Relevant bibliographies by topics / Heterodimerization

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Heterodimerization'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 July 2024

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Journal articles on the topic "Heterodimerization"

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Feng, Xiuyan, Meilin Zhang, Rongbin Guan, and Deborah L. Segaloff. "Heterodimerization Between the Lutropin and Follitropin Receptors is Associated With an Attenuation of Hormone-Dependent Signaling." Endocrinology 154, no. 10 (2013): 3925–30. http://dx.doi.org/10.1210/en.2013-1407.

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The LH receptor (LHR) and FSH receptor (FSHR) are each G protein-coupled receptors that play critical roles in reproductive endocrinology. Each of these receptors has previously been shown to self-associate into homodimers and oligomers shortly after their biosynthesis. As shown herein using bioluminescence resonance energy transfer to detect protein-protein interactions, our data show that the LHR and FSHR, when coexpressed in the same cells, specifically heterodimerize with each other. Further experiments confirm that at least a portion of the cellular LHR/FSHR heterodimers are present on th
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Biener, Eva, Cyril Martin, Nathalie Daniel, et al. "Ovine Placental Lactogen-Induced Heterodimerization of Ovine Growth Hormone and Prolactin Receptors in Living Cells Is Demonstrated by Fluorescence Resonance Energy Transfer Microscopy and Leads to Prolonged Phosphorylation of Signal Transducer and Activator of Transcription (STAT)1 and STAT3." Endocrinology 144, no. 8 (2003): 3532–40. http://dx.doi.org/10.1210/en.2003-0096.

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Abstract HEK-293T cells transiently transfected with ovine (o) GH receptor (GHR) and prolactin receptor (PRLR) constructs respectively tagged downstream with cyan or yellow fluorescent proteins were used to study ovine placental lactogen (oPL)-stimulated heterodimerization by fluorescence resonance energy transfer (FRET) microscopy. The oPL-stimulated transient heterodimerization of GHR and PRLR had a peak occurring 2.5–3 min after oPL application, whereas oGH or oPRL had no effect at all. The results indicate none or only little dimerization occurring before the hormonal stimulation. The effe
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Khoubza, Lamyaa, Franck Chatelain, Sylvain Feliciangeli, Delphine Bichet, and Florian Lesage. "Heterodimerization of TALK Subunits." Biophysical Journal 118, no. 3 (2020): 416a. http://dx.doi.org/10.1016/j.bpj.2019.11.2349.

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Barth, B. U., J. M. Wahlberg, and H. Garoff. "The oligomerization reaction of the Semliki Forest virus membrane protein subunits." Journal of Cell Biology 128, no. 3 (1995): 283–91. http://dx.doi.org/10.1083/jcb.128.3.283.

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The Semliki Forest virus (SFV) spike is composed of three copies of a membrane protein heterodimer. The two subunits of this heterodimer (p62 and E1) are synthesized sequentially from a common mRNA together with the capsid (C) in the order C-p62-E1. In this work heterodimerization of the spike proteins has been studied in BHK 21 cells. The results indicate that: (a) the polyprotein is cotranslationally cleaved into individual chains; (b) the two membrane protein subunits are initially not associated with each other in the endoplasmic reticulum (ER); (c) heterodimerization occurs predominantly
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BERGMAN, Thomas, Vincent C. HENRICH, Uwe SCHLATTNER, and Markus LEZZI. "Ligand control of interaction in vivo between ecdysteroid receptor and ultraspiracle ligand-binding domain." Biochemical Journal 378, no. 3 (2004): 779–84. http://dx.doi.org/10.1042/bj20031302.

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Ecdysteroids (Ecs) enhance the formation of Ec receptor–ultraspiracle protein (EcR–USP) heterodimers which regulate gene transcription. To study EcR–USP heterodimerization, fusion proteins were constructed from the LBDs (ligand-binding domains) of Drosophila EcR or USP and the activation or DNA-binding region of GAL4 respectively. Reporter gene (lacZ) activation was fully dependent on the co-expression of the two fusion proteins and thus constitutes a reliable measure for the interaction in vivo between the two LBDs in the yeast cell. To identify structures involved in heterodimerization, a to
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Andersson, Helena, and Henrik Garoff. "Lectin-Mediated Retention of p62 Facilitates p62-E1 Heterodimerization in Endoplasmic Reticulum of Semliki Forest Virus-Infected Cells." Journal of Virology 77, no. 12 (2003): 6676–82. http://dx.doi.org/10.1128/jvi.77.12.6676-6682.2003.

