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Academic literature on the topic 'Tim22'

Author: Grafiati

Published: 6 September 2023

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Journal articles on the topic "Tim22"

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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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Koehler, Carla M., Michael P. Murphy, Nikolaus A. Bally, Danielle Leuenberger, Wolfgang Oppliger, Luisita Dolfini, Tina Junne, Gottfried Schatz, and Eran Or. "Tim18p, a New Subunit of the TIM22 Complex That Mediates Insertion of Imported Proteins into the Yeast Mitochondrial Inner Membrane." Molecular and Cellular Biology 20, no. 4 (February 15, 2000): 1187–93. http://dx.doi.org/10.1128/mcb.20.4.1187-1193.2000.

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ABSTRACT Import of carrier proteins from the cytoplasm into the mitochondrial inner membrane of yeast is mediated by a distinct system consisting of two soluble 70-kDa protein complexes in the intermembrane space and a 300-kDa complex in the inner membrane, the TIM22 complex. The TIM22 complex contains the peripheral subunits Tim9p, Tim10p, and Tim12p and the integral membrane subunits Tim22p and Tim54p. We identify here an additional subunit, an 18-kDa integral membrane protein termed Tim18p. This protein is made as a 21.9-kDa precursor which is imported into mitochondria and processed to its mature form. When mitochondria are gently solubilized, Tim18p comigrates with the other subunits of the TIM22 complex on nondenaturing gels and is coimmunoprecipitated with Tim54p and Tim12p. Tim18p does not cofractionate with the TIM23 complex upon immunoprecipitation or nondenaturing gel electrophoresis. Deletion of Tim18p decreases the growth rate of yeast cells by a factor of two and is synthetically lethal with temperature-sensitive mutations in Tim9p or Tim10p. It also impairs the import of several precursor proteins into isolated mitochondria, and lowers the apparent mass of the TIM22 complex. We suggest that Tim18p functions in the assembly and stabilization of the TIM22 complex but does not directly participate in protein insertion into the inner membrane.

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Kerscher, Oliver, Jason Holder, Maithreyan Srinivasan, Roxanne S. Leung, and Robert E. Jensen. "The Tim54p–Tim22p Complex Mediates Insertion of Proteins into the Mitochondrial Inner Membrane." Journal of Cell Biology 139, no. 7 (December 29, 1997): 1663–75. http://dx.doi.org/10.1083/jcb.139.7.1663.

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We have identified a new protein, Tim54p, located in the yeast mitochondrial inner membrane. Tim54p is an essential import component, required for the insertion of at least two polytopic proteins into the inner membrane, but not for the translocation of precursors into the matrix. Several observations suggest that Tim54p and Tim22p are part of a protein complex in the inner membrane distinct from the previously characterized Tim23p-Tim17p complex. First, multiple copies of the TIM22 gene, but not TIM23 or TIM17, suppress the growth defect of a tim54-1 temperature-sensitive mutant. Second, Tim22p can be coprecipitated with Tim54p from detergent-solubilized mitochondria, but Tim54p and Tim22p do not interact with either Tim23p or Tim17p. Finally, the tim54-1 mutation destabilizes the Tim22 protein, but not Tim23p or Tim17p. Our results support the idea that the mitochondrial inner membrane carries two independent import complexes: one required for the translocation of proteins across the inner membrane (Tim23p–Tim17p), and the other required for the insertion of proteins into the inner membrane (Tim54p–Tim22p).

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Hwang, David K., Steven M. Claypool, Danielle Leuenberger, Heather L. Tienson, and Carla M. Koehler. "Tim54p connects inner membrane assembly and proteolytic pathways in the mitochondrion." Journal of Cell Biology 178, no. 7 (September 24, 2007): 1161–75. http://dx.doi.org/10.1083/jcb.200706195.

