Relevant bibliographies by topics / Kinesin superfamily protein

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Academic literature on the topic 'Kinesin superfamily protein'

Author: Grafiati
Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Kinesin superfamily protein"

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Park, Hye-Young, Sang-Jin Kim, Sung-Su Ye, Won-Hee Jang, Sang-Kyeong Lee, Yeong-Hong Park, Yong-Wook Jung, Il-Soo Moon, Moo-Seong Kim, and Dae-Hyun Seog. "Pcp-2 Interacts Directly with Kinesin Superfamily KIF21A Protein." Journal of Life Science 18, no. 8 (August 30, 2008): 1059–65. http://dx.doi.org/10.5352/jls.2008.18.8.1059.

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Jang, Won Hee, and Dae-Hyun Seog. "Kinesin Superfamily-associated Protein 3 (KAP3) Mediates the Interaction between Kinesin-II Motor Subunits and HS-1-associated Protein X-1 (HAX-1) through Direct Binding." Journal of Life Science 23, no. 8 (August 30, 2013): 978–83. http://dx.doi.org/10.5352/jls.2013.23.8.978.

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Wong-Riley, Margaret T. T., and Joseph C. Besharse. "The kinesin superfamily protein KIF17: one protein with many functions." BioMolecular Concepts 3, no. 3 (June 1, 2012): 267–82. http://dx.doi.org/10.1515/bmc-2011-0064.

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AbstractKinesins are ATP-dependent molecular motors that carry cargos along microtubules, generally in an anterograde direction. They are classified into 14 distinct families with varying structural and functional characteristics. KIF17 is a member of the kinesin-2 family that is plus end-directed. It is a homodimer with a pair of head motor domains that bind microtubules, a coiled-coil stalk, and a tail domain that binds cargos. In neurons, KIF17 transports N-methyl-D-aspartate receptor NR2B subunit, kainate receptor GluR5, and potassium Kv4.2 channels from cell bodies exclusively to dendrites. These cargos are necessary for synaptic transmission, learning, memory and other functions. KIF17’s interaction with nuclear RNS export factor 2 (NXF2) enables the transport of mRNA bidirectionally in dendrites. KIF17 or its homolog osmotic avoidance abnormal protein 3 (OSM-3) also mediates intraflagellar transport of cargos to the distal tips of flagella or cilia, thereby aiding in ciliogenesis. In many invertebrate and vertebrate sensory cells, KIF17 delivers cargos that contribute to chemosensory perception and signal transduction. In vertebrate photoreceptors, KIF17 is necessary for outer segment development and disc morphogenesis. In the testis, KIF17 (KIF17b) mediates microtubule-independent delivery of an activator of cAMP-responsive element modulator (ACT) from the nucleus to the cytoplasm and microtubule-dependent transport of Spatial-ε, both are presumably involved in spermatogenesis. KIF17 is also implicated in epithelial polarity and morphogenesis, placental transport and development, and the development of specific brain regions. The transcriptional regulation of Kif17 has recently been found to be mediated by nuclear respiratory factor 1 (NRF-1), which also regulates NR2B as well as energy metabolism in neurons. Dysfunctions of KIF17 are linked to a number of pathologies.
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Hares, K., K. Kemp, C. Rice, E. Gray, N. Scolding, and A. Wilkins. "Reduced axonal motor protein expression in non-lesional grey matter in multiple sclerosis." Multiple Sclerosis Journal 20, no. 7 (October 21, 2013): 812–21. http://dx.doi.org/10.1177/1352458513508836.