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ABSTRACT The Semliki Forest virus (SFV) spike subunits p62 and E1 are made from a common coding unit in the order p62-E1. The proteins are separated by the host signal peptidase upon translocation into the endoplasmic reticulum (ER). Shortly thereafter, p62 and E1 form heterodimers. Heterodimerization preferentially occurs between subunits derived from the same translation product, so-called cis heterodimerization. As the p62 protein has the capacity to leave the ER in the absence of E1, it has been postulated that there exists a retention mechanism for the p62 protein, putatively at or near t
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Noppes, Saskia, Simon Franz Müller, Josefine Bennien, et al. "Homo- and heterodimerization is a common feature of the solute carrier family SLC10 members." Biological Chemistry 400, no. 10 (2019): 1371–84. http://dx.doi.org/10.1515/hsz-2019-0148.

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AbstractThe solute carrier family SLC10 consists of seven members, including the bile acid transporters Na+/taurocholate co-transporting polypeptide (NTCP) and apical sodium-dependent bile acid transporter (ASBT), the steroid sulfate transporter SOAT as well as four orphan carriers (SLC10A3, SLC10A4, SLC10A5 and SLC10A7). Previously, homodimerization of NTCP, ASBT and SOAT was described and there is increasing evidence that carrier oligomerization is an important regulatory factor for protein sorting and transport function. In the present study, homo- and heterodimerization were systematically
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Vivat-Hannah, Valerie, William Bourguet, Marco Gottardis, and Hinrich Gronemeyer. "Separation of Retinoid X Receptor Homo- and Heterodimerization Functions." Molecular and Cellular Biology 23, no. 21 (2003): 7678–88. http://dx.doi.org/10.1128/mcb.23.21.7678-7688.2003.

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ABSTRACT As a promiscuous dimerization partner the retinoid X receptor (RXR) can contribute to signaling by multiple nuclear receptors. However, the impact of RXR cosignaling and the possible existence of an RXR homodimer signaling pathway are largely unexplored. We report here on the separation of RXR homo- and heterodimerization as an essential step towards the elucidation of the roles of RXR homo- and heterodimers in retinoid-rexinoid signaling. RXR homodimerization was specifically disrupted by single mutations in the RXR dimerization interface. In contrast, even multiple mutations did not
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Hosaka, Masahiro, and Thomas C. Südhof. "Homo- and Heterodimerization of Synapsins." Journal of Biological Chemistry 274, no. 24 (1999): 16747–53. http://dx.doi.org/10.1074/jbc.274.24.16747.

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Ibrahim, Ahmad A., Divya Nalla, Maxwell Van Raaphorst, and Nessan J. Kerrigan. "Catalytic Asymmetric Heterodimerization of Ketenes." Journal of the American Chemical Society 134, no. 6 (2012): 2942–45. http://dx.doi.org/10.1021/ja211678m.

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Dissertations / Theses on the topic "Heterodimerization"

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Doll, John M. 1976. "Catalysis of tubulin heterodimerization in vivo." Thesis, Massachusetts Institute of Technology, 2004. http://hdl.handle.net/1721.1/32259.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2004.<br>Includes bibliographical references.<br>The heterodimerization of α- and β-tubulin represents a critical early step in microtubule morphogenesis. In vitro studies have defined a pathway that mediates the incorporation of monomeric tubulin polypeptides into heterodimer. The components of this pathway, tubulin cofactors, are dispensable for growth in Saccharomyces cerevisiae under laboratory conditions. Yet, these proteins are required for survival under conditions of stress or in the presence of a weakened tubuli
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Grant, Michael 1976. "The pharmacological and cellular effects of human somatostatin receptor homo- and heterodimerization /." Thesis, McGill University, 2008. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=115682.