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Tim54p, a component of the inner membrane TIM22 complex, does not directly mediate the import of inner membrane substrates but is required for assembly/stability of the 300-kD TIM22 complex. In addition, Δtim54 yeast exhibit a petite-negative phenotype (also observed in yeast harboring mutations in the F1Fo ATPase, the ADP/ATP carrier, mitochondrial morphology components, or the i–AAA protease, Yme1p). Interestingly, other import mutants in our strain background are not petite-negative. We report that Tim54p is not involved in maintenance of mitochondrial DNA or mitochondrial morphology. Rather, Tim54p mediates assembly of an active Yme1p complex, after Yme1p is imported via the TIM23 pathway. Defective Yme1p assembly is likely the major contributing factor for the petite-negativity in strains lacking functional Tim54p. Thus, Tim54p has two independent functions: scaffolding/stability for the TIM22 membrane complex and assembly of Yme1p into a proteolytically active complex. As such, Tim54p links protein import, assembly, and turnover pathways in the mitochondrion.

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VERGNOLLE, Maïlys A. S., Helen SAWNEY, Tina JUNNE, Luisita DOLFINI, and Kostas TOKATLIDIS. "A cryptic matrix targeting signal of the yeast ADP/ATP carrier normally inserted by the TIM22 complex is recognized by the TIM23 machinery." Biochemical Journal 385, no. 1 (December 14, 2004): 173–80. http://dx.doi.org/10.1042/bj20040650.

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The yeast ADP/ATP carrier (AAC) is a mitochondrial protein that is targeted to the inner membrane via the TIM10 and TIM22 translocase complexes. AAC is devoid of a typical mitochondrial targeting signal and its targeting and insertion are thought to be guided by internal amino acid sequences. Here we show that AAC contains a cryptic matrix targeting signal that can target up to two thirds of the N-terminal part of the protein to the matrix. This event is coordinated by the TIM23 translocase and displays all the features of the matrix-targeting pathway. However, in the context of the whole protein, this signal is ‘masked’ and rendered non-functional as the polypeptide is targeted to the inner membrane via the TIM10 and TIM22 translocases. Our data suggest that after crossing the outer membrane the whole polypeptide chain of AAC is necessary to commit the precursor to the TIM22-mediated inner membrane insertion pathway.

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Kumar, Abhishek, Srujan Kumar Matta, and Patrick D'Silva. "Conserved regions of budding yeast Tim22 have a role in structural organization of the carrier translocase." Journal of Cell Science 133, no. 14 (June 26, 2020): jcs244632. http://dx.doi.org/10.1242/jcs.244632.

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ABSTRACTMitochondrial biogenesis requires efficient sorting of various proteins into different mitochondrial sub-compartments, mediated by dedicated protein machinery present in the outer and inner membrane. Among them, the TIM22 complex enables the integration of complex membrane proteins with internal targeting signals into the inner membrane. Although the Tim22 protein forms the core of the complex, the dynamic recruitment of subunits to the channel is still enigmatic. In this study, we highlight that the intermembrane space (IMS) and transmembrane 4 (TM4) regions of Tim22 are critically required for interactions with the membrane-embedded subunits, including Tim54, Tim18, and Sdh3, and thereby maintain the functional architecture of the TIM22 translocase. Furthermore, we find that the TM1 and TM2 regions of Tim22 are important for association with Tim18, whereas TM3 is exclusively required for the interaction with Sdh3. Moreover, impairment of TIM22 complex assembly influences its translocase activity, the mitochondrial network, and the viability of cells lacking mitochondrial DNA. Overall, our findings provide compelling evidence highlighting the significance of conserved regions of Tim22 that are important for the maintenance of the TIM22 complex and mitochondrial integrity.

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Wrobel, Lidia, Agata Trojanowska, Malgorzata E. Sztolsztener, and Agnieszka Chacinska. "Mitochondrial protein import: Mia40 facilitates Tim22 translocation into the inner membrane of mitochondria." Molecular Biology of the Cell 24, no. 5 (March 2013): 543–54. http://dx.doi.org/10.1091/mbc.e12-09-0649.

