Academic literature on the topic 'Ubiquitin'
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Journal articles on the topic "Ubiquitin"
Kama, Rachel, Galina Gabriely, Vydehi Kanneganti, and Jeffrey E. Gerst. "Cdc48 and ubiquilins confer selective anterograde protein sorting and entry into the multivesicular body in yeast." Molecular Biology of the Cell 29, no. 8 (April 15, 2018): 948–63. http://dx.doi.org/10.1091/mbc.e17-11-0652.
Full textLee, Dong Yun, and Eric J. Brown. "Ubiquilins in the crosstalk among proteolytic pathways." Biological Chemistry 393, no. 6 (June 1, 2012): 441–47. http://dx.doi.org/10.1515/hsz-2012-0120.
Full textJantrapirom, Salinee, Luca Lo Piccolo, Dumnoensun Pruksakorn, Saranyapin Potikanond, and Wutigri Nimlamool. "Ubiquilin Networking in Cancers." Cancers 12, no. 6 (June 15, 2020): 1586. http://dx.doi.org/10.3390/cancers12061586.
Full textHurtley, Stella M. "One Ubiquitin, Two Ubiquitin, Three Ubiquitin, Four." Science's STKE 2007, no. 369 (January 16, 2007): tw26. http://dx.doi.org/10.1126/stke.3692007tw26.
Full textHill, Spencer, Joseph S. Harrison, Steven M. Lewis, Brian Kuhlman, and Gary Kleiger. "Mechanism of Lysine 48 Selectivity during Polyubiquitin Chain Formation by the Ube2R1/2 Ubiquitin-Conjugating Enzyme." Molecular and Cellular Biology 36, no. 11 (April 4, 2016): 1720–32. http://dx.doi.org/10.1128/mcb.00097-16.
Full textFord, Diana L., and Mervyn J. Monteiro. "Dimerization of ubiquilin is dependent upon the central region of the protein: evidence that the monomer, but not the dimer, is involved in binding presenilins." Biochemical Journal 399, no. 3 (October 13, 2006): 397–404. http://dx.doi.org/10.1042/bj20060441.
Full textSeok Ko, Han, Takashi Uehara, Kazuhiro Tsuruma, and Yasuyuki Nomura. "Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains." FEBS Letters 566, no. 1-3 (April 28, 2004): 110–14. http://dx.doi.org/10.1016/j.febslet.2004.04.031.
Full textChatrin, Chatrin, Mads Gabrielsen, Lori Buetow, Mark A. Nakasone, Syed F. Ahmed, David Sumpton, Gary J. Sibbet, Brian O. Smith, and Danny T. Huang. "Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases." Science Advances 6, no. 38 (September 2020): eabc0418. http://dx.doi.org/10.1126/sciadv.abc0418.
Full textMorgan, Rachel E., Vijay Chudasama, Paul Moody, Mark E. B. Smith, and Stephen Caddick. "A novel synthetic chemistry approach to linkage-specific ubiquitin conjugation." Organic & Biomolecular Chemistry 13, no. 14 (2015): 4165–68. http://dx.doi.org/10.1039/c5ob00130g.
Full textIkeda, Hiromi, and Tom K. Kerppola. "Lysosomal Localization of Ubiquitinated Jun Requires Multiple Determinants in a Lysine-27–Linked Polyubiquitin Conjugate." Molecular Biology of the Cell 19, no. 11 (November 2008): 4588–601. http://dx.doi.org/10.1091/mbc.e08-05-0496.
Full textDissertations / Theses on the topic "Ubiquitin"
Sekiyama, Naotaka. "STRUCTURAL ANALYSIS OF UBIQUITIN AND UBIQUITIN-LIKE PROTEIN RECEPTORS." 京都大学 (Kyoto University), 2010. http://hdl.handle.net/2433/120884.
Full textBraxton, Courtney N. "The progress on mapping ubiquitin signaling using photocrosslinking mono and di-ubiquitin probes and other ubiquitin moieties." VCU Scholars Compass, 2018. https://scholarscompass.vcu.edu/etd/5382.
Full textHaririnia, Aydin. "Molecular interactions of ubiquitin and polyubiquitin with ubiquitin binding domains." College Park, Md. : University of Maryland, 2007. http://hdl.handle.net/1903/7627.
Full textThesis research directed by: Dept. of Chemistry and Biochemistry. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.
