Relevant bibliographies by topics / TIM400

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Academic literature on the topic 'TIM400'

Author: Grafiati
Published: 28 June 2021
Last updated: 2 February 2022

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Journal articles on the topic "TIM400"

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Murphy, Michael P., Danielle Leuenberger, Sean P. Curran, Wolfgang Oppliger, and Carla M. Koehler. "The Essential Function of the Small Tim Proteins in the TIM22 Import Pathway Does Not Depend on Formation of the Soluble 70-Kilodalton Complex." Molecular and Cellular Biology 21, no. 18 (September 15, 2001): 6132–38. http://dx.doi.org/10.1128/mcb.21.18.6132-6138.2001.

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ABSTRACT The TIM22 protein import pathway of the yeast mitochondrion contains several components, including a family of five proteins (Tim8p, -9p, -10p, -12p, and -13p [Tim, for translocase of inner membrane]) that are located in the intermembrane space and are 25% identical. Tim9p and Tim10p have dual roles in mediating the import of inner membrane proteins. Like the Tim8p-Tim13p complex, the Tim9p-Tim10p complex functions as a putative chaperone to guide hydrophobic precursors across the intermembrane space. Like membrane-associated Tim12p, they are members of the Tim18p-Tim22p-Tim54p membrane complex that mediates precursor insertion into the membrane. To understand the role of this family in protein import, we have used a genetic approach to manipulate the complement of the small Tim proteins. A strain has been constructed that lacks the 70-kDa soluble Tim8p-Tim13p and Tim9p-Tim10p complexes in the intermembrane space. Instead, a functional version of Tim9p (Tim9S67Cp), identified as a second-site suppressor of a conditional tim10 mutant, maintains viability. Characterization of this strain revealed that Tim9S67Cp and Tim10p were tightly associated with the inner membrane, the soluble 70-kDa Tim8p-Tim13p and Tim9p-Tim10p complexes were not detectable, and the rate of protein import into isolated mitochondria proceeded at a slower rate. An arrested translocation intermediate bound to Tim9S67Cp was located in the intermembrane space, associated with the inner membrane. We suggest that the 70-kDa complexes facilitate import, similar to the outer membrane receptors of the TOM (hetero-oligomeric translocase of the outer membrane) complex, and the essential role of Tim9p and Tim10p may be to mediate protein insertion in the inner membrane with the TIM22 complex.
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Muñoz-Gómez, Sergio A., Shannon N. Snyder, Samantha J. Montoya, and Jeremy G. Wideman. "Independent accretion of TIM22 complex subunits in the animal and fungal lineages." F1000Research 9 (August 28, 2020): 1060. http://dx.doi.org/10.12688/f1000research.25904.1.

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Background: The mitochondrial protein import complexes arose early in eukaryogenesis. Most of the components of the protein import pathways predate the last eukaryotic common ancestor. For example, the carrier-insertase TIM22 complex comprises the widely conserved Tim22 channel core. However, the auxiliary components of fungal and animal TIM22 complexes are exceptions to this ancient conservation. Methods: Using comparative genomics and phylogenetic approaches, we identified precisely when each TIM22 accretion occurred. Results: In animals, we demonstrate that Tim29 and Tim10b arose early in the holozoan lineage. Tim29 predates the metazoan lineage being present in the animal sister lineages, choanoflagellate and filastereans, whereas the erroneously named Tim10b arose from a duplication of Tim9 at the base of metazoans. In fungi, we show that Tim54 has representatives present in every holomycotan lineage including microsporidians and fonticulids, whereas Tim18 and Tim12 appeared much later in fungal evolution. Specifically, Tim18 and Tim12 arose from duplications of Sdh3 and Tim10, respectively, early in the Saccharomycotina. Surprisingly, we show that Tim54 is distantly related to AGK suggesting that AGK and Tim54 are extremely divergent orthologues and the origin of AGK/Tim54 interaction with Tim22 predates the divergence of animals and fungi. Conclusions: We argue that the evolutionary history of the TIM22 complex is best understood as the neutral structural divergence of an otherwise strongly functionally conserved protein complex. This view suggests that many of the differences in structure/subunit composition of multi-protein complexes are non-adaptive. Instead, most of the phylogenetic variation of functionally conserved molecular machines, which have been under stable selective pressures for vast phylogenetic spans, such as the TIM22 complex, is most likely the outcome of the interplay of random genetic drift and mutation pressure.
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Li, Jingzhi, and Bingdong Sha. "The structure of Tim50(164–361) suggests the mechanism by which Tim50 receives mitochondrial presequences." Acta Crystallographica Section F Structural Biology Communications 71, no. 9 (August 25, 2015): 1146–51. http://dx.doi.org/10.1107/s2053230x15013102.