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The mitochondrial intermembrane space assembly (MIA) pathway is generally considered to be dedicated to the redox-dependent import and biogenesis of proteins localized to the intermembrane space of mitochondria. The oxidoreductase Mia40 is a central component of the pathway responsible for the transfer of disulfide bonds to intermembrane space precursor proteins, causing their oxidative folding. Here we present the first evidence that the function of Mia40 is not restricted to the transport and oxidative folding of intermembrane space proteins. We identify Tim22, a multispanning membrane protein and core component of the TIM22 translocase of inner membrane, as a protein with cysteine residues undergoing oxidation during Tim22 biogenesis. We show that Mia40 is involved in the biogenesis and complex assembly of Tim22. Tim22 forms a disulfide-bonded intermediate with Mia40 upon import into mitochondria. Of interest, Mia40 binds the Tim22 precursor also via noncovalent interactions. We propose that Mia40 not only is responsible for disulfide bond formation, but also assists the Tim22 protein in its integration into the inner membrane of mitochondria.

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Kurz, Martin, Heiko Martin, Joachim Rassow, Nikolaus Pfanner, and Michael T. Ryan. "Biogenesis of Tim Proteins of the Mitochondrial Carrier Import Pathway: Differential Targeting Mechanisms and Crossing Over with the Main Import Pathway." Molecular Biology of the Cell 10, no. 7 (July 1999): 2461–74. http://dx.doi.org/10.1091/mbc.10.7.2461.

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Two major routes of preprotein targeting into mitochondria are known. Preproteins carrying amino-terminal signals mainly use Tom20, the general import pore (GIP) complex and the Tim23–Tim17 complex. Preproteins with internal signals such as inner membrane carriers use Tom70, the GIP complex, and the special Tim pathway, involving small Tims of the intermembrane space and Tim22–Tim54 of the inner membrane. Little is known about the biogenesis and assembly of the Tim proteins of this carrier pathway. We report that import of the preprotein of Tim22 requires Tom20, although it uses the carrier Tim route. In contrast, the preprotein of Tim54 mainly uses Tom70, yet it follows the Tim23–Tim17 pathway. The positively charged amino-terminal region of Tim54 is required for membrane translocation but not for targeting to Tom70. In addition, we identify two novel homologues of the small Tim proteins and show that targeting of the small Tims follows a third new route where surface receptors are dispensable, yet Tom5 of the GIP complex is crucial. We conclude that the biogenesis of Tim proteins of the carrier pathway cannot be described by either one of the two major import routes, but involves new types of import pathways composed of various features of the hitherto known routes, including crossing over at the level of the GIP.

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Weems, Ebony, Ujjal K. Singha, VaNae Hamilton, Joseph T. Smith, Karin Waegemann, Dejana Mokranjac, and Minu Chaudhuri. "Functional Complementation Analyses Reveal that the Single PRAT Family Protein of Trypanosoma brucei Is a Divergent Homolog of Tim17 in Saccharomyces cerevisiae." Eukaryotic Cell 14, no. 3 (January 9, 2015): 286–96. http://dx.doi.org/10.1128/ec.00203-14.

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ABSTRACT Trypanosoma brucei , a parasitic protozoan that causes African trypanosomiasis, possesses a single member of the presequence and amino acid transporter (PRAT) protein family, which is referred to as TbTim17. In contrast, three homologous proteins, ScTim23, ScTim17, and ScTim22, are found in Saccharomyces cerevisiae and higher eukaryotes. Here, we show that TbTim17 cannot rescue Tim17, Tim23, or Tim22 mutants of S. cerevisiae . We expressed S. cerevisiae Tim23, Tim17, and Tim22 in T. brucei . These heterologous proteins were properly imported into mitochondria in the parasite. Further analysis revealed that although ScTim23 and ScTim17 were integrated into the mitochondrial inner membrane and assembled into a protein complex similar in size to TbTim17, only ScTim17 was stably associated with TbTim17. In contrast, ScTim22 existed as a protease-sensitive soluble protein in the T. brucei mitochondrion. In addition, the growth defect caused by TbTim17 knockdown in T. brucei was partially restored by the expression of ScTim17 but not by the expression of either ScTim23 or ScTim22, whereas the expression of TbTim17 fully complemented the growth defect caused by TbTim17 knockdown, as anticipated. Similar to the findings for cell growth, the defect in the import of mitochondrial proteins due to depletion of TbTim17 was in part restored by the expression of ScTim17 but was not complemented by the expression of either ScTim23 or ScTim22. Together, these results suggest that TbTim17 is divergent compared to ScTim23 but that its function is closer to that of ScTim17. In addition, ScTim22 could not be sorted properly in the T. brucei mitochondrion and thus failed to complement the function of TbTim17.