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Somatostatin (SST) is a peptide hormone that was originally identified in the hypothalamus and subsequently found throughout the central nervous system and in various peripheral organs. Generally classified as an inhibitory factor, SST is secreted by endocrine, neuronal and immune cells and acts to regulate cell secretion, neurotransmission and cell proliferation. There are five receptor-subtypes known to engage SST, termed SSTR1-5, all belonging to the superfamily of G-protein coupled receptors (GPCRs). Within the past few years, there has been a prepondef8:llce of evidence to suggest the imp
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McVey, Mary. "An investigation of homo and heterodimerization of the human delta opioid receptor." Thesis, University of Glasgow, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.392648.

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Vincent, Karla Kristine. "Transactivation of Beta 2 Adrenergic Receptor by Bradykinin type 2 Receptor via heterodimerization." Diss., Georgia Institute of Technology, 2009. http://hdl.handle.net/1853/37117.

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Although a long standing convention maintained that G Protein Coupled Receptors (GPCRs) exist in the plasma membrane solely as monomers, substantial work over the last two decades has demonstrated that these ubiquitous receptors can and in many cases, preferentially, exist as homodimers, heterodimers, or higher order oligomers. Often, two GPCRs of the same class heterodimerize; it is less common for two GPCRs of different signaling pathways to interact. The work presented here studied the physical and functional interaction of two GPCRs from discrete classes, the Beta 2 Adrenergic Receptor
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Jing, Stanley M. "Cationic Cobalt(I)-Mediated Heterodimerizations: From Mechanistic Insights to Reaction Discovery." The Ohio State University, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=osu1503302900762289.

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Bedi, Shimpi. "Identification of Novel Ligands and Structural Requirements for Heterodimerization of the Liver X Receptor Alpha." Wright State University / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=wright1495630797912988.

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Unlu, Gokhan. "Optimization Of Fret Method To Detect Dimerization Of Dopamine D2 And Adenosine A2a Receptors In Live Cells." Master's thesis, METU, 2011. http://etd.lib.metu.edu.tr/upload/12613365/index.pdf.

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Recent studies demonstrate that there are several G-protein coupled receptors (GPCRs) that dimerize with other GPCRs and form heterodimers. Adenosine A2A-Dopamine D2 receptor interaction is one of the examples for GPCR heterodimerization. Both receptors bear critical roles in physiological processes. Adenosine A2A receptor has functions in neurotransmission, cardiovascular system and immune response. On the other hand, dopamine receptors are the key point of dopaminergic system, which controls the regulation of memory, attention, food intake, endocrine regulation, psychomotor activity and posi
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Akkuzu, Selin. "The Functional Assessment Of Fluorecently Tagged Adenosine A2a And Dopamine D2 Receptors And Qualitative Analysis Of Dimerization Of Adenosine A2a And Dopamine D2 Receptor By Using Fret." Master's thesis, METU, 2013. http://etd.lib.metu.edu.tr/upload/12615474/index.pdf.

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Recently, several studies have demonstrated that G protein coupled receptors exist as homo/heterodimers or oligomers. Adenosine A2A receptors and dopamine D2 receptors are present as both homo- and heterodimer. In the GABAergic striatopallidal neurons A2AR are co- localized with D2 receptors (D2R), and establish functional A2AR-D2R heteromers, which modulates dopaminergic activity. Due to be involved in physiological processes, these receptors bear critical roles. Dopamine receptors play critical role in dopaminergic pathways in regulation of memory, food intake and psychomotor activity, etc.
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Guigues, Adeline. "Interactions entre CCR5 et trois récepteurs couplés aux protéines G : EBI2, A2A et S1P1 : effets sur l'infection par le VIH-1, mécanismes d'action et perspectives thérapeutiques." Thesis, Montpellier, 2017. http://www.theses.fr/2017MONTT048/document.

