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1

Lin, Junyan. "Assembly and function of cytosolic nuclear pore complexes." Electronic Thesis or Diss., Strasbourg, 2024. http://www.theses.fr/2024STRAJ037.

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Les complexes des pores nucléaires (CPN) sont d'énormes assemblages protéiques intégrés dans l'enveloppe nucléaire (EN). Ils servent de structures pour le transport bidirectionnel. Essentiels, ils permettent le maintien de l'équilibre entre le noyau et le cytoplasme. Au-delà de leur résidence dans l'EN, les CPN se trouvent également dans des feuillets du réticulum endoplasmique (RE) empilés connus sous le nom de lamelles annulaires (LA). Cependant, la fonction et les voies régissant la biogenèse des LA restent énigmatiques. Notre investigation dans les cellules de mammifères révèle un mécanism
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Walther, Tobias. "The role of Peripheral Nuclear Pore Complex (NPC) structures in nuclear transport and NPC architecture." Diss., lmu, 2002. http://nbn-resolving.de/urn:nbn:de:bvb:19-4945.

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Kelich, Joseph M. "Single-Molecule Studies on Nuclear Pore Complex Structure and Function." Diss., Temple University Libraries, 2018. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/511772.

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Biology<br>Ph.D.<br>Nuclear pore complexes (NPCs) are large macromolecular gateways embedded in the nuclear envelope of Eukaryotic cells that serve to regulate bi-directional trafficking of particles to and from the nucleus. NPCs have been described as creating a selectively permeable barrier mediating the nuclear export of key endogenous cargoes such as mRNA, and pre-ribosomal subunits as well as allow for the nuclear import of nuclear proteins and some viral particles. Remarkably, other particles that are not qualified for nucleocytoplasmic transport are repelled from the NPC, unable to tran
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Lolodi, Ogheneochukome. "Kinetic analysis of karyopherin-mediated transport through the nuclear pore complex." 京都大学 (Kyoto University), 2016. http://hdl.handle.net/2433/215696.

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Authors are permitted to post the MBoC PDF of their articles (and/or supplemental material) on their personal websites or in an online institutional repository provided there appears always the proper citation of the manuscript in MBoC and a link to the original publication of the manuscript in MBoC (http://www.molbiolcell.org/site/misc/ifora.xhtml)<br>Kyoto University (京都大学)<br>0048<br>新制・課程博士<br>博士(生命科学)<br>甲第19869号<br>生博第350号<br>新制||生||46(附属図書館)<br>32905<br>京都大学大学院生命科学研究科統合生命科学専攻<br>(主査)教授 河内 孝之, 教授 藤田 尚志, 教授 永尾 雅哉<br>学位規則第4条第1項該当
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Liu, Hui-Lin. "Analyses of mitotic nuclear pore complex dynamics in Aspergillus nidulans." The Ohio State University, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=osu1243862963.

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Xu, Xianfeng. "Two sides of the plant nuclear pore complex and a potential link between Ran GTPase and plant cell division." Columbus, Ohio : Ohio State University, 2007. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1190050471.

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Markossian, Sarine W. "Nup2 and a Newly Discovered Nuclear Pore Complex Protein, NupA, Function at Mitotic Chromatin Controlled by the NIMA Kinase." The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1306851345.

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Anderson, Daniel J. "Dynamics of nuclear envelope and nuclear pore complex formation." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2008. http://wwwlib.umi.com/cr/ucsd/fullcit?p3336561.

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Thesis (Ph. D.)--University of California, San Diego, 2008.<br>Title from first page of PDF file (viewed December 16, 2008). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (p. 127-145).
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9

Onischenko, Evgeny. "Disassembly and reassembly of the nuclear pore complex /." Stockholm, 2006. http://diss.kib.ki.se/2006/91-7140-929-7/.

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10

Osmanovic, D. "Polymer theory applied to the nuclear pore complex." Thesis, University College London (University of London), 2014. http://discovery.ucl.ac.uk/1451621/.