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Horten, Patrick, Lilia Colina-Tenorio, and Heike Rampelt. "Biogenesis of Mitochondrial Metabolite Carriers." Biomolecules 10, no. 7 (July 7, 2020): 1008. http://dx.doi.org/10.3390/biom10071008.

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Metabolite carriers of the mitochondrial inner membrane are crucial for cellular physiology since mitochondria contribute essential metabolic reactions and synthesize the majority of the cellular ATP. Like almost all mitochondrial proteins, carriers have to be imported into mitochondria from the cytosol. Carrier precursors utilize a specialized translocation pathway dedicated to the biogenesis of carriers and related proteins, the carrier translocase of the inner membrane (TIM22) pathway. After recognition and import through the mitochondrial outer membrane via the translocase of the outer membrane (TOM) complex, carrier precursors are ushered through the intermembrane space by hexameric TIM chaperones and ultimately integrated into the inner membrane by the TIM22 carrier translocase. Recent advances have shed light on the mechanisms of TOM translocase and TIM chaperone function, uncovered an unexpected versatility of the machineries, and revealed novel components and functional crosstalk of the human TIM22 translocase.

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Dissertations / Theses on the topic "Tim22"

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Mühlenbein, Nicole. "Charakterisierung der mitochondrialen TIM22-Translokase des Menschen." Diss., lmu, 2004. http://nbn-resolving.de/urn:nbn:de:bvb:19-29299.

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Adam, Alexander. "Tim8 und Tim9, neue Komponenten der TIM22 Präproteintranslokase in Mitochondrien." Diss., lmu, 2004. http://nbn-resolving.de/urn:nbn:de:bvb:19-31385.

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Endres, Maxi. "Funktionelle Charakterisierung des Imports des ADP-ATP-Carriers über die TIM22-Translokase der mitochondrialen Innenmembran." [S.l.] : [s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=963609351.

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Endres, Maxi. "Funktionelle Charakterisierung des Imports des ADP/ATP-Carriers über die TIM22-Translokase der mitochondrialen Innenmembran." Diss., lmu, 2000. http://nbn-resolving.de/urn:nbn:de:bvb:19-2204.

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Vasiljev, Andreja. "Isolation and characterisation of the intermembrane space components of the mitochondrial TIM22 protein import machinery of Neurospora crassa." Diss., lmu, 2004. http://nbn-resolving.de/urn:nbn:de:bvb:19-28243.

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Mapa, Koyeli. "Conformational Dynamics of the Mitochondrial TIM23 Preprotein Translocase." Diss., lmu, 2009. http://nbn-resolving.de/urn:nbn:de:bvb:19-104371.

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Glaser, Stephanie. "Structural and functional characterisation of Plasmodium falciparum Tic22." Thesis, University of Cambridge, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.610235.

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Mokranjac, Dejana. "Structure and function of the mitochondrial TIM23 preprotein translocase." Diss., lmu, 2004. http://nbn-resolving.de/urn:nbn:de:bvb:19-23304.

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Valença, Andreia Barbosa. "Analysis of TIM2 deficiency in the mouse retina." Doctoral thesis, Universidade de Lisboa, Faculdade de Medicina Veterinária, 2019. http://hdl.handle.net/10400.5/18022.