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Mitochondrial preproteins are transported through the translocase of the outer membrane (TOM) complex. Tim50 and Tim23 then transfer preproteins with N-terminal targeting presequences through the intermembrane space (IMS) across the inner membrane. The crystal structure of the IMS domain of Tim50 [Tim50(164–361)] has previously been determined to 1.83 Å resolution. Here, the crystal structure of Tim50(164–361) at 2.67 Å resolution that was crystallized using a different condition is reported. Compared with the previously determined Tim50(164–361) structure, significant conformational changes occur within the protruding β-hairpin of Tim50 and the nearby helix A2. These findings indicate that the IMS domain of Tim50 exhibits significant structural plasticity within the putative presequence-binding groove, which may play important roles in the function of Tim50 as a receptor protein in the TIM complex that interacts with the presequence and multiple other proteins. More interestingly, the crystal packing indicates that helix A1 from the neighboring monomer docks into the putative presequence-binding groove of Tim50(164–361), which may mimic the scenario of Tim50 and the presequence complex. Tim50 may recognize and bind the presequence helix by utilizing the inner side of the protruding β-hairpin through hydrophobic interactions. Therefore, the protruding β-hairpin of Tim50 may play critical roles in receiving the presequence and recruiting Tim23 for subsequent protein translocations.
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Krimmer, Thomas, Joachim Rassow, Wolf-H. Kunau, Wolfgang Voos, and Nikolaus Pfanner. "Mitochondrial Protein Import Motor: the ATPase Domain of Matrix Hsp70 Is Crucial for Binding to Tim44, while the Peptide Binding Domain and the Carboxy-Terminal Segment Play a Stimulatory Role." Molecular and Cellular Biology 20, no. 16 (August 15, 2000): 5879–87. http://dx.doi.org/10.1128/mcb.20.16.5879-5887.2000.

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ABSTRACT The import motor for preproteins that are targeted into the mitochondrial matrix consists of the matrix heat shock protein Hsp70 (mtHsp70) and the translocase subunit Tim44 of the inner membrane. mtHsp70 interacts with Tim44 in an ATP-dependent reaction cycle, binds to preproteins in transit, and drives their translocation into the matrix. While different functional mechanisms are discussed for the mtHsp70-Tim44 machinery, little is known about the actual mode of interaction of both proteins. Here, we have addressed which of the three Hsp70 regions, the ATPase domain, the peptide binding domain, or the carboxy-terminal segment, are required for the interaction with Tim44. By two independent means, a two-hybrid system and coprecipitation of mtHsp70 constructs imported into mitochondria, we show that the ATPase domain interacts with Tim44, although with a reduced efficiency compared to the full-length mtHsp70. The interaction of the ATPase domain with Tim44 is ATP sensitive. The peptide binding domain and carboxy-terminal segment are unable to bind to Tim44 in the absence of the ATPase domain, but both regions enhance the interaction with Tim44 in the presence of the ATPase domain. We conclude that the ATPase domain of mtHsp70 is essential for and directly interacts with Tim44, clearly separating the mtHsp70-Tim44 interaction from the mtHsp70-substrate interaction.
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Merlin, Alessio, Wolfgang Voos, Ammy C. Maarse, Michiel Meijer, Nikolaus Pfanner, and Joachim Rassow. "The J-related Segment of Tim44 Is Essential for Cell Viability: A Mutant Tim44 Remains in the Mitochondrial Import Site, but Inefficiently Recruits mtHsp70 and Impairs Protein Translocation." Journal of Cell Biology 145, no. 5 (May 31, 1999): 961–72. http://dx.doi.org/10.1083/jcb.145.5.961.