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Physically interesting behaviour can arise when soft matter is confined to nanoscale dimensions. A highly relevant biological example of such a phenomenon is the Nuclear Pore Complex (NPC), found perforating the Nuclear Envelope of all eukaryotic cells. In the central conduit of the NPC, of 30-60 nm diameter, a disordered arrangement of proteins regulates all macromolecular transport between the nucleus and the cytoplasm. Its selectivity for larger macromolecules relies on changes in a permeability barrier that is formed by these unstructured proteins, induced by interactions of these proteins
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11

Talamas, Jessica Arielle. "Cell cycle dependent differences in nuclear pore complex assembly." Diss., [La Jolla] : University of California, San Diego, 2010. http://wwwlib.umi.com/cr/ucsd/fullcit?p3403712.

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Thesis (Ph. D.)--University of California, San Diego, 2010.<br>Title from first page of PDF file (viewed June 1, 2010). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (leaves 90-98).
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12

Stanley, George. "Probing the transport barrier of the nuclear pore complex." Thesis, University College London (University of London), 2018. http://discovery.ucl.ac.uk/10061418/.

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The nuclear pore complex (NPC) is the selective gateway through which macromolecules must pass when entering or exiting the nucleus. It is a cog in the gene expression pathway, an entrance to the nucleus exploited by viruses, and a highly-tuned nanoscale filter. The NPC is a large proteinaceous assembly with a central channel occluded by natively disordered proteins, known as FG-nucleoporins (or FG-nups). These FG-nups, along with a family of soluble proteins (known as nuclear transport receptors, or NTRs), form the selective transport barrier. Although much is known about the transport cycle
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13

Suresh, Subbulakshmi. "Nup2: A multifunctional player in nuclear transport and mitotic nuclear pore complex inheritance." The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu1480153558155228.

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Quintana, Star-Lena Jaramillo. "Discrete 3D Model of Molecular Diffusion Through the Nuclear Pore Complex." Master's thesis, Temple University Libraries, 2015. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/343686.

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Mathematics<br>M.S.<br>Nuclear pore complexes (NPCs) are passageways that exist within the nuclear envelope (NE) of a eukaryotic cell. Molecular cargo travel through the passageways to either import to the nucleus or export to the cytoplasm of the cell. Efficient export of certain cargo is necessary for maintained health of a cell, and hence, the organism. Traditional methods of observing NPCs lack resolution great enough for scientists to study the many interactions that take place inside of the complex. A discrete 3D model of the molecular diffusion was built to understand how cargo moves th
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Bestembayeva, A. "Biophysical properties of the transport barrier in the nuclear pore complex." Thesis, University College London (University of London), 2016. http://discovery.ucl.ac.uk/1474430/.

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The Nuclear Pore Complex (NPC) is a large protein structure found in eukaryotic cells, perforating the nuclear envelope. It mediates bidirectional selective transport between the nucleus and the cytoplasm. The NPC contains a permeability barrier consisting of unstructured nuclear pore proteins. The structure of the permeability barrier is not well defined. As a consequence, various models have been proposed for its structure and functionality. Typically, these models consider the unstructured nuclear pore proteins as weakly or strongly interacting polymers: In the first case nuclear pore prote
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Mossaid, Ikram. "The nuclear pore protein Nup153: Dissecting its role in nuclear envelope and nuclear pore complex architecture and its interaction with the spindle assembly checkpoint protein Mad1." Doctoral thesis, Universite Libre de Bruxelles, 2016. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/234375.

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Nuclear pore complexes (NPCs) are embedded in the nuclear envelope (NE) and composed of proteins called nucleoporins. NPCs as such control the bidirectional traffic of proteins and RNAs between the nucleus and the cytoplasm in eukaryotic cells whereas individual nucleoporins were found to be implicated in other cellular processes such as, cell division, kinetochore assembly, gene expression and cell migration. A prime example for nucleoporin functional versatility can be seen in Nup153. Nup153 is since its discovery known to be a central player in nucleocytoplasmic transport, but additionally
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Kelley, Kotaro. "Structural and biochemical characterization of nuclear pore complex structural scaffold sub-complexes." Thesis, Massachusetts Institute of Technology, 2017. http://hdl.handle.net/1721.1/113466.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2017<br>Cataloged from PDF version of thesis.<br>Includes bibliographical references.<br>The nuclear pore complex (NPC) is a large, modular protein assembly that regulates nucleocytoplasmic transport in all eukaryotes. The ~60-120 MDa NPC is a modular assembly of multiple copies of ~30 distinct proteins that are arranged into biochemically distinct sub-complexes. We believe that the structural characterization of the NPC is essential for understanding its transport mechanisms and various pathologies and human disease
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18

Hamed, Mohamed [Verfasser]. "A nuclear export sequence in Nup214 promotes its targeting to the nuclear pore complex / Mohamed Hamed." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2020. http://d-nb.info/1220504505/34.