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Background: Multiple sclerosis (MS) is a neurological disease characterised by central nervous system inflammation, demyelination, axonal degeneration and neuronal injury. Preventing neuronal and axon damage is of paramount importance in attempts to prevent disease progression. Intact axonal transport mechanisms are crucial to axonal integrity and evidence suggests these mechanisms are disrupted in MS. Anterograde axonal transport is mediated to a large extent through the kinesin superfamily proteins. Recently, certain kinesin superfamily proteins (KIF5A, KIF1B and KIF21B) were implicated in MS pathology. Objectives: To investigate the expression of KIF5A, KIF21B and KIF1B in MS and control post-mortem grey matter. Methods: Using both quantitative real-time polymerase chain reaction (PCR) and Immunodot-blots assays, we analysed the expression of kinesin superfamily proteins in 27 MS cases and 13 control cases not linked to neurological disease. Results: We have shown significant reductions in KIF5A, KIF21B and KIF1B messenger ribonucleic acid (mRNA) expression and also KIF5A protein expression in MS grey matter, as compared to control grey matter. Conclusion: We have shown significant reductions in mRNA and protein levels of axonal motor proteins in the grey matter of MS cases, which may have important implications for the pathogenesis of neuronal/axonal injury in the disease.
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Barrett, Jennifer G., Brendan D. Manning, and Michael Snyder. "The Kar3p Kinesin-related Protein Forms a Novel Heterodimeric Structure with Its Associated Protein Cik1p." Molecular Biology of the Cell 11, no. 7 (July 2000): 2373–85. http://dx.doi.org/10.1091/mbc.11.7.2373.

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Proteins that physically associate with members of the kinesin superfamily are critical for the functional diversity observed for these microtubule motor proteins. However, quaternary structures of complexes between kinesins and kinesin-associated proteins are poorly defined. We have analyzed the nature of the interaction between the Kar3 motor protein, a minus-end–directed kinesin from yeast, and its associated protein Cik1. Extraction experiments demonstrate that Kar3p and Cik1p are tightly associated. Mapping of the interaction domains of the two proteins by two-hybrid analyses indicates that Kar3p and Cik1p associate in a highly specific manner along the lengths of their respective coiled-coil domains. Sucrose gradient velocity centrifugation and gel filtration experiments were used to determine the size of the Kar3-Cik1 complex from both mating pheromone-treated cells and vegetatively growing cells. These experiments predict a size for this complex that is consistent with that of a heterodimer containing one Kar3p subunit and one Cik1p subunit. Finally, immunoprecipitation of epitope-tagged and untagged proteins confirms that only one subunit of Kar3p and Cik1p are present in the Kar3-Cik1 complex. These findings demonstrate that the Kar3-Cik1 complex has a novel heterodimeric structure not observed previously for kinesin complexes.
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Alphey, Luke, Louise Parker, Gillian Hawcroft, Yiquan Guo, Kim Kaiser, and Gareth Morgan. "KLP38B: A Mitotic Kinesin-related Protein That Binds PP1." Journal of Cell Biology 138, no. 2 (July 28, 1997): 395–409. http://dx.doi.org/10.1083/jcb.138.2.395.

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We have identified a new member of the kinesin superfamily in Drosophila, KLP38B (kinesin-like protein at 38B). KLP38B was isolated through its two-hybrid interaction with the catalytic subunit of type 1 serine/threonine phosphoprotein phosphatase (PP1). We demonstrate that recombinant KLP38B and PP1 associate in vitro. This is the first demonstration of direct binding of a kinesin-related protein to a regulatory enzyme. Though most closely related to the Unc-104 subfamily of kinesin-related proteins, KLP38B is expressed only in proliferating cells. KLP38B mutants show cell proliferation defects in many tissues. KLP38B is required for normal chromatin condensation as embryos from KLP38B mutant mothers have undercondensed chromatin at metaphase and anaphase. This is the first time that a kinesin-related protein has been shown to have such a role. Incomplete lethality of a strong KLP38B allele suggests partial redundancy with one or more additional kinesin-related proteins.
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Mahase, Vidhyanand, Adebiyi Sobitan, Christina Johnson, Farion Cooper, Yixin Xie, Lin Li, and Shaolei Teng. "Computational analysis of hereditary spastic paraplegia mutations in the kinesin motor domains of KIF1A and KIF5A." Journal of Theoretical and Computational Chemistry 19, no. 06 (August 5, 2020): 2041003. http://dx.doi.org/10.1142/s0219633620410035.