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Tim44 is a protein of the mitochondrial inner membrane and serves as an adaptor protein for mtHsp70 that drives the import of preproteins in an ATP-dependent manner. In this study we have modified the interaction of Tim44 with mtHsp70 and characterized the consequences for protein translocation. By deletion of an 18-residue segment of Tim44 with limited similarity to J-proteins, the binding of Tim44 to mtHsp70 was weakened. We found that in the yeast Saccharomyces cerevisiae the deletion of this segment is lethal. To investigate the role of the 18-residue segment, we expressed Tim44Δ18 in addition to the endogenous wild-type Tim44. Tim44Δ18 is correctly targeted to mitochondria and assembles in the inner membrane import site. The coexpression of Tim44Δ18 together with wild-type Tim44, however, does not stimulate protein import, but reduces its efficiency. In particular, the promotion of unfolding of preproteins during translocation is inhibited. mtHsp70 is still able to bind to Tim44Δ18 in an ATP-regulated manner, but the efficiency of interaction is reduced. These results suggest that the J-related segment of Tim44 is needed for productive interaction with mtHsp70. The efficient cooperation of mtHsp70 with Tim44 facilitates the translocation of loosely folded preproteins and plays a crucial role in the import of preproteins which contain a tightly folded domain.
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Mokranjac, Dejana, Martin Sichting, Dušan Popov-Čeleketić, Koyeli Mapa, Lada Gevorkyan-Airapetov, Keren Zohary, Kai Hell, Abdussalam Azem, and Walter Neupert. "Role of Tim50 in the Transfer of Precursor Proteins from the Outer to the Inner Membrane of Mitochondria." Molecular Biology of the Cell 20, no. 5 (March 2009): 1400–1407. http://dx.doi.org/10.1091/mbc.e08-09-0934.

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Transport of essentially all matrix and a number of inner membrane proteins is governed, entirely or in part, by N-terminal presequences and requires a coordinated action of the translocases of outer and inner mitochondrial membranes (TOM and TIM23 complexes). Here, we have analyzed Tim50, a subunit of the TIM23 complex that is implicated in transfer of precursors from TOM to TIM23. Tim50 is recruited to the TIM23 complex via Tim23 in an interaction that is essentially independent of the rest of the translocase. We find Tim50 in close proximity to the intermembrane space side of the TOM complex where it recognizes both types of TIM23 substrates, those that are to be transported into the matrix and those destined to the inner membrane, suggesting that Tim50 recognizes presequences. This function of Tim50 depends on its association with TIM23. We conclude that the efficient transfer of precursors between TOM and TIM23 complexes requires the concerted action of Tim50 with Tim23.
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Schiller, Dirk, Yu Chin Cheng, Qinglian Liu, William Walter, and Elizabeth A. Craig. "Residues of Tim44 Involved in both Association with the Translocon of the Inner Mitochondrial Membrane and Regulation of Mitochondrial Hsp70 Tethering." Molecular and Cellular Biology 28, no. 13 (April 21, 2008): 4424–33. http://dx.doi.org/10.1128/mcb.00007-08.

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ABSTRACT Translocation of proteins from the cytosol across the mitochondrial inner membrane is driven by the action of the import motor, which is associated with the translocon on the matrix side of the membrane. It is well established that an essential peripheral membrane protein, Tim44, tethers mitochondrial Hsp70 (mtHsp70), the core of the import motor, to the translocon. This Tim44-mtHsp70 interaction, which can be recapitulated in vitro, is destabilized by binding of mtHsp70 to a substrate polypeptide. Here we report that the N-terminal 167-amino-acid segment of mature Tim44 is sufficient for both interaction with mtHsp70 and destabilization of a Tim44-mtHsp70 complex caused by client protein binding. Amino acid alterations within a 30-amino-acid segment affected both the release of mtHsp70 upon peptide binding and the interaction of Tim44 with the translocon. Our results support the idea that Tim44 plays multiple roles in mitochondrial protein import by recruiting Ssc1 and its J protein cochaperone to the translocon and coordinating their interactions to promote efficient protein translocation in vivo.
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Davis, Alison J., Naresh B. Sepuri, Jason Holder, Arthur E. Johnson, and Robert E. Jensen. "Two Intermembrane Space Tim Complexes Interact with Different Domains of Tim23p during Its Import into Mitochondria." Journal of Cell Biology 150, no. 6 (September 18, 2000): 1271–82. http://dx.doi.org/10.1083/jcb.150.6.1271.