Lange, Anja. "Structural characterization of the interaction of the Stam2's ubiquitin binding domains with ubiquitin chains by NMR : Cooperativity or not, that is the question !" Thesis, Lyon 1, 2010. http://www.theses.fr/2010LYO10308.
Full textFrom the discovery of ubiquitin and its function as signal for proteasomal degradation over 20 years ago to this days, it became evident that ubiquitin is a universal signal in eukaryotic cells. Ubiquitin in its different forms is involved in many versatile cellular processes. Knowing that the ubiquitin signal is differently translated, depending on its occurrences as mono-ubiquitin or poly-ubiquitin, raises the question: how do cells distinguish between the different occurrences of ubiquitin and translate it into the proper response? Proteins interacting with ubiquitin contain so called ubiquitin binding domains (UBDs), whereas the affinities to ubiquitin vary from a few _M to mM. So far only three (K63, K48 and linear chains) out of the eight possible chain-linkages can be produced in sufficient amounts to characterize their interaction with UBDs. K48- and K63- linked ubiquitin chains regulate different cellular events and need to be recognized by different proteins. Thus, it is of prime importance to characterize the binding of different UBDs to these two kinds of ubiquitin chains, as it can give important clues related to the general mechanism of chain discrimination by ubiquitin adapter proteins. Some isolated UBDs exhibit a preference for one chain linkage type over the other, whereas others do not discriminate between mono-ubiquitin or K63- and K48-linked chains. Interestingly, many ubiquitin adapter proteins harbor more than one UBD. STAM2 is a ubiquitin adapter protein, that is involved in endosomal receptor sorting and supposed to preferentially bind mono-ubiquitin and K63- over K48-linked ubiquitin. STAM2 contains two UBDs (a VHS and UIM domain) that were shown to bind to ubiquitin . The current manuscript shows that STAM2’s SH3 domain binds ubiquitin as well. To understand the function of the sequential arrangement of three UBDs in one protein, first binding of the individual VHS and UIM domains to monoubiquitin as well as K48- and K63-linked di-ubiquitin was investigated. This work shows, that the VHS domain displays a different mode of binding for K63- and K48-linked diubiquitin. In spite of the fact, that the apparent Kd for both chains is the same, only one VHS domain can bind to K48-linked di-ubiquitin chains (with a preference for the distal domain), whereas K63-linked di-ubiquitin can accommodate two VHS domains at a time. Since no conclusion can be drawn with respect to the apparent Kds, the different binding modes might gain more impact in consideration of the ensemble of three UBDs. Results presented in this manuscript, based on a construct containing the VHS and UIM domain, show that binding to K63- but not K48-linked di-ubiquitin is cooperative
Pirim, Ibrahim. "Ubiquitin and neurogenerative diseases." Thesis, University of Nottingham, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.335277.
Full textDeschutter, Julie. "Identification de la monoubiquitination de la protéine SHIP2 et caractérisation des mécanismes régulateurs associés." Doctoral thesis, Universite Libre de Bruxelles, 2009. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/241308.
Full textDepaux, Arnaud. "Régulation des complexes d'ubiquitinylation et de sumoylation par la ligase E3 hSIAH2." Paris 7, 2006. http://www.theses.fr/2006PA077094.
Full textAfter synthesis, proteins are targeted to post-translational modifications such as acetylation, phosphorylation or ubiquitination. These mechanisms regulate their function, stability, localization or interaction with partners. Modification process by ubiquitin or sumo named ubiquitination or sumoylation respectively involve complexes with similar organization but compose of different enzymes. Their organization relies on Sumo or ubiquitin activating El enzyme, transferring E2-ligase and E3-ligase or sub-complex conferring the substrate specific récognition. El-ligase is unique for each complex, whereas E2 and E3-ligases are multiple. Among E3-ligase families, RING Finger protein family only has been involved in both modifications complexes. Two human homologs of Drosophila Seven In Absentia (hSIAHl et hSIAH2), belong to RING Finger E3-ligase family. In a yeast two hybrid assay, we have identified new SIAH interacting proteins. Their characterization has been the purpose of my PhD project. We have characterized partners implicated in both ubiquitination (ubiquitin, Ubc5 or hSIAH) and sumoylation (Sumo, Ubc9 and PIAS) pathways. In a first attempt, I have demonstrated that hSIAH proteins can form homo- or hetero-dimers. Dimerization régulates their stability via a proteasome dependent degradation. I have also demonstrated that hSIAH2 catalyzes the proteasome dependent degradation of PIAS1, a sumo E3-ligase. Altogether this study evidences an important rôle for hSIAH2 in the regulation of the stability of ubiquitination and sumolation complexes
Bazirgan, Omar Al-Kasim. "Functional analysis of the ubiquitin ligase Hrd1p with the ubiquitin-conjugating enzyme Ubc7p." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2007. http://wwwlib.umi.com/cr/ucsd/fullcit?p3246079.