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Tese de Doutoramento em Ciências Veterinárias, na especialidade de Ciências Biológicas e Biomédicas
Careful control of iron availability in the retina is central to maintenance of iron homeostasis, as its imbalance is associated with oxidative stress and progress of several retinopathies, such as diabetic retinopathy. Ferritin, known for its role in iron storage and detoxification, has also been proposed as an iron-transporter and can be regarded as a potential deliverer of a considerable large amount of iron to the retina compared to transferrin, the classical ironcarrier protein. Ferritin can bind to scavenger receptor class A member 5 (Scara5) and T-cell immunoglobulin and mucin-domain 2 (TIM2) receptors and is likely endocytosed. In this study, the presence of TIM2, which remained unknown in the retina, was investigated. Although no human ortholog for mouse TIM2 has been identified, human TIM1 and mouse TIM2 have similar functions. Our results revealed for the first time the presence of TIM2 receptors in the mouse retina, mainly expressed in Müller cells, unveiling new aspects of retinal iron metabolism regarding the putative role of TIM2 in this tissue. A knockout mouse for this membrane receptor was generated in order to better understand TIM2 functions in the retina. TIM2 deficiency affected retinal iron metabolism. Iron-loaded ferritin accumulation, probably due to increased ferritin uptake mediated by Scara5, and increased iron uptake by transferrin receptor 1 (TfR1)- transferrin binding led to retinal iron overload. Consequently, increased vascular permeability and blood-retinal barrier (BRB) breakdown were observed, inducing edema of the central retina. Paracellular and transcellular transports were impaired with tight junction integrity loss and increased caveolae number. Two mechanisms seem to be involved in this process: association of iron and ferritin overload with vascular endothelial growth factor (VEGF) overexpression and oxidative stress triggered by reactive oxygen species (ROS) overproduction generated by retinal iron overload. Altogether, these results point to TIM2 as a new key player in iron homeostasis in the mouse retina, possibly modulating cellular iron levels, and a potential target for the treatment of diabetic macular edema.
RESUMO - Análise da deficiência de TIM2 na retina de murganho - A retina necessita especificamente de ferro, devido a este ser um co-factor essencial da enzima guanilato ciclase que assegura a síntese de monofosfato de guanosina cíclico, segundo mensageiro na cascata de fototransdução. Para além disso, a retina é particularmente dependente de ferro devido à contínua necessidade de síntese de membranas, para suprir a constante renovação dos segmentos externos dos fotorrecetores, que requer como co-factor este elemento. Porém, o desequilíbrio da homeostasia do ferro está associado ao dano oxidativo e ao desenvolvimento de várias situações de retinopatia, como por exemplo a retinopatia diabética. A retina é particularmente propensa a stress oxidativo e o excesso de ferro exacerba potencialmente esta situação, devido à participação do ferro na reação de Fenton, que gera a superprodução de espécies reativas de oxigénio que, por sua vez, desencadeiam stress oxidativo. Por conseguinte, a manutenção da homeostasia do ferro é crucial neste tecido. Contudo, mecanismos de regulação do ferro na retina ainda não são completamente conhecidos. A retina obtém ferro a partir da circulação sanguínea. No entanto, a barreira hemato-retiana isola a retina da circulação sanguínea, protegendo-a de potenciais estímulos nocivos. Assim, são necessários mecanismos específicos e rigorosamente regulados de absorção de ferro para atravessar esta barreira e importar a quantidade de ferro estritamente essencial para o normal funcionamento da retina. Classicamente, a transferrina foi estabelecida como a proteína transportadora de ferro na retina, sendo aceite que a transferrina sérica se liga ao seu recetor de membrana, recetor da transferrina 1, na superfície das células endoteliais e do epitélio pigmentar da retina. Após a endocitose deste complexo, o ferro é libertado no parênquima retiniano. Mais recentemente, a ferritina, considerada classicamente como uma proteína de armazenamento de ferro e destoxificação, foi também proposta como uma proteína transportadora deste elemento. A vantagem da ferritina sérica em relação à transferrina no transporte de ferro prende-se na capacidade da ferritina de incorporar ~ 4,500 átomos de ferro, ao passo que a transferrina apenas transporta 2 átomos de ferro, constituindo, assim, a ferritina uma fonte muito eficiente de ferro para os tecidos. A molécula da ferritina é composta por 24 subunidades de dois tipos: cadeia leve (L) e cadeia pesada (H) que se unem aos recetores Scara5 (scavenger receptor class A member 5) e TIM2 (T-cell immunoglobulin and mucin-domain 2), respetivamente. O nosso grupo identificou pela primeira vez a presença de recetores Scara5 na retina humana e do murganho. No entanto, até à data, a presença de recetores TIM2 na retina não foi reportada na bibliografia. O TIM2, uma proteína transmembranar do tipo 1, é um membro da família de genes portadores dos domínios mucina e imunoglobulina de células T e, para além de ser um recetor para a ferritina-H, está envolvido na regulação da resposta imunitária...
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Popov-Celeketic, Dusan. "Dynamic Regulation of Function of the Mitochondrial TIM23 Preprotein Translocase." Diss., lmu, 2007. http://nbn-resolving.de/urn:nbn:de:bvb:19-81728.