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Tim23p (translocase of the inner membrane) is an essential import component located in the mitochondrial inner membrane. To determine how the Tim23 protein itself is transported into mitochondria, we used chemical cross-linking to identify proteins adjacent to Tim23p during its biogenesis. In the absence of an inner membrane potential, Tim23p is translocated across the mitochondrial outer membrane, but not inserted into the inner membrane. At this intermediate stage, we find that Tim23p forms cross-linked products with two distinct protein complexes of the intermembrane space, Tim8p–Tim13p and Tim9p–Tim10p. Tim9p and Tim10p cross-link to the COOH-terminal domain of the Tim23 protein, which carries all of the targeting signals for Tim23p. Therefore, our results suggest that the Tim9p–Tim10p complex plays a key role in Tim23p import. In contrast, Tim8p and Tim13p cross-link to the hydrophilic NH2-terminal segment of Tim23p, which does not carry essential import information and, thus, the role of Tim8p–Tim13p is unclear. Tim23p contains two matrix-facing, positively charged loops that are essential for its insertion into the inner membrane. The positive charges are not required for interaction with the Tim9p–Tim10p complex, but are essential for cross-linking of Tim23p to components of the inner membrane insertion machinery, including Tim54p, Tim22p, and Tim12p.
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Baker, Michael J., Chaille T. Webb, David A. Stroud, Catherine S. Palmer, Ann E. Frazier, Bernard Guiard, Agnieszka Chacinska, Jacqueline M. Gulbis, and Michael T. Ryan. "Structural and Functional Requirements for Activity of the Tim9–Tim10 Complex in Mitochondrial Protein Import." Molecular Biology of the Cell 20, no. 3 (February 2009): 769–79. http://dx.doi.org/10.1091/mbc.e08-09-0903.

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The Tim9–Tim10 complex plays an essential role in mitochondrial protein import by chaperoning select hydrophobic precursor proteins across the intermembrane space. How the complex interacts with precursors is not clear, although it has been proposed that Tim10 acts in substrate recognition, whereas Tim9 acts in complex stabilization. In this study, we report the structure of the yeast Tim9–Tim10 hexameric assembly determined to 2.5 Å and have performed mutational analysis in yeast to evaluate the specific roles of Tim9 and Tim10. Like the human counterparts, each Tim9 and Tim10 subunit contains a central loop flanked by disulfide bonds that separate two extended N- and C-terminal tentacle-like helices. Buried salt-bridges between highly conserved lysine and glutamate residues connect alternating subunits. Mutation of these residues destabilizes the complex, causes defective import of precursor substrates, and results in yeast growth defects. Truncation analysis revealed that in the absence of the N-terminal region of Tim9, the hexameric complex is no longer able to efficiently trap incoming substrates even though contacts with Tim10 are still made. We conclude that Tim9 plays an important functional role that includes facilitating the initial steps in translocating precursor substrates into the intermembrane space.
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Truscott, Kaye N., Nils Wiedemann, Peter Rehling, Hanne Müller, Chris Meisinger, Nikolaus Pfanner, and Bernard Guiard. "Mitochondrial Import of the ADP/ATP Carrier: the Essential TIM Complex of the Intermembrane Space Is Required for Precursor Release from the TOM Complex." Molecular and Cellular Biology 22, no. 22 (November 15, 2002): 7780–89. http://dx.doi.org/10.1128/mcb.22.22.7780-7789.2002.