Full textTitle from first page of PDF file (viewed March 9, 2007). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references.
Rumsby, Ellen Louise. "Regulation of the cell division cycle by ubiquitin and ubiquitin-like modifications in yeast." Thesis, University of Newcastle upon Tyne, 2015. http://hdl.handle.net/10443/2938.
Full textSouza, Letícia Martins Ignácio de 1987. "Sistema ubiquitina-proteassoma no hipotálamo : implicações para a gênese da obesidade." [s.n.], 2013. http://repositorio.unicamp.br/jspui/handle/REPOSIP/310374.
Full textTese (Doutorado) - Universidade Estadual de Campinas, Faculdade de Ciências Médicas
Made available in DSpace on 2018-08-22T00:15:51Z (GMT). No. of bitstreams: 1 Souza_LeticiaMartinsIgnaciode_D.pdf: 4083691 bytes, checksum: 4627dc93519577a00d2747b36d1a406f (MD5) Previous issue date: 2013
Resumo: Dentre os fatores ambientais que contribuem para o desenvolvimento de obesidade, o consumo de dietas ricas em ácidos graxos saturados desempenha o papel mais importante. Estudos recentes realizados por vários grupos, inclusive o nosso, revelam que ácidos graxos saturados presentes na dieta levam ao desenvolvimento de resistência hipotalâmica à ação dos hormônios leptina e insulina, fenômeno este fundamental para que ocorra a quebra no equilíbrio entre ingestão e gasto calórico. Até o momento caracterizaram-se dois mecanismos moleculares potencialmente envolvidos na iniciação do processo que resulta na disfunção hipotalâmica na obesidade, a ativação de TLR4 e a indução de estresse de retículo endoplasmático, ambos levando a uma resposta inflamatória local e, eventualmente, a apoptose neuronal. Estudos recentes têm revelado que frente a situações que oferecem risco de dano celular, ativa-se um mecanismo de controle de tráfico e degradação protéica chamado sistema ubiquitina-proteassoma (UPS). O acúmulo de agregados protéicos positivos para ubiquitina pode gerar toxicidade celular e regular a plasticidade neuronal. Também a modulação de componentes do UPS pode gerar neurodegeneração hipotalâmica e fenótipo obeso em animais experimentais. Neste estudo aventamos a hipótese que durante períodos prolongados de obesidade a ativação anômala do UPS contribuiria para a perpetuação do quadro de obesidade. De fato, os resultados obtidos revelam que roedores com predisposição para a obesidade induzida por dieta mantém, a princípio, a capacidade de regular adequadamente a UPS no hipotálamo. Com o passar do tempo esta capacidade é perdida resultando numa maior dificuldade para perda de peso frente à redução do aporte calórico. Roedores com mutações que os protegem da inflamação, não apresentam distúrbio funcional do UPS quando expostos a dieta rica em ácidos graxos e, são também protegidos da obesidade. Portanto, o defeito funcional do UPS no hipotálamo no curso de obesidade prolongada, constitui-se num fator importante contribuindo para a refratariedade ao tratamento e perpetuação da doença
Abstract: The consumption of high-fat diets, especially those rich in saturated fatty acids, plays the most important role in the development of obesity. Recent studies by several groups, including ours, have shown that dietary long-chain saturated fatty acids lead to the development of hypothalamic resistance to leptin and insulin, an important condition contributing for breaking of the balance between caloric intake and energy expenditure. Two molecular mechanisms are currently known to play a triggering role in this process; activation of TLR4 and endoplasmic reticulum stress, both leading to local inflammation and eventually apoptosis of neurons. The ubiquitin-proteasome system (UPS) plays an important role in the control of protein recycling in the cell. The accumulation of ubiquitin-positive protein aggregates can cause cell toxicity and regulate neuronal plasticity. Also the modulation or differential activation of UPS can produce hypothalamic neurodegeneration and obese phenotype in experimental animals. Here, we hypothesized that under prolonged diet-induced obesity, a defect in the UPS in the hypothalamus could contribute for the defective control of energy homeostasis leading to the refractoriness of obesity to caloric restriction. In fact in an obesity-prone rodent strain, prolonged, but not short-term obesity was accompanied by functional abnormality of the UPS in the hypothalamus. In mutants protected from inflammation, resistance to diet-induced obesity was accompanied by stability of the UPS in the hypothalamus. Thus, defect of the UPS in the hypothalamus, during prolonged obesity is an important factor contributing the refractoriness of obesity to caloric restriction
Doutorado
Biologia Estrutural, Celular, Molecular e do Desenvolvimento
Doutora em Fisiopatologia Médica
Books on the topic "Ubiquitin"
Conaway, Joan, and Ray DeShaies. Abstracts of papers presented at the 2005 meeting on the ubiquitin family: April 27-May 1, 2005. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 2005.
