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        "date_end":"2025-12-11",
        "time_start":"13:30:00",
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        "time_zone":"America\/Detroit",
        "event_title":"ChE SEMINAR: Jeff McCutcheon, University of Connecticut",
        "occurrence_title":"",
        "combined_title":"ChE SEMINAR: Jeff McCutcheon, University of Connecticut",
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        "event_type":"Workshop \/ Seminar",
        "event_type_id":"21",
        "description":"A reception with light refreshments will be held in the B10 lobby before each seminar from 1-1:30 p.m.\r\n\r\nMore details to come.",
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        "tags":["chemical engineering","Free","Graduate","Michigan Engineering","Undergraduate"],
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                "group_name":"Chemical Engineering",
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                "website":"http:\/\/che.engin.umich.edu\/"                }                    ],
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        "datetime_modified":"20251226T123107",
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        "time_start":"14:00:00",
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        "event_title":"Internship Lab",
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        "combined_title":"Internship Lab",
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        "event_type":"Careers \/ Jobs",
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        "description":"*RSVP required to attend. Click \"Join Event\" here:https:\/\/umich.joinhandshake.com\/edu\/events\/1862720Are you ready to start searching for a great internship? Do you have a few ideas, but you\u2019re not sure where to get started? Let's talk about search strategy!!\u00a0Get real-time, personalized support by checking out the in person Internship Lab. You\u2019ll be guided by one of our Career Coaches who hasdesigned this experience to provide you strategies, tools, and motivation to get on the right track with searching for internships.\u00a0Chat with folks from the University Career Center to explore Handshake,the University Career Alumni Network (UCAN) and to learn about other tools you can use to build a great job\/internship search strategy.\u00a0**If you're not sure what you're interested in, consider making an \"Exploring Major\/Career Option\" appointment to get started clarifying your interests with a career coach in a 1-on-1 setting.\u00a0Recent Grads: If you are an alumni, you will not be able to access the link due the University\u2019s policy of discontinuing alumni Zoom accounts 30 days after graduation. Please contact careercenter@umich.edu with the subject line\u201cRecent Grad Help\u201d to receive either a recording of the session or tobe set up with a 1:1. Include the name of the workshop\/event in your email.#UCC",
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        "event_title":"The Power of Singing, the Power of Song",
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        "combined_title":"The Power of Singing, the Power of Song: Matt Watroba  Folk Singer",
        "event_subtitle":"Matt Watroba  Folk Singer",
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        "description":"Join us and enjoy a demonstration of the healing and unifying power of community singing. Inspired by the work of Pete Seeger, Watroba will use a variety of song genres and techniques to create an experience that is as entertaining as it is uplifting and healing. Many know Matt Watroba as the voice of folk music in Michigan for his work producing and hosting shows for public radio. He has devoted his life and career to being a custodian of American folk and roots music. This has shaped a repertoire and presentation that is unique on stages across the state and country. He is committed to inspiring the world to sing\u2014one town at a time. In 2019, Matt, along with his life-long musical partner Robert Jones, co-founded the Detroit non-profit, Common Chords. Also in 2019, Matt was inducted into the Folk DJ Hall of Fame at the Folk Alliance International Conference in Montreal.",
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        "time_zone":"America\/Detroit",
        "event_title":"RTG NT: Construction via relative cohomology",
        "occurrence_title":"",
        "combined_title":"RTG NT: Construction via relative cohomology: Lue Pan",
        "event_subtitle":"Lue Pan",
        "event_type":"Workshop \/ Seminar",
        "event_type_id":"21",
        "description":"TBA",
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                "guid":"142372-21890767@events.umich.edu",
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             {