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Hase, Manuela. "Molecular and ultrastructural analysis of Tpr, a nuclear pore complex-attached coiled-coil protein /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-525-5/.

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Loeb, Jonathan David Joshua. "Molecular characterization of components of the nuclear pore complex and the nuclear import system in Saccharomyces cerevisiae." Thesis, Massachusetts Institute of Technology, 1995. http://hdl.handle.net/1721.1/33532.

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Sachdev, Ruchika [Verfasser], and Ralf-Peter [Akademischer Betreuer] Jansen. "Functional Characterization of the Nup93 Complex in Nuclear Pore Complex Assembly / Ruchika Sachdev ; Betreuer: Ralf-Peter Jansen." Tübingen : Universitätsbibliothek Tübingen, 2013. http://d-nb.info/1162844442/34.

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Zhang, Wanzhen. "Redox-dependent regulation of molecular crowding barrier in the nuclear pore." Doctoral thesis, Kyoto University, 2021. http://hdl.handle.net/2433/263794.

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Zimmerli, Christian Eugen [Verfasser], and Ed [Akademischer Betreuer] Hurt. "In cellulo architecture of the nuclear pore complex / Christian Eugen Zimmerli ; Betreuer: Ed Hurt." Heidelberg : Universitätsbibliothek Heidelberg, 2020. http://d-nb.info/1233867547/34.

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Chalhoub, Antonious. "The Amyotrophic Lateral Sclerosis 8 Mutant VAPB-P56S Causes a Nuclear Envelope and Nuclear Pore Defect." Thèse, Université d'Ottawa / University of Ottawa, 2012. http://hdl.handle.net/10393/23191.

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A P56S mutation in the VAPB MSP domain is linked to adult-onset amyotrophic lateral sclerosis 8. The objective of this study is to characterize the functional role of VAPB in transport of NE and NPC proteins from the ER to the NE. Over-expression of VAPB-P56S blocked the transport of nucleoporins (Nups) and NE proteins, resulting in their sequestration in dilated cytoplasmic membranes. Simultaneous overexpression of the FFAT motif (two phenylalanines in an acidic track) antagonizes mutant VAPB effects and restores transport to the NE. VAPB function is required for transport to the NE because k
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Nordeen, Sarah Ann. "A nanobody suite for yeast scaffold nucleoporins provides details of the Y complex structure and nuclear pore complex assembly." Thesis, Massachusetts Institute of Technology, 2020. https://hdl.handle.net/1721.1/127138.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, May, 2020<br>Cataloged from the official PDF of thesis.<br>Includes bibliographical references.<br>Nuclear pore complexes (NPCs) are the main conduits for molecular exchange across the nuclear envelope. The NPC is a modular assembly of ~500 individual proteins, called nucleoporins or nups, that can be classified into three categories: 1. Stably associated scaffolding nups, 2. Peripheral nups, and 3. Phenylalanine-glycine (FG) repeat containing nups that form the permeability barrier of the NPC. Most scaffolding nups
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Orjalo, Arturo V. "Functional analysis of the Nup107-160 complex, the major subunit of the vertebrate nuclear pore /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2005. http://wwwlib.umi.com/cr/ucsd/fullcit?p3190168.