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ABSTRACT The mitochondrial intermembrane space contains a protein complex essential for cell viability, the Tim9-Tim10 complex. This complex is required for the import of hydrophobic membrane proteins, such as the ADP/ATP carrier (AAC), into the inner membrane. Different views exist about the role played by the Tim9-Tim10 complex in translocation of the AAC precursor across the outer membrane. For this report we have generated a new tim10 yeast mutant that leads to a strong defect in AAC import into mitochondria. Thereby, for the first time, authentic AAC is stably arrested in the translocase complex of the outer membrane (TOM), as shown by antibody shift blue native electrophoresis. Surprisingly, AAC is still associated with the receptors Tom70 and Tom20 when the function of Tim10 is impaired. The nonessential Tim8-Tim13 complex of the intermembrane space is not involved in the transfer of AAC across the outer membrane. These results define a two-step mechanism for translocation of AAC across the outer membrane. The initial insertion of AAC into the import channel is independent of the function of Tim9-Tim10; however, completion of translocation across the outer membrane, including release from the TOM complex, requires a functional Tim9-Tim10 complex.
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Dissertations / Theses on the topic "TIM400"

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Roman, Matej. "Automatizované měření teploty v boji proti COVID." Master's thesis, Vysoké učení technické v Brně. Fakulta elektrotechniky a komunikačních technologií, 2021. http://www.nusl.cz/ntk/nusl-442439.

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This thesis focuses on the development of an open source software capable of automatic face detection in an image captured by a thermal camera, followed by a temperature measuring. This software is supposed to aid in the COVID-19 pandemics. The developed software is independent of used thermal camera. In this thesis, I am using TIM400 thermal camera. The implementation of the face detection was achieved by an OpenCV module. The methods tested were Template Matching, Eigen Faces, and Cascade Classifier. The last-mentioned had the best results, hence was used in the final version of the software. Cascade Classifier is looking for the eyes and their surrounding area in the image, allowing the software to subsequently measure the temperature on the surface of one's forehead. One can therefore be wearing a face mask or a respirator safely. The temperature measuring works in real time and the software is able to capture several people at once. It then keeps a record of the temperature of each measured individual as well as the time of the measurement. The software as a whole is a part of an installation file compatible with the Windows operating system. The functionality of this software was tested – the video recordings are included in this thesis.
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Josyula, Ratnakar. "Structural studies of yeast mitochondrial peripheral membrane protein TIM44." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2009. https://www.mhsl.uab.edu/dt/2009p/josyula.pdf.

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Miyanishi, Masanori. "Identification of Tim4 as a phosphatidylserine receptor." Kyoto University, 2009. http://hdl.handle.net/2433/124269.

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Nishi, Chihiro. "Tim4- and MerTK-Mediated Engulfment of Apoptotic Cells by Mouse Resident Peritoneal Macrophages." Kyoto University, 2016. http://hdl.handle.net/2433/215456.

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© 2014, American Society for Microbiology.
Kyoto University (京都大学)
0048
新制・課程博士
博士(医科学)
甲第19630号
医科博第68号
新制||医科||5(附属図書館)
32666
京都大学大学院医学研究科医科学専攻
(主査)教授 松田 道行, 教授 竹内 理, 教授 杉田 昌彦
学位規則第4条第1項該当
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Guo, Liang. "Structural and functional studies of mitochondrial small Tim proteins." Thesis, University of Manchester, 2013. https://www.research.manchester.ac.uk/portal/en/theses/structural-and-functional-studies-of-mitochondrial-small-tim-proteins(03dde6fd-6692-4af5-9023-b85a33803fcd).html.

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Most mitochondrial proteins are encoded by nuclear DNA, and synthesised in the cytosol, then imported into the different mitochondrial subcompartments. To reach their destination, mitochondrial inner membrane proteins require import across the outer mitochondrial membrane, and through the intermembrane space. This passage through the IMS is assisted by the small Tim proteins. This family is characterised by conserved cysteine residues arranged in a twin CX3C motif. They can form Tim9-Tim10 and Tim8-Tim13 complexes, while Tim12 appears to form part of a Tim9-Tim10-Tim12 complex that is associated with the inner membrane translocase TIM22 complex. Current models suggest that the biogenesis of small Tim proteins and their assembly into complexes is dependent on the redox states of the proteins. However, the role of the conserved cysteine residues, and the disulphide bonds formed by them, in small Tim biogenesis and complex formation is not clear. As there is no research about the structural characterisation of Tim12 and double cysteine mutants of Tim9, purification of these proteins was attempted using different methods. To investigate how cysteine mutants affect complex formation, the purified double cysteine mutants of Tim9 were studied using in vitro methods. It showed that the double cysteine mutants were partially folded, and they can form complexes with Tim10 with low affinities, suggesting disulphide bonds are important for the structures and complex formation of small Tim proteins. The effect of cysteine mutants on mitochondrial function was addressed using in vivo methods. It showed that cysteines of small Tim proteins were not equally essential for cell viability, and growth defect of the lethal cysteine mutant was caused by low level of protein. Thus, the conclusion of this study is that disulphide bond formation is highly important for correct Tim9- Tim10 complex formation, and yeast can survive with low levels of complex, but it results in instability of the individual proteins.
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RAHMAN, Md Bytul Mokaddesur. "NMR analyses on recognition of the mitochondrial targeting signal by Tim50." Thesis, 2014. http://hdl.handle.net/2237/20002.