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Books on the topic "Tim22"

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Chaykin, Howard Victor. Time2. Image Comics, 2022.

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Book chapters on the topic "Tim22"

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Bobet, J.-L., B. Chevalier, and B. Darriet. "Investigation of Hydrogen Sorption Properties of TiMn2 Based Alloys." In Hydrogen Materials Science and Chemistry of Metal Hydrides, 115–23. Dordrecht: Springer Netherlands, 2002. http://dx.doi.org/10.1007/978-94-010-0558-6_13.

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Shiono, Takeshi, Hideaki Hagihara, Satoru Yoshida, and Tomiki Ikeda. "Kinetic Features of Living Polymerization of Propene with the [t-BuNSiMe2Flu]TiMe2/B(C6F5)3 Catalyst." In Metalorganic Catalysts for Synthesis and Polymerization, 264–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-60178-1_24.

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Hinterseher, I., D. Krex, H. Bergert, E. Kuhlisch, and H. D. Saeger. "Genomische Analyse der Tissue Inhibitors of Metalloproteinases 1 und 2 (TIMP1 und TIMP2) als potentielle ätiologische Faktoren spontaner Aortenaneurysmen." In Deutsche Gesellschaft für Chirurgie, 97–98. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-642-18547-2_30.

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Oktay, Yavuz, Robert N. Rainey, and Carla M. Koehler. "The Function of TIM22 in the Insertion of Inner Membrane Proteins in Mitochondria." In Molecular Machines Involved in Protein Transport across Cellular Membranes, 367–85. Elsevier, 2007. http://dx.doi.org/10.1016/s1874-6047(07)25014-0.

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Ayad, Shirley, Ray Boot-Handford, Martin J. Humphries, Karl E. Kadler, and Adrian Shuttleworth. "TIMP2 tissue inhibitor of metalloproteinase-2." In The Extracellular Matrix FactsBook, 280–81. Elsevier, 1998. http://dx.doi.org/10.1016/b978-012068911-8.50179-2.

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Intaragamjon, Nawapom, Takeshi Shiono, and Piyasan Praserthdama. "A comparative study ethylene/1-hexene copolymerization with [t-BuNSiMe2Flu]TiMe2 catalyst via various activators." In New Developments and Application in Chemical Reaction Engineering, 841–44. Elsevier, 2006. http://dx.doi.org/10.1016/s0167-2991(06)81728-3.

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Dudek, Jan, Bernard Guiard, and Peter Rehling. "The Role of the TIM23 Complex and Its Associated Motor Complex in Mitochondrial Protein Import." In Molecular Machines Involved in Protein Transport across Cellular Membranes, 387–411. Elsevier, 2007. http://dx.doi.org/10.1016/s1874-6047(07)25015-2.

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Intaragamjon, Nawaporn, Takeshi Shiono, Bunjerd Jongsomjit, and Piyasan Praserthdam. "Effect of α-Olefins on Copolymerization of Ethylene and α-Olefin with [t-BuNSiMe2Flu]TiMe2 Catalyst." In Studies in Surface Science and Catalysis, 271–74. Elsevier, 2006. http://dx.doi.org/10.1016/s0167-2991(06)80469-6.

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Shiono, Takeshi, Zhengguo Cai, and Yuushou Nakayama. "Effects of Solvents in Living Polymerization of Propene with [t-BuNSiMe2(3,6-t-Bu2Flu)]TiMe2-MMAO Catalyst." In Studies in Surface Science and Catalysis, 47–52. Elsevier, 2006. http://dx.doi.org/10.1016/s0167-2991(06)80433-7.