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Partridge, James R. (James Robert). "Biophysical and structural characterization of components from the nuclear pore complex and the ubiquitin pathway." Thesis, Massachusetts Institute of Technology, 2010. http://hdl.handle.net/1721.1/57994.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2010.<br>Cataloged from PDF version of thesis.<br>Includes bibliographical references (p. 136-151).<br>Formation of an endomembrane system in the eukaryotic cell is a hallmark of biological evolution. One such system is the nuclear envelope (NE), composed of an inner and outer membrane, used to form a nucleus and enclose the cell's genome. Access to the nucleus from the cytoplasm is mediated by a massive macromolecular machine called the nuclear pore complex (NPC). The NPC resides as a circular opening embedded in the NE
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Brohawn, Stephen Graf. "Structural elucidation of a common architecture of the nuclear pore complex and COPIl vesicle coats." Thesis, Massachusetts Institute of Technology, 2010. http://hdl.handle.net/1721.1/58396.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2010.<br>Cataloged from PDF version of thesis.<br>Includes bibliographical references (p. 156-169).<br>Nuclear pore complexes (NPCs) are massive protein assemblies that perforate the nuclear envelope and form the exclusive passageway for nucleocytoplasmic transport. NPCs play critical roles in molecular transport and a myriad of other cellular processes. Elucidation of the structure of the NPC is thus expected to provide important insight into cell biology. In this thesis, I investigate the structure of a key subcomplex
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Khalaf, Bouchra. "Beyond the Nuclear Pore Complex, Nup358 Clusters at the Axon Initial Segment of Cultured Neurons." Doctoral thesis, Università degli studi di Trento, 2018. https://hdl.handle.net/11572/368993.

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Nup358 is the largest nucleoporin of around 358 kDa molecular weight that localizes on the cytoplasmic face of the nuclear pore complex (NPC). It takes part in the overall activity of the NPC mediating the transport of nucleic acids and proteins between the nucleus and the cytoplasm. However, due to its multi-domain configuration, Nup358 has a more pleiotropic function in several cellular mechanisms such as mediating the stability of microtubules and axon specification. Since little is known about the non-conventional role of Nup358 in neuronal polarity, my PhD thesis was focused on characteri
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Khalaf, Bouchra. "Beyond the Nuclear Pore Complex, Nup358 Clusters at the Axon Initial Segment of Cultured Neurons." Doctoral thesis, University of Trento, 2018. http://eprints-phd.biblio.unitn.it/2971/3/Thesis_BKhalaf.pdf.

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Nup358 is the largest nucleoporin of around 358 kDa molecular weight that localizes on the cytoplasmic face of the nuclear pore complex (NPC). It takes part in the overall activity of the NPC mediating the transport of nucleic acids and proteins between the nucleus and the cytoplasm. However, due to its multi-domain configuration, Nup358 has a more pleiotropic function in several cellular mechanisms such as mediating the stability of microtubules and axon specification. Since little is known about the non-conventional role of Nup358 in neuronal polarity, my PhD thesis was focused on characteri
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Enninga, Jost. "Studies on the characterization and regulation of two major nuclear pore complex proteins Nup98 and Nup96." [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972566570.

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Tabarraei, Alijan. "Studies on the interaction of HSV-1 multifunctional protein ICP27 with the nuclear pore complex proteins." Thesis, University of Glasgow, 2009. http://theses.gla.ac.uk/750/.

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Herpes simplex virus (HSV-1) ICP27 is a multifunctional immediate early (IE) protein, required for expression of several early and late genes and acts at transcriptional and posttranscriptional levels. ICP27 contains both a nuclear localization signal and a nuclear export signal and shuttles between the nucleus and the cytoplasm. It interacts directly with various cellular proteins including REF and cellular mRNA export receptor TAP to export viral mRNAs. However other transport mechanisms may also be employed. All transport across the nuclear envelope must occur via the nuclear pore complex,
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Capra, T. "THE DNA DAMAGE CHECKPOINT PRESERVES REPLICATION FORK INTEGRITY BY REGULATING TRANSCRIBED GENES ASSOCIATION TO THE NUCLEAR PORE COMPLEX." Doctoral thesis, Università degli Studi di Milano, 2010. http://hdl.handle.net/2434/150161.