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Daneschdar, Matin. "Neue Wege zur rekombinanten Oligomerisierung von Peptiden und Proteine über den mitochondrialen Tim10/Tim9-Komplex." Phd thesis, 2010. https://tuprints.ulb.tu-darmstadt.de/2357/1/Dissertation_Matin_Daneschdar.pdf.

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Das Ziel dieser Arbeit war der Aufbau und die Etablierung eines rekombinanten Oligomerisierungsverfahrens von Peptiden und kleinen Proteinen über den mitochondrialen Tim10/Tim9‐Komplex. Das System sollte in Hinsicht auf die Generierung bispezifischer Oligomere, der Oligomerisierung von Proteinen, der Bindung und Modulation pharmazeutisch relevanter Rezeptoren und der chemischen Funktionalisierung untersucht werden. Im ersten Abschnitt der Arbeit erfolgte der Aufbau eines robusten Expressionsystems zur Bereitstellung funktionaliserter Tim10/9‐Komplexe. Es war möglich sowohl ein bicistronisches als auch ein duales Expressionssystem zu etablieren. Beide Systeme stellten funktionalisierte Tim10/Tim9‐Komplexe für weitere Analysen in ausreichender Mengen bereit. Dabei konnte gezeigt werden, dass die Integrität der hexameren Struktur bei N‐ oder C‐terminaler Fusion einer Passagierdomäne an die Tim9‐ oder Tim10‐Untereinheit erhalten bleibt. Der zweite Abschnitt beschäftigte sich mit der Generierung biofunktionaler Tim10/Tim9‐Komplexe. Dabei war es möglich sowohl pseudozyklische Peptide, als auch Cystin‐Knoten‐Mikroproteine über Fusion an den Tim10/Tim9‐Komplex zu oligomeriseren. Es konnte gezeigt werden, dass durch die Oligomeriserung eines VEGFR‐2 spezifischen Bindepeptids über den mitochondrialen Tim10/Tim9‐Komplex eine höhere Affinität gegenüber dem Rezeptor erreicht werden kann. Zudem war es durch die Kombination ErbB2‐ und VEGFR‐2‐bindender Tim10/Tim9‐Komplexe möglich eine bispezifische Variante herzustellen. Bei der Inhibition beider Signaltransduktionswege konnte in verschiedenen Arbeiten ein synergistischer Effekt in Bezug auf die Supression von Tumorwachstum erzielt werden. Als Vertreter der Proteinfamilie konnten hinsichtlich ihrer Faltung komplexe Cystin‐Knoten‐Mikroproteine oligomerisiert werden. Die verwendete Variante ET‐TP‐020 stimulierte in oligomeriserter Form die Proliferation von M‐07e Zellen (humane Megakaryoblasten). Die Stimulation der Zellproliferation setzt eine Darreichung des Bindeproteins in oligomerer Form voraus. Diese Ergebnisse zeigen an, dass die in dieser Arbeit generierten Komplexe auch im zellulären Kontext eine oligomerisierungsabhängige Aktivität aufweisen. Im letzten Abschnitt wurde die Möglichkeit der spezifischen chemischen Funktionalisierung untersucht. Dabei konnte ein Verfahren aufgebaut werden, das durch Oxidation des durch Spaltung mit TEV‐Protease erhaltenen N‐terminalen Serins zu einer Aldehydfunktion eine spezifische Kopplung von Hydrazid‐ oder Thiosemicarbazidderivaten ermöglicht. Dabei konnte gezeigt werden, dass die Kopplung eines Fluorescein‐5‐Thiosemicarbazids spezifisch an die Tim10‐Untereinheit erfolgt und die Integrität des Tim10/Tim9‐Komplexes erhalten bleibt. Die vorliegende Arbeit zeigt, dass eine rekombinante Oligomeriserung pharmazeutisch relevanter Peptide und Proteine über den mitochondrialen Tim10/Tim9‐Komplex möglich ist und die Oligomeriserung zu einer besseren Affinität konjugierter Peptide führen kann. Das hier vorgestellte System ermöglicht zudem eine gerichtete chemische Funktionalisierung bereits rekombinant funktionalisierter mitochondrialer Tim10/Tim9‐Komplexe.
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Schulz, Christian. "Protein interactions along the presequence import pathway." Doctoral thesis, 2013. http://hdl.handle.net/11858/00-1735-0000-0022-5EAD-B.