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Zhou, Jing. "Bridges Among Visualization, Aesthetics, and Technology." In Visual Approaches to Cognitive Education With Technology Integration, 101–20. IGI Global, 2018. http://dx.doi.org/10.4018/978-1-5225-5332-8.ch007.

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This chapter presents the motivation, background, implementation, and comparison of two interactive projects created by the same artist—Living Mandala: The Cosmic of Being1 and Through the Aleph: A Glimpse of the World in Real Time2. Living Mandala is an interactive graphics installation that combines real-time data, multi-cultural mandalas, scientific imagery, and cosmological and mythological symbols; this living graphical system is an exploration into uncharted territories of the human soul sculpted by our present time. Through the Aleph is a net art project offering an unprecedented visual and interactive experience where many places on Earth and in space can be seen simultaneously in an instant; with an unexpected approach to surveillance cameras and global networks, this meditative web project draws the connections between individuals and the global environment, Earth and outer space, eternity and time, and art and science. Built in an open source environment using live data and complex graphics, both projects visualize microcosm (the diversity of human civilizations and perceptions of life) and macrocosm (the unity of humanity and the ever-changing universe). Although one work is responsive to the physical environment while another to the virtual space, each project merges multiple layers of dynamic imagery and symbols related to cultural heritage, cosmology, science, technology, and nature in a globalized society through time and space in the present moment. 3 In spite of the differences in visual expressions and media platforms between the two projects, the quintessential force bridging visualization, aesthetics, and technology emerges from the artist's journey of being a humble student of Life.

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Conference papers on the topic "Tim22"

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"Preface: TIM20-21 Physics Conference." In PROCEEDINGS OF THE TIM20-21 PHYSICS CONFERENCE. AIP Publishing, 2023. http://dx.doi.org/10.1063/12.0017678.

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Macris, Chris G., Robert G. Ebel, Christopher B. Leyerle, and John C. McCullough. "Phase Change Metallic Alloy TIM2 Performance and Reliability." In ASME 2007 InterPACK Conference collocated with the ASME/JSME 2007 Thermal Engineering Heat Transfer Summer Conference. ASMEDC, 2007. http://dx.doi.org/10.1115/ipack2007-33702.

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With processor power levels exceeding 200 Watts and nearly 25% of the overall processor junction-to-ambient thermal resistance budget consumed at the second-level thermal interface (TIM2), the use of an all-metal interfacial thermal path is highly desirable [1]. Phase Change Metallic Alloys (PCMAs) offer superior thermal performance due to their high thermal conductivities and low contact resistance resulting from their excellent surface wetting. Also, reworkability and ease of handling make PCMAs attractive in a high volume setting. The current work utilizes packaged Thermal Test Vehicles (TTVs) for thermal performance characterization and an In-situ Test Vehicle (ITV) platform for reliability testing. Comparative thermal performance between a PCMA and organic thermal interface products will be presented. Additionally, reliability data from PCMA samples subject to various environmental stress conditions will be discussed.

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Kishii, Noriyuki, Katsuya Shirai, Shin-ichiro Tamura, Jun'etsu Seto, Katsumi Tokumaru, Satohiro Takagi, Tatsuo Arai, and Hirochika Sakuragi. "Electron Transfer Reaction from Zinc(II)tetraphenylporphine to Dichloromethane." In Spectral Hole-Burning and Related Spectroscopies: Science and Applications. Washington, D.C.: Optica Publishing Group, 1994. http://dx.doi.org/10.1364/shbs.1994.wd20.

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Persistent spectral hole burning (PHB) offers the potential of ultra high density optical data storage1). Recently much effort has been directed towards photon-gated PHB material systems, since the systems have good properties for optical memories such as non-destructive reading and fast reaction time2). Thus it is important to study the reaction mechanism of photon-gated material systems not only to develop suitable material systems for optical memories but also to find new photochemical reactions at cryogenic temperatures.