                "group_name":"RTG Seminar on Number Theory - Department of Mathematics",
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        "datetime_modified":"20251202T115857",
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        "event_title":"Dissertation Defense Seminar: Cassandra Zuckerman",
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        "combined_title":"Dissertation Defense Seminar: Cassandra Zuckerman: Investigation of shelterin complex assembly at C. elegans telomeres and structural characterization of a novel centrosomal protein complex critical for mammalian sperm development",
        "event_subtitle":"Investigation of shelterin complex assembly at C. elegans telomeres and structural characterization of a novel centrosomal protein complex critical for mammalian sperm development",
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        "description":"Telomeres are nucleoprotein complexes at chromosome termini that are vital for the preservation of genome integrity. Telomeric DNA consists of hexad repeats (GGTTAG in mammals) that are mostly double-stranded (ds), ending in a short, single-stranded (ss) 3\u2032 overhang. In dividing cells, telomeric DNA shortens with each round of DNA replication, causing the \u201cend replication problem.\u201d A specialized ribonucleoprotein (RNP) enzyme, telomerase, replenishes telomeric DNA repeats to aid in resolving this problem. \r\nNatural chromosome ends resemble dsDNA breaks, creating the \u201cend protection problem,\u201d the necessity to protect natural ends from the DNA damage response\/repair machinery. The six-protein mammalian shelterin complex binds telomeric repeats to protect chromosome ends from unwanted repair. Shelterin dysfunction results in end deprotection and mouse embryonic lethality. POT1 is a critical shelterin component that protects the telomeric ssDNA overhang and the ds\u2013ss junction, and helps facilitate telomerase action. Thus, a single POT1 orchestrates multiple telomeric functions, complicating the dissection of its functions individually. Studying the shelterin complex in in toto is even more challenging, as POT1 is separated from the dsDNA-binding shelterin proteins by two additional shelterin subunits. \r\n\r\nIn contrast to humans, C. elegans (Ce) has four putative POT1 homologs (Ce POT-1, POT-2, POT-3, and MRT-1), leading us to hypothesize that POT1 functions are separated on different polypeptides, making it feasible to study each POT1 function individually. The dsDNA-binding proteins of C. elegans have also been discovered, and they bind directly to CePOT-1, greatly simplifying the composition of the shelterin complex. However, how the other CePOT1 homologs integrate into shelterin to protect and replicate chromosome ends is not known. Through my doctoral studies, I discovered a novel interaction of CePOT-1 with CePOT-2 and Ce-MRT-1 via a CePOT-1 binding site shared by CePOT-2 and CeMRT-1. My studies revealed that CePOT-1 acts as a bridge to connect these single-stranded DNA-binding proteins with CeTEBP-1 and ceTEBP-2, C. elegans\u2019 telomeric dsDNA-binding proteins. Taken together, my findings shed light on how C. elegans shelterin assembles at chromosome ends.\r\n\r\nThe second part of my thesis involves MEICEN, a testis-specific protein essential for male fertility. Centrosomes are organelles that play several major roles during mitosis and meiosis, including the formation of the bipolar spindle during mitosis and the formation of cilia and flagella. In sperm, remodeled centrosomes, called basal bodies, anchor the sperm flagellum to the sperm head. Centrins are proteins fundamental to centrosome assembly and duplication. Of the four mammalian centrins, centrin 1 is specifically expressed in testes and is essential for male fertility. \r\n\r\nOur collaborators, the Shibuya lab, identified MEICEN as a novel, testes-specific regulator of centrosome dynamics and sperm tail maturation that binds centrin and is essential for male fertility. Meicen knockout mice display irregular centrin 1 localization, which results in sperm tail defects. Yet how MEICEN binds centrin during meiosis was unknown. As part of my doctoral studies, I used SEC-MALS to reveal that MEICEN homodimerizes to bind a total of sixteen centrin molecules. I then solved the crystal structure of the MEICEN-centrin 1 complex to provide the structural basis of an interaction critical for spermatogenesis. Finally, I introduced mutations at the MEICEN-centrin interface to demonstrate that it abrogates the MEICEN-centrin interaction. Overall, our findings inspire a model in which MEICEN acts as a storage system for centrin to limit its over-accumulation at meiotic centrosomes, preventing their overduplication.",
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