{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/117785"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/117785","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"An Hsp90 physical interactome","abstract":"Submission original under an indefinite embargo labeled 'Open Access'. The submission was exported from vireo on 2023-04-12 without embargo terms","abstract_html":"Submission original under an indefinite embargo labeled 'Open Access'. The submission was exported from vireo on 2023-04-12 without embargo terms","abstract_has_math":false,"creators":["Kolhe, Janhavi Atit"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Cell and Developmental Biology","degree_department":null,"school":null,"contributors":["Freeman, Brian C","Brieher, William M","Raetzman, Lori T","Li, Xin"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2022,"date_issued":"2022-12","date_published":"2022-12","updated_at":"2026-07-22T22:24:56Z","subjects":["Hsp90","Molecular Chaperone","Bpa Crosslinking"],"languages":["en","eng"],"rights":["Copyright 2022 Janhavi Kolhe"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/2142/117785","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Freeman, Brian C","Brieher, William M","Raetzman, Lori T","Li, Xin"]},{"key":"dc:creator","label":"Author","values":["Kolhe, Janhavi Atit"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2022-12","2022-11-29"]},{"key":"dc:type","label":"Dc Type","values":["text","Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Cell and Developmental Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Hsp90","Molecular Chaperone","Bpa Crosslinking"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en","eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 2022 Janhavi Kolhe"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://hdl.handle.net/2142/117785"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Submission original under an indefinite embargo labeled 'Open Access'. The submission was exported from vireo on 2023-04-12 without embargo terms","The student, Janhavi Kolhe, accepted the attached license on 2022-11-28 at 09:41.","The student, Janhavi Kolhe, submitted this Dissertation for approval on 2022-11-28 at 09:44.","This Dissertation was approved for publication on 2022-11-29 at 10:39.","DSpace SAF Submission Ingestion Package generated from Vireo submission #18643 on 2023-04-12 at 07:34:02","Hsp90 is a critical eukaryotic molecular chaperone, ubiquitously expressed in all organisms. It is a highly abundant protein (~2% of a cell’s protein mass) and is involved in numerous processes including protein trafficking, chromatin remodeling, and signal transduction. To govern a broad variety of biological pathways Hsp90 exploits two different modes of interactions with clients and/or co-chaperones - a stable association such as when maintaining a metastable client in a soluble state and a transient binding such as when driving the dynamics of proteins working in transcription, chromatin remodeling, or DNA repair. Despite the numerous and extensive studies on Hsp90, the complete clientele of Hsp90 is unknown. Likely, the transient interactions between Hsp90 and many of its clients make their identification through traditional techniques difficult. To gain a better understanding of the factors interacting with Hsp90, I exploited the non-natural amino acid p-Benzoyl-L-Phenylalanine (Bpa) to generate an in vivo kinetic trap to capture Hsp90 interactions. In conjunction with mass spectrometry, I have identified 1114 physical interactors of Hsp90. Nearly half of the hits were novel for Hsp90-association and included pathways such as translation initiation and genome organization. My studies provide mechanistic insights into Hsp90 as a molecular chaperone as well as its functional role in different cellular processes."]},{"key":"dc:format","label":"Dc Format","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["An Hsp90 physical interactome"]}]}],"canonical_facts":{"dc:contributor":["Freeman, Brian C","Brieher, William M","Raetzman, Lori T","Li, Xin"],"dc:creator":["Kolhe, Janhavi Atit"],"dc:date":["2022-12","2022-11-29"],"dc:description":["Submission original under an indefinite embargo labeled 'Open Access'. The submission was exported from vireo on 2023-04-12 without embargo terms","The student, Janhavi Kolhe, accepted the attached license on 2022-11-28 at 09:41.","The student, Janhavi Kolhe, submitted this Dissertation for approval on 2022-11-28 at 09:44.","This Dissertation was approved for publication on 2022-11-29 at 10:39.","DSpace SAF Submission Ingestion Package generated from Vireo submission #18643 on 2023-04-12 at 07:34:02","Hsp90 is a critical eukaryotic molecular chaperone, ubiquitously expressed in all organisms. It is a highly abundant protein (~2% of a cell’s protein mass) and is involved in numerous processes including protein trafficking, chromatin remodeling, and signal transduction. To govern a broad variety of biological pathways Hsp90 exploits two different modes of interactions with clients and/or co-chaperones - a stable association such as when maintaining a metastable client in a soluble state and a transient binding such as when driving the dynamics of proteins working in transcription, chromatin remodeling, or DNA repair. Despite the numerous and extensive studies on Hsp90, the complete clientele of Hsp90 is unknown. Likely, the transient interactions between Hsp90 and many of its clients make their identification through traditional techniques difficult. To gain a better understanding of the factors interacting with Hsp90, I exploited the non-natural amino acid p-Benzoyl-L-Phenylalanine (Bpa) to generate an in vivo kinetic trap to capture Hsp90 interactions. In conjunction with mass spectrometry, I have identified 1114 physical interactors of Hsp90. Nearly half of the hits were novel for Hsp90-association and included pathways such as translation initiation and genome organization. My studies provide mechanistic insights into Hsp90 as a molecular chaperone as well as its functional role in different cellular processes."],"dc:format":["application/pdf"],"dc:identifier":["https://hdl.handle.net/2142/117785"],"dc:language":["en","eng"],"dc:rights":["Copyright 2022 Janhavi Kolhe"],"dc:subject":["Hsp90","Molecular Chaperone","Bpa Crosslinking"],"dc:title":["An Hsp90 physical interactome"],"dc:type":["text","Thesis"],"thesis:degree_discipline":["Cell and Developmental Biology"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:24:56Z"}