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DTSTART;TZID=America/New_York:20260304T120000
DTEND;TZID=America/New_York:20260304T130000
DTSTAMP:20260521T090023
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
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DTSTART;TZID=America/New_York:20260311T120000
DTEND;TZID=America/New_York:20260311T130000
DTSTAMP:20260521T090023
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:20260521T090023
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
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