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Hereditary spastic paraplegias (HSPs) are a genetically heterogeneous collection of neurodegenerative disorders categorized by progressive lower-limb spasticity and frailty. The complex HSP forms are characterized by various neurological features including progressive spastic weakness, urinary sphincter dysfunction, extra pyramidal signs and intellectual disability (ID). The kinesin superfamily proteins (KIFs) are microtubule-dependent molecular motors involved in intracellular transport. Kinesins directionally transport membrane vesicles, protein complexes, and mRNAs along neurites, thus playing important roles in neuronal development and function. Recent genetic studies have identified kinesin mutations in patients with HSPs. In this study, we used the computational approaches to investigate the 40 missense mutations associated with HSP and ID in KIF1A and KIF5A. We performed homology modeling to construct the structures of kinesin–microtubule binding domain and kinesin–tubulin complex. We applied structure-based energy calculation methods to determine the effects of missense mutations on protein stability and protein–protein interaction. The results revealed that the most of disease-causing mutations could change the folding free energy of kinesin motor domain and the binding free energy of kinesin–tubulin complex. We found that E253K associated with ID in KIF1A decrease the protein stability of kinesin motor domains. We showed that the HSP mutations located in kinesin–tubulin complex interface, such as K253N and R280C in KIF5A, can destabilize the kinesin–tubulin complex. The computational analysis provides useful information for understanding the roles of kinesin mutations in the development of ID and HSPs.
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Okada, Y. "A Processive Single-Headed Motor: Kinesin Superfamily Protein KIF1A." Science 283, no. 5405 (February 19, 1999): 1152–57. http://dx.doi.org/10.1126/science.283.5405.1152.

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Cole, D. G., W. Z. Cande, R. J. Baskin, D. A. Skoufias, C. J. Hogan, and J. M. Scholey. "Isolation of a sea urchin egg kinesin-related protein using peptide antibodies." Journal of Cell Science 101, no. 2 (February 1, 1992): 291–301. http://dx.doi.org/10.1242/jcs.101.2.291.

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To understand the roles of kinesin and its relatives in cell division, it is necessary to identify and characterize multiple members of the kinesin superfamily from mitotic cells. To this end we have raised antisera to peptides corresponding to highly conserved regions of the motor domains of several known members of the kinesin superfamily. These peptide antibodies react specifically with the motor domains of kinesin and ncd protein, as expected, and they also react with several polypeptides (including kinesin heavy chain) that cosediment with microtubules (MTs) precipitated from AMPPNP-treated sea urchin egg cytosol. Subsequent fractionation of ATP eluates of these MTs yields a protein of relative molecular mass 330 × 10(3) that behaves as a complex of three polypeptides that are distinct from conventional kinesin subunits or fragments thereof. This complex contains 85 kDa and 95 kDa polypeptides, which react with our peptide antibodies, and a 115 kDa polypeptide, which does not. This triplet of polypeptides, which we refer to as KRP(85/95), binds to purified sea urchin egg tubulin in an AMPPNP-enhanced, ATP-sensitive manner and induces the formation of microtubule bundles. We therefore propose that the triplet corresponds to a novel sea urchin egg kinesin-related protein.
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Pereira, Andrea J., Brian Dalby, Russell J. Stewart, Stephen J. Doxsey, and Lawrence S. B. Goldstein. "Mitochondrial Association of a Plus End–Directed Microtubule Motor Expressed during Mitosis in Drosophila." Journal of Cell Biology 136, no. 5 (March 10, 1997): 1081–90. http://dx.doi.org/10.1083/jcb.136.5.1081.

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The kinesin superfamily is a large group of proteins (kinesin-like proteins [KLPs]) that share sequence similarity with the microtubule (MT) motor kinesin. Several members of this superfamily have been implicated in various stages of mitosis and meiosis. Here we report our studies on KLP67A of Drosophila. DNA sequence analysis of KLP67A predicts an MT motor protein with an amino-terminal motor domain. To prove this directly, KLP67A expressed in Escherichia coli was shown in an in vitro motility assay to move MTs in the plus direction. We also report expression analyses at both the mRNA and protein level, which implicate KLP67A in the localization of mitochondria in undifferentiated cell types. In situ hybridization studies of the KLP67A mRNA during embryogenesis and larval central nervous system development indicate a proliferation-specific expression pattern. Furthermore, when affinity-purified anti-KLP67A antisera are used to stain blastoderm embryos, mitochondria in the region of the spindle asters are labeled. These data suggest that KLP67A is a mitotic motor of Drosophila that may have the unique role of positioning mitochondria near the spindle.
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Dissertations / Theses on the topic "Kinesin superfamily protein"

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REDONDO, JULIANA. "Role of kinesin superfamily proteins in neurodegeneration." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2012. http://hdl.handle.net/10281/40033.