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Kearney, Andrew, Li Li, and Sean Sanford. "Interaction between TIM1 and TIM2 for mechanical robustness of integrated heat spreader." In 2009 25th Annual IEEE Semiconductor Thermal Measurement and Management Symposium. IEEE, 2009. http://dx.doi.org/10.1109/stherm.2009.4810778.

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Pandey, J., J. L. Larson-Casey, L. Gu, C. He, and A. B. Carter. "Abrogation of the TOM20-TIM23 Pathway Ameliorates NOX4-Induced Mitochondria ROS in Pulmonary Fibrosis." In American Thoracic Society 2022 International Conference, May 13-18, 2022 - San Francisco, CA. American Thoracic Society, 2022. http://dx.doi.org/10.1164/ajrccm-conference.2022.205.1_meetingabstracts.a5238.

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Pugacheva, Elena N., Sarah McLaughlin, Ryan Ice, Anuradha Rajulapati, Polina Kozyulina, Ryan Livengood, Varvara Kozyreva, Yuriy Loskutov, Alexey Ivanov, and Scott Weed. "Abstract 2013: NEDD9 depletion leads to MMP14 inactivation by TIMP2 and prevents invasion and metastasis." 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.am2014-2013.

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7

Lu, Jun, Michelle C. Lin, and Bernie Short. "Measuring and Optimizing Thermal Interface Material Performance for VR Heatsink Designs." In ASME 2015 International Technical Conference and Exhibition on Packaging and Integration of Electronic and Photonic Microsystems collocated with the ASME 2015 13th International Conference on Nanochannels, Microchannels, and Minichannels. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/ipack2015-48146.

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With increasingly high powers on processors, memories, and chipsets, the voltage regulators (VR) become heavily loaded and a heatsink is often required to prevent overheating the surrounding components on the board. For VR heatsink designs, thermal interface silicone gap filler pads are often used and there is an increasing need to improve VR thermal solutions by reducing thermal resistance of the TIM. A series of TIM2 thickness and performance measurements based on thermal testing was performed in order to understand gap filler characteristics, optimize TIM performance, and utilize best retention design. By utilizing a VR thermal and mechanical test board in wind tunnel testing using the same VR heatsink, thermal performance of TIM2 using gap filler pads over a range of airflow velocities can be measured and compared. The study shows how the optimum TIM performance can be achieved by using the gap filler pads with appropriate thickness for the given designed heatsink standoff heights. The benefit of choosing the right thickness pads over others can be significant and is a valuable learning that can be applied to future VR heatsink designs. Furthermore, the silicone gap filler characteristics and its relationship to board bending and result TIM thickness and thermal performance are investigated and further improved. The learnings help understand the limitations and where the area of improvement can be for future VR heatsink designs.

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Subramaniam, Ranjithkumar, Selvakumar Subramanian, Balachandar Krishnamurthy, Jegadeeshwaran Rakkiyannan, Sakthivel Gnanasekaran, and Yogesh Bhalerao. "Brake fault diagnosis using histogram features and artificial immune recognition system (AIRS)." In PROCEEDINGS OF THE TIM20-21 PHYSICS CONFERENCE. AIP Publishing, 2023. http://dx.doi.org/10.1063/5.0149302.

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Raj, K. Mohith, M. Bhuvanesh, J. Dinesh, and B. Anbarasu. "Optical flow and infrared sensor based indoor navigation system for micro aerial vehicle." In PROCEEDINGS OF THE TIM20-21 PHYSICS CONFERENCE. AIP Publishing, 2023. http://dx.doi.org/10.1063/5.0149178.

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Mohamed, Ahmed Ushan, and Alexander Chee Hon Cheong. "Automated color sorting for material handling system." In PROCEEDINGS OF THE TIM20-21 PHYSICS CONFERENCE. AIP Publishing, 2023. http://dx.doi.org/10.1063/5.0148572.

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Reports on the topic "Tim22"

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Rizzoni, Giorgio. GATE: Energy Efficient Vehicles for Sustainable Mobility-Project TI022- FinalReport. Office of Scientific and Technical Information (OSTI), February 2018. http://dx.doi.org/10.2172/1422746.

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