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Reif, Sebastian [Verfasser]. "Untersuchungen zur Funktion des Tim44-mtHsp70-Komplexes bei der Membraninsertion und Oligomerisierung mitochondrialer Proteine / vorgelegt von Sebastian Reif." 2005. http://d-nb.info/976594978/34.

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Daneschdar, Matin [Verfasser]. "Neue Wege zur rekombinanten Oligomerisierung von Peptiden und Proteinen über den mitochondrialen Tim10-, Tim9-Komplex / von Matin Daneschdar." 2010. http://d-nb.info/100917066X/34.

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Books on the topic "TIM400"

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Times, Occidental Medical. Occidental Medical Times, Combining The Pacific Record Of Medicine And Surgery And The Occidental Medical Times0, Volume 15. Palala Press, 2015.

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Book chapters on the topic "TIM400"

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Turecek, P. L., H. P. Schwarz, N. Barrett, G. Pölsler, F. Dorner, and J. Eibl. "Abreicherung und Inaktivierung von HIV-1 bei der Herstellung von FEIBA® S-TIM4." In 24. Hämophilie-Symposion, 97–102. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-79009-6_18.

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Conference papers on the topic "TIM400"

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Mörsdorf, S., E. Seified, M. Köhler, F. Fasco, P. Hellstern, and G. Pindur. "IN VIVO RECOVERY AND HALF-LIFE OF A STEAM-TREATED FACTOR IX (FIX) CONCENTRATE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644067.

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The introduction of heat treatment of FVIII or FIX concentrates has reduced the risk of infection, however, has raised the question of a reduced haemo-statical effect. Therefore, the in vivo recovery and half-life of a steam-treated FIX concentrate (S-TIM4, Immuno) were investigated in 10 haemophilia B patients from two haemophilia centers. Patients mean age was 33 y (range 17-51 y) and the mean body weight (BW> was 67 kg (range 44-81 kg). Basal FIX levels ranged from 0.007 to 0.03 (median 0,007) U/ml. The patients had not received FIX concentrate at least 7 d prior to the study. Patients 1-4 received 4 different lots, patients 5-10 received one single lot. Blood was drawn before and after 15, 30 min, 1h, 4 h, 8 h, 10 h, 12 h, 24 h and additionally 48 h in patients 1-4. FIX levels were measured using FIX deficient plasma from Immuno (patients 1-10) in center 1, additionally in patients 5-10 using FIX deficient plasma from MerzDade. In vivo recovery and half-life were calculated according to Allain (1980, 1984) and given in % and h, respectively. Results: The table shows the dose and the calculated in vivo recovery and half-life, according to the FIX measurements in center 1 (C1) or center 2 (C2).Although the apparently longer half-life of patients 1-4 may in part be explained by the longer period of FIX measurements in center 1, the exclusive use of one single lot of FIX concentrate suggests an influence of the lot transfused in these patients. However, laboratory signs of DIC were not present.
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Reports on the topic "TIM400"

1

Sankala, Heidi. The Role of Tim50 in Chemoresistance and Oncogenesis of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 2010. http://dx.doi.org/10.21236/ada535626.

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2

Sankala, Heidi. The Role of Tim50 in Chemoresistance and Oncogenesis of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, February 2011. http://dx.doi.org/10.21236/ada545585.

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