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Mon laboratoire d’accueil avait montré que la densité de CCR5 à la surface des cellules cibles du VIH détermine très fortement leur infectabilité par les souches virales R5, et que les signaux d’activation cellulaire induits par la fixation virale et transitant par CCR5 favorisent une infection productive des cellules primaires. L’hypothèse de notre travail était que d’autres récepteurs couplés aux protéines G (RCPG) exprimés dans les lymphocytes T CD4+ CCR5+ pourraient également influer sur le cycle de réplication des virus R5. Pour tester cette hypothèse, les RCPGs co-exprimés avec CCR5 dans
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Benleulmi-Chaachoua, Abla. "Etude des partenaires protéiques associés aux homodimères et aux hétérodimères des récepteurs couplés aux protéines G." Thesis, Paris 11, 2014. http://www.theses.fr/2014PA11T018/document.

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La mélatonine est une neuro-hormone secrétée par la glande pinéale pour réguler les rythmes circadiens, le sommeil, la physiologie de la rétine, la reproduction saisonnière et diverses fonctions neuronales. La mélatonine exerce ses fonctions en se liant à deux récepteurs membranaires appelés MT1 et MT2 qui appartiennent à la famille des récepteurs couplés aux protéines G (RCPG). Les RCPG sont connus pour former des homo- et hétérodimères mais la pertinence physiologique de ces complexes reste à démontrer. Plusieurs études montrent que la fonction de ces complexes ne se limite pas à la régulati
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Books on the topic "Heterodimerization"

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Fussner, Eden Margaret. Heterodimerization and oligomerization of the BTB domain. 2006.

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Book chapters on the topic "Heterodimerization"

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Łukasiewicz, Sylwia, Ewa Błasiak, and Marta Dziedzicka-Wasylewska. "5-HT2A Receptor Heterodimerization." In 5-HT2A Receptors in the Central Nervous System. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-70474-6_3.

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Funnell, Alister P. W., and Merlin Crossley. "Homo- and Heterodimerization in Transcriptional Regulation." In Advances in Experimental Medicine and Biology. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-3229-6_7.

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Laviano, Alessandro, and Alessia Mari. "Homodimerization and Heterodimerization of the Ghrelin Receptor." In Central Functions of the Ghrelin Receptor. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0823-3_2.

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Fan, Qing R., William Y. Guo, Yong Geng, and Marisa G. Evelyn. "Class C GPCR: Obligatory Heterodimerization of GABAB Receptor." In G-Protein-Coupled Receptor Dimers. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_12.

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O’Neill, Sharon, and Ulla G. Knaus. "Protein–Protein Interaction Assay to Analyze NOX4/p22phox Heterodimerization." In Methods in Molecular Biology. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9424-3_26.

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Rizzo, Sophie, and Damien Thévenin. "Identifying Transmembrane Interactions in Receptor Protein Tyrosine Phosphatase Homodimerization and Heterodimerization." In Methods in Molecular Biology. Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3569-8_13.

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Zhu, Shanshan, and Michael J. Matunis. "Characterization of the Effects and Functions of Sumoylation Through Rapamycin-Mediated Heterodimerization." In Methods in Molecular Biology. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-566-4_10.

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Achour, Lamia, Maud Kamal, Ralf Jockers, and Stefano Marullo. "Using Quantitative BRET to Assess G Protein-Coupled Receptor Homo- and Heterodimerization." In Methods in Molecular Biology. Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-160-4_9.

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Yin, Xiao-Ming, Zoltán N. Oltvai, and Stanley J. Korsmeyer. "Heterodimerization with Bax is Required for Bcl-2 to Repress Cell Death." In Current Topics in Microbiology and Immunology. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79275-5_38.

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Lavigne, P., L. H. Kondejewski, M. E. Houston, R. S. Hodges, and C. M. Kay. "On the energetics of the heterodimerization of the Max and c-Myc leucine zippers." In Peptides Frontiers of Peptide Science. Springer Netherlands, 2002. http://dx.doi.org/10.1007/0-306-46862-x_203.

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Conference papers on the topic "Heterodimerization"

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Ellebæk, Sofie, Thomas Bouquin, Michael V. Grandal, Michael Kragh, and Thomas T. Poulsen. "Abstract 655: Effect of antibody mixtures on HER-family heterodimerization." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-655.