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Genome instability, defined as the occurrence and amplification of mutations and chromosomal rearrangements, is a hallmark of neoplasic transformation and cancer onset. Cells have evolved DNA damage checkpoint processes that act in response to replicative stress induced by genotoxic agents. In Saccharomyces cerevisiae the DNA damage checkpoint requires the essential- Rad53 kinase. Checkpoint-defective cells accumulate gross chromosomal rearrangements and loose viability following exposure to hydroxyurea (HU), mainly due to their failure to stabilize stalled replication forks. In this work I sh
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Olsson, Magnus. "Nuclear pore membrane glycoprotein 210 as a new marker for epithelial cells." Doctoral thesis, Uppsala University, Department of Cell and Molecular Biology, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3265.

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<p>Epithelial cell polarisation is a prerequisite for the branching morphogenesis in several organs. Differential screening techniques were used to identify genes, which are upregulated during induction of epithelium in early kidney development. This investigation revealed two separate genes, Nuclear localising protein 1 (Nulp1), a previously undescribed gene with sequence characteristics of the basic helix-loop-helix transcription factor family, and glycoprotein 210 (gp210, POM210), an integral membrane protein constituent of the nuclear pore complex (NPC). Of these, gp210 was found to be upr
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Monette, Anne. "The remodelling of the nuclear pore complex by human immunodeficiency virus type 1: proteomic analysis and biological significance." Thesis, McGill University, 2011. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=96805.

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Human immunodeficiency virus type 1 (HIV-1) commandeers host proteins and cellular machineries to its advantage at every step of its replication cycle. This work initially shows that HIV-1 infection causes enhanced expression of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) and promotes its cytoplasmic retention; and that this is dependent on the nuclear export of the unspliced viral genomic RNA (vRNA) and to alterations in the abundance and localization of nucleoporin p62 (Nup62). HnRNP A1 and the vRNA remain colocalized in the cytoplasm where hnRNP A1 acts as an internal ribosomal
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Farr, Julia Christina [Verfasser], and Berenike [Akademischer Betreuer] Maier. "Structural and functional analysis of the nuclear pore complex in Saccharomyces cerevisiae / Julia Christina Farr ; Betreuer: Berenike Maier." Münster : Universitäts- und Landesbibliothek Münster, 2009. http://d-nb.info/1140917676/34.

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Vollmer, Benjamin [Verfasser], and Wolfram [Akademischer Betreuer] Antonin. "The membrane interaction of Nup53 and its implication in nuclear pore complex assembly / Benjamin Vollmer ; Betreuer: Wolfram Antonin." Tübingen : Universitätsbibliothek Tübingen, 2015. http://d-nb.info/1163321087/34.

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Bangs, Peter Lawrence. "Cloning, Characterization and Functional Analysis of TPR, an Oncogene-Activating Protein of the Nuclear Pore Complex: A Dissertation." eScholarship@UMMS, 1998. http://escholarship.umassmed.edu/gsbs_diss/146.

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A monoclonal antibody, mAb 203.37, raised against purified nuclear matrix proteins identified a single ~270 kDa protein that localized to the nuclear envelope. Double-label immunofluorescent microscopy using differential permeabilization protocols showed that this protein was present exclusively on the nucleoplasmic side of the nuclear envelope and that it co-localized with components of the nuclear pore complex. The nucleotide sequence of clones isolated using mAb 203.37 identified this protein as Tpr, a protein previously shown to be involved in oncogenic fusions with a number of protein kin
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Al-Haboubi, Teiba. "Characterisation of the molecular links between the nuclear pore complex and the nuclear lamins and reconstitution of the xenopus oocyte lamin assembly in vitro /." [S.l.] : [s.n.], 2009. http://edoc.unibas.ch/diss/DissB_8778.

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Apelt, Luise Karin [Verfasser]. "Investigation of the binary protein-protein interactions of the yeast and the human nuclear pore complex / Luise Karin Apelt." Berlin : Freie Universität Berlin, 2015. http://d-nb.info/1073868710/34.

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Sarma, Ashapurna. "A Single Molecule Study of Calcium Effect on Nuclear Transport." Bowling Green State University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1282326584.

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De, Magistris Paola [Verfasser], and Wolfram [Akademischer Betreuer] Antonin. "Functional characterization of the nucleoporins Nup50 and Nup155 in postmitotic nuclear pore complex assembly / Paola De Magistris ; Betreuer: Wolfram Antonin." Tübingen : Universitätsbibliothek Tübingen, 2019. http://d-nb.info/1198859067/34.