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Intracellular transport is fundamental for neuronal function and survival. The majority of proteins are synthesized in the neuron cell body and transported along axons and dendrites through molecular motors as the Kinesin superfamily proteins (KIFs). Two specific KIFs that have been associated strongly with neurodegenerative processes in humans and in rodents are KIF5A and KIF21B. In fact, KIF5A down regulation has been associated with axonal transport defects in models of multiple sclerosis (MS) and a genome wide association screen for MS correlated single nucleotide polymorphisms located in the KIF21B intron with the disease, establishing this kinesin as a susceptibility locus for MS. Since nitric oxide (NO) has a key role in mediating inflammatory axonopathy in MS promoting protein mis-folding, disruption of mitochondrial respiratory chain and organelle fragmentation, the first aim of the present study was to determine the effect of NO exposure on the expression of KIF5A and KIF21B in rodent cortical neurons and to evaluate whether KIFs expression correlates with axon pathology. Results demonstrated that NO cause a time dependent decrease of gene and protein expression for both KIF proteins. Furthermore, dot blot analysis showed that NO cause a time dependent decrease in axon phosphorylation and that KIFs reduction precede the loss of neurofilament. Human bone marrow mesenchymal stem cells (MSCs) represent a promising candidate for neuronal repair due to anti-inflammatory, antioxidant and neurotrophic properties. The second part of this study was therefore to investigate the capacity of MSC to protect neurons and axonal transport mechanisms in rodent cortical neurons exposed to NO. Results showed that MSC were able to preserve axonal length and increase survival in cortical neurons exposed to NO, furthermore MSCs had the ability to preserve both KIF5A and KIF21B protein expression from nitric oxide damage. Finally in this study, it was evaluated if there were any changes in KIFs gene and protein expression in cerebellum of MS patients in relation to appropriate control patients. Results demonstrated significant changes in KIF5A and KIF21B expression and the presence of KIF positive spheroids aggregates in sections derived from MS patients. In conclusion, the results of this study allow a better understanding of the mechanisms involved in the abnormal accumulation of proteins in axons during oxidative insult, that represent a hallmark of several neurodegenerative disorders. Moreover, the ability of MSCs to protect KIF expression from NO damage provides further evidence of their significant therapeutic potential in multiple sclerosis.
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MAGGIORE, BEATRICE. "Structural and aggregation properties of bovine α1-acid glycoprotein, a member of the lipocalin superfamily." Doctoral thesis, 2017. http://hdl.handle.net/11566/245551.

