at CUNY and NYU\, and other stakeholders to explore how these approaches can support equitable\, community-centered climate research and urban resilience initiatives. \nRegister to attend at https://bit.ly/3VaJcvl
URL:https://asrc.gc.cuny.edu/event/floodnet-community-session-building-community-together-lessons-from-2023-to-now/
LOCATION:Advanced Science Research Center (ASRC)\, 85 St. Nicholas Terrace\, New York\, NY\, 10031\, United States
CATEGORIES:Environmental Sciences,Nanoscience,Neuroscience,Photonics,Structural Biology
ATTACH;FMTTYPE=image/jpeg:https://asrc.gc.cuny.edu/wp-content/uploads/media/event/floodnet-community-session-building-community-together-lessons-from-2023-to-now/TAYB5169_1280x720.jpg
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END:VCALENDAR