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Minten, Elizabeth V., Priya Kappor-Vazirani, Chunyang Li, Hui Zhang, Kamakshi Balakrishnan, and David S. Yu. "Abstract PR-002: SIRT2 promotes BRCA1-BARD1 heterodimerization through deacetylation." In Abstracts: AACR Virtual Special Conference on Radiation Science and Medicine; March 2-3, 2021. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1557-3265.radsci21-pr-002.

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BARBIERI, C. M., C. M. THOMSON, and W. W. WARD. "HETERODIMERIZATION BETWEEN BLUE AND GREEN FORMS OF AEQUOREA VICTORIA GFP." In Proceedings of the 11th International Symposium. WORLD SCIENTIFIC, 2001. http://dx.doi.org/10.1142/9789812811158_0003.

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Chen, Ming-Chi, Cynthia Wei-Sheng Lee, and Guan-Yu Zhuo. "Investigating opioid-modulated receptor heterodimerization by two-photon fluorescence microscopy." In Biomedical Imaging and Sensing Conference, edited by Osamu Matoba, Yasuhiro Awatsuji, Yuan Luo, Toyohiko Yatagai, and Yoshihisa Aizu. SPIE, 2023. http://dx.doi.org/10.1117/12.3008159.

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Li, J., H. Liu, I. Espinoza, and R. Lupu. "Heregulin induces Iressa-resistance of breast cancer cells through receptor heterodimerization." In CTRC-AACR San Antonio Breast Cancer Symposium: 2008 Abstracts. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-2016.

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Rudkouskaya, Alena, Jason Smith, Xavier Intes, and Margarida Barroso. "Monitoring receptor heterodimerization along intracellular trafficking pathways using anti-HER2 therapeutic antibodies." In Visualizing and Quantifying Drug Distribution in Tissue V, edited by Conor L. Evans and Kin Foong Chan. SPIE, 2021. http://dx.doi.org/10.1117/12.2578402.

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Casarosa, Paola, and Ines Kollak. "Molecular Interactions Between The Human Muscarinic M3 And ß2 Receptors: Evidence For Heterodimerization." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a6368.

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Scarlett, Kisha, Elshaddai White, Christopher Coke, Jada Carter, LaToya Bryant та Cimona V. Hinton. "Abstract 2512: Agonist-induced heterodimerization between CXCR4 and CB2 inhibits Gα13/RhoA-mediated cell migration". У 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.am2018-2512.

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Eva, Razumienko J., and Raymond M. Reilly. "Abstract 4553: Novel bispecific111In-labeled immunoconjugates (bsICs) for imaging HER2/HER3 heterodimerization in breast cancer." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4553.

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Lamerdin, Jane, Abhishek Saharia, Jennifer Lin-Jones, et al. "Abstract 3742: Detection of EGFR, HER2, HER3 and HER4 homodimerization and heterodimerization using EFC-based cellular assays." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-3742.

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Reports on the topic "Heterodimerization"

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Lemmon, Mark A. Development of Strategies to Manipulate ErbB Receptor Heterodimerization from a Quantitative Analysis of Receptor/Ligand Relationships. Defense Technical Information Center, 2001. http://dx.doi.org/10.21236/ada398353.

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Yarden, Yosef. Erb-2/HER2 Oncogene in Breast Cancer: Does Bivalency of Growth Factors Drive Tumorigenicity Through Receptor Heterodimerization. Defense Technical Information Center, 1999. http://dx.doi.org/10.21236/ada382955.

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Muthuswamy, Senthil K., and Michael E. Gilman. Controlling Homo- & Heterodimerization of ErbB Receptors Using Synthetic Ligands & Understanding the RTK Heterodimer Signaling Specificity in Breast Cancer. Defense Technical Information Center, 1998. http://dx.doi.org/10.21236/ada374289.

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Muthuswamy, Senthil. Controlling Homo- & Heterodimerization of ErbB Receptors Using Synthetic Ligands and Understanding the RTK Heterodimer Signaling Specificity in Breast Cancer. Defense Technical Information Center, 1999. http://dx.doi.org/10.21236/ada382502.

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