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Collins, Patrick. "The Characterisation of Putative Nuclear Pore-Anchoring Proteins in Arabidopsis thaliana." Thesis, University of Canterbury. Biological Sciences, 2013. http://hdl.handle.net/10092/8885.

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The nuclear pore complex (NPC) is perhaps the largest protein complex in the eukaryotic cell, and controls the movement of molecules across the nuclear envelope. The NPC is composed of up to 30 proteins termed nucleoporins (Nups), each grouped in different sub-complexes. The transmembrane ring sub-complex is composed of Nups responsible for anchoring the NPC to the nuclear envelope. Bioinformatic analysis has traced all major sub-complexes of the NPC back to the last eukaryotic common ancestor, meaning that the nuclear pore structure and function is conserved amongst all eukaryotes. In this st
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Floch, Aurélie. "Mécanismes d'adressage de Pom33, protéine transmembranaire associée aux pores nucléaires chez la levure Saccharomyces cerevisiae levure Saccharomyces cerevisiae." Thesis, Paris 11, 2014. http://www.theses.fr/2014PA112182.

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Chez les eucaryotes, les pores nucléaires (NPCs), ancrés dans l’enveloppe nucléaire (EN), régulent les échanges nucléocytoplasmiques. Ces complexes, très conservés, sont composés d’une trentaine de protéines appelées nucléoporines (Nups) présentes en multiples copies au sein de chaque NPC. Chez la levure S. cerevisiae, seules quatre Nups, dont la protéine Pom33, possèdent des domaines transmembranaires. Une étude réalisée en amont de ce projet a permis de caractériser Pom33 et de montrer que le mutant pom33∆ est viable et ne présente pas de défaut apparent de transport nucléocytoplasmique mais
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Matreyek, Kenneth Anzai. "HIV-1 capsid engages nucleoporin NUP153 to promote viral nuclear entry." Thesis, Harvard University, 2013. http://dissertations.umi.com/gsas.harvard:11210.

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Lentiviruses can infect non-dividing cells, and various cellular nuclear transport proteins provide crucial functions for lentiviral nuclear entry and integration. Genome-wide small interfering RNA screens previously identified nuclear pore complex component nucleoporin 153 (NUP153) as being important for infection by human immunodeficiency virus type 1 (HIV-1). We found that HIV-1 infection of NUP153 depleted cells resulted in normal levels of reverse transcription, a moderate reduction of 2-long terminal repeat circles, and a relatively large reduction in integrated proviruses, consistent wi
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Jimenez, Sabinina Vilma [Verfasser], and Ed [Akademischer Betreuer] Hurt. "Analysis of the Architecture of the Nuclear Pore Complex by 3D super-resolution fluorescence microscopy / Vilma Jimenez Sabinina ; Betreuer: Ed Hurt." Heidelberg : Universitätsbibliothek Heidelberg, 2019. http://d-nb.info/1201346363/34.

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Eisenhardt, Nathalie [Verfasser], and Wolfram [Akademischer Betreuer] Antonin. "Functional characterisation of the interplay between Ndc1, Nup53 and Nup155 in nuclear pore complex biogenesis / Nathalie Eisenhardt ; Akademischer Betreuer: Wolfram Antonin." Tübingen : Universitätsbibliothek Tübingen, 2014. http://d-nb.info/1163239968/34.

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Böhmer, Thomas. "Functional and structural dissection of Nup107 and Nup133, two members of the Nup107-160 subcomplex, linchpin of the vertebrate nuclear pore complex." [S.l. : s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=975117866.

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Marelli, Marcello. "The yeast nucleoporin Nup53p provides a specific binding site for the karyopherin Kap121p and has a role in nuclear pore complex assembly." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0013/NQ59631.pdf.

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Mackmull, Marie-Therese [Verfasser], and Darren [Akademischer Betreuer] Gilmour. "The landscape of the nucleocytoplasmic transport system and cell-type specific variations of the nuclear pore complex / Marie-Therese Mackmull ; Betreuer: Darren Gilmour." Heidelberg : Universitätsbibliothek Heidelberg, 2017. http://d-nb.info/1180985680/34.

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