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Lo studio delle proprietà strutturali e funzionali della α1-glicoproteina acida (AGP) costituisce l’oggetto di questa tesi. L’AGP rappresenta, dopo l’albumina, la più abbondante proteina nel plasma. Essa appartiene alla famiglia delle lipocaline, un ampio gruppo di proteine caratterizzato da una struttura centrale a barile β (β-barrel) che funge da sito di legame per numerose molecole ad attività biologica. E’ stata dimostrata l’applicabilità biotecnologica dell’AGP nel campo dello sviluppo di nuovi biosensori e delle purificazioni industriali. Durante il mio dottorato, è stata condotta un’ampia analisi riguardante numerosi fattori ambientali (pH, stato ossidoriduttivo, temperatura), la quale ha mostrato che valori di pH debolmente o fortemente acidi e/o condizioni riducenti, inducono la concomitante denaturazione e aggregazione delle catene polipeptidiche in seguito all’aumento della temperatura. Da queste osservazioni si è passati alla caratterizzazione delle forme aggregate dell’AGP ottenute in specifiche condizioni di pH, temperatura e stato ossidoriduttivo. La capacità, di questi aggregati, di legare la Tioflavina T indica che tali forme aggregate sono di natura amiloide. Indagini più mirate sono state condotte sulla cinetica di formazione delle fibrille, da cui ricavare parametri cinetici utili nell’individuare un possibile modello di aggregazione. È importante notare che le analisi cinetiche non mostrano la presenza di una fase di nucleazione, il che esclude il modello di polimerizzazione dipendente da nucleazione. In questo modello, il passaggio limitante, è rappresentato dalla formazione di un nucleo che funge da innesco critico per l’intero processo di fibrillazione. Dati sperimentali hanno evidenziato la mancanza di questa fase, il ché suggerisce un meccanismo a cascata, in cui lo step critico è rappresentato dalla conversione del monomero stabile in monomero ‘attivato’, il quale è più propenso all’aggregazione e si assembla in strutture fibrillari.
α1-Acidglycoprotein (AGP) is an important member of the acute phase response involved in drug binding and modulation of the immune system. AGP belongs to the lipocalin superfamily, a wide group of proteins sharing a strikingly conserved β-barrel fold that serves as a binding site for a large number of hydrophobic and neutral molecules. Several biological functions have been associated to AGP, both in vivo and in vitro. AGP is able to bind and transport a wide number of hydrophobic molecules. Potential therapeutic uses of AGP in the treatment of immune diseases have been envisioned, including, for instance, reduction of histamine levels. In the light of these observations, a detailed knowledge of the structure and stability of AGP appears essential. Fourier-Transform infrared (FT-IR) spectroscopy has been extensively used in the investigation of AGP due to its sensitivity towards fluctuations within protein structures. A survey of several environmental conditions, including pH and disulfide redox state, has shown that strongly acidic and reducing environments induce concomitant denaturation and aggregation of the polypeptide chain following increases in temperature. My doctoral research has been undertaken to characterize AGP aggregates obtained in the presence of the disulfide-specific reducing agents. The binding of Thioflavin T dye indicate that the aggregates possess a cross-β motif, suggesting that they are amyloid in nature. A molecular interpretation on the fibrillation kinetics of AGP was proposed. The experimental data do not show a nucleation-dependent polymerization mechanism otherwise they suggest a downhill polymerization mechanism as described for transthyretin and serum albumin. In this model, an aggregation-prone species self-assembles to form the amyloid fibrils. Further support to the downhill polymerization mechanism was provided by the seeding experiments and a more accurate kinetic analysis of fibril formation.
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Book chapters on the topic "Kinesin superfamily protein"

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Hirokawa, Nobutaka, and Yasuko Noda. "Preparation of Recombinant Kinesin Superfamily Proteins Using the Baculovirus System." In Kinesin Protocols, 57–63. Totowa, NJ: Humana Press, 2001. http://dx.doi.org/10.1385/1-59259-069-1:57.

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Kapitein, Lukas C., and Erwin J. G. Peterman. "Single Molecule Experiments and the Kinesin Motor Protein Superfamily." In Single Molecule Biology, 35–60. Elsevier, 2009. http://dx.doi.org/10.1016/b978-0-12-374227-8.00002-x.

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Hirokawa, N., and R. Takemura. "Kinesin Superfamily Proteins." In Encyclopedia of Biological Chemistry, 679–87. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-378630-2.00431-x.

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Hirokawa, Nobutaka, and Reiko Takemura. "Kinesin Superfamily Proteins." In Encyclopedia of Biological Chemistry, 508–16. Elsevier, 2004. http://dx.doi.org/10.1016/b0-12-443710-9/00348-3.

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Hirokawa, Nobutaka, Yosuke Tanaka, and Reiko Takemura. "Further Reading | Kinesin Superfamily Proteins." In Encyclopedia of Biological Chemistry III, 535–46. Elsevier, 2021. http://dx.doi.org/10.1016/b978-0-12-819460-7.00301-7.

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Hackney, DavidD. "Motor proteins of the kinesin superfamily." In Energy Coupling and Molecular Motors, 