Find full textRechsteiner, Martin, ed. Ubiquitin. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2.
Full textMartin, Rechsteiner, ed. Ubiquitin. New York: Plenum Press, 1988.
Find full text1961-, Deshaies Raymond Joseph, ed. Ubiquitin and protein degradation. Amsterdam: Elsevier Academic Press, 2005.
Find full textS, Jentsch, and Haendler B, eds. The ubiquitin system in health and disease. Berlin: Springer, 2009.
Find full textPatterson, Cam, and Douglas M. Cyr. Ubiquitin-Proteasome Protocols. New Jersey: Humana Press, 2005. http://dx.doi.org/10.1385/1592598951.
Full textRodriguez, Manuel S., and Rosa Barrio, eds. The Ubiquitin Code. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2859-1.
Full textCam, Patterson, and Cyr Douglas M, eds. Ubiquitin-proteasome protocols. Totowa, N.J: Humana Press, 2005.
Find full textArgilés, Josep M. Ubiquitin and disease. Austin, Tex., U.S.A: R.G. Landes, 1998.
Find full textJ, Schlesinger Milton, Hershko Avram, and Cold Spring Harbor Laboratory, eds. The Ubiquitin system. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 1988.
Find full textBook chapters on the topic "Ubiquitin"
Rechsteiner, Martin. "Introduction." In Ubiquitin, 1–4. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_1.
Full textSiegelman, Mark, and Irving L. Weissman. "Lymphocyte Homing Receptors, Ubiquitin, and Cell Surface Proteins." In Ubiquitin, 239–69. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_10.
Full textCiechanover, Aaron. "Role of Transfer RNA in the Degradation of Selective Substrates of the Ubiquitin- and ATP-Dependent Proteolytic System." In Ubiquitin, 271–86. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_11.
Full textVarshavsky, Alexander, Andreas Bachmair, Daniel Finley, David Gonda, and Ingrid Wünning. "The N-End Rule of Selective Protein Turnover." In Ubiquitin, 287–324. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_12.
Full textHershko, Avram. "Selectivity of Ubiquitin-Mediated Protein Breakdown." In Ubiquitin, 325–32. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_13.
Full textWilkinson, Keith D. "Purification and Structural Properties of Ubiquitin." In Ubiquitin, 5–38. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_2.
Full textFinley, Daniel, Engin Özkaynak, Stefan Jentsch, John P. McGrath, Bonnie Bartel, Michael Pazin, Robert M. Snapka, and Alexander Varshavsky. "Molecular Genetics of the Ubiquitin System." In Ubiquitin, 39–75. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_3.
Full textPickart, Cecile M. "Ubiquitin Activation and Ligation." In Ubiquitin, 77–99. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_4.
Full textHough, Ronald F., Gregory W. Pratt, and Martin Rechsteiner. "Ubiquitin/ATP-Dependent Protease." In Ubiquitin, 101–34. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_5.
Full textRose, Irwin A. "Ubiquitin Carboxyl-Terminal Hydrolases." In Ubiquitin, 135–55. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_6.
Full textConference papers on the topic "Ubiquitin"
Zhi, Xu, Dong Zhao, Zhongmei Zhou, and Ceshi Chen. "Abstract 213: RNF126 E3 ubiquitin ligase targets p21cipfor ubiquitin-mediated degradation." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-213.
Full textSong, Chengcheng, Vyacheslav Akimov, Peter Foote, Xiaolong Lu, Blagoy Blagoev, and Rajesh Singh. "Abstract B074: Ubiquitin proteomics: profiling the landscape of ubiquitin modification by ubisite-omics." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; October 26-30, 2017; Philadelphia, PA. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1535-7163.targ-17-b074.
Full textQin, Haoran, Yilin Zhong, and Shuning Liu. "Ubiquitin-proteasome pathway in disease." In Third International Conference on Biological Engineering and Medical Science (ICBioMed2023), edited by Alan Wang. SPIE, 2024. http://dx.doi.org/10.1117/12.3021667.
Full textYao, Eric, Shenshen Lai, and Jun Yan. "Abstract 3862: Empowering research on ubiquitin and ubiquitin-like protein modification cascade using recombinant enzyme systems." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3862.
Full textHong, Huang Chun, Hu Tian, Wu Xin Yin, Jie Ke Ming, Yan Nian long, and Ying Mu Ying. "Structure and function of ubiquitin-conjugating enzymes." In International conference on Human Health and Medical Engineering. Southampton, UK: WIT Press, 2014. http://dx.doi.org/10.2495/hhme130411.
Full textWang, Zehua, Arun Seth, and Ceshi Chen. "Abstract 509: RNF115/BCA2 E3 ubiquitin ligase promotes breast cancer cell proliferation through targeting p21Waf1/Cip1for ubiquitin-mediated degradation ." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-509.
Full textRuiz-Agudo, Cristina, Lutz Joachim, King Michael, Marx Andreas, and Gebauer Denis. "Designer Ubiquitin Proteins Towards Controlling Calcium Carbonate Crystallization." In Goldschmidt2020. Geochemical Society, 2020. http://dx.doi.org/10.46427/gold2020.2242.
Full textYoshida, Yukiko, Koji Matsuoka, Tomoki Chiba, Toshiaki Suzuki, Keiji Tanaka, and Tadashi Tai. "N-GLYCANS ARE RECOGNIZED BY E3 UBIQUITIN-LIGASE." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.430.
Full textMa, Ke, Philip Ryan, Rachel Klevit, and Stanley Lipkowitz. "Abstract 4965: Multiple ubiquitin-conjugating enzymes modulate the ubiquitination and downregulation of the EGFR by the Cbl RING finger ubiquitin ligase." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4965.
Full textDriscoll, James J., and Sajjeev Jagannathan. "Abstract 1708: Metabolic regulation of the ubiquitin+proteasome system." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-1708.
Full textReports on the topic "Ubiquitin"
Royer, Lacey. Cul3 Ubiquitin Ligase and Ctb73 Protein Interactions. Portland State University Library, January 2014. http://dx.doi.org/10.15760/honors.48.
Full textWhitehead, Ian P. A Role for Ubiquitin Binding in Bcr-Abl Transformation. Fort Belvoir, VA: Defense Technical Information Center, June 2008. http://dx.doi.org/10.21236/ada487390.
Full textVierstra, R. D. Mechanism for the selective conjugation of ubiquitin to phytochrome. Office of Scientific and Technical Information (OSTI), January 1990. http://dx.doi.org/10.2172/5229610.
Full textWhitehead, Ian P. A Role for Ubiquitin Binding in Bcr-Abl Transformation. Fort Belvoir, VA: Defense Technical Information Center, June 2009. http://dx.doi.org/10.21236/ada510762.
Full textZhang, Hui. The Role of Ubiquitin E3 Ligase SCFSKP2 in Prostate Cancer Development. Fort Belvoir, VA: Defense Technical Information Center, February 2005. http://dx.doi.org/10.21236/ada435854.
Full textSpruck, Charles H. Identification of Substances for Ubiquitin-Dependent Proteolysis During Breast Tumor Progression. Fort Belvoir, VA: Defense Technical Information Center, October 2008. http://dx.doi.org/10.21236/ada510763.
Full textSchultz, David C. Analysis BAP-1 as a Ubiquitin Hydrolase in the BRCA1 Pathway. Fort Belvoir, VA: Defense Technical Information Center, October 1999. http://dx.doi.org/10.21236/ada392104.
Full textSchultz, David C. Analysis BAP-1 as a Ubiquitin Hydrolase in the BRCA1 Pathway. Fort Belvoir, VA: Defense Technical Information Center, October 2000. http://dx.doi.org/10.21236/ada392881.
Full textDavidge, Brittney. The Cul3 Ubiquitin Ligase: An Essential Regulator of Diverse Cellular Processes. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.5666.
Full textSrikanth, Appikonda. The Role of Ubiquitin-Mediated Proteolysis of Cyclin D in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, April 2005. http://dx.doi.org/10.21236/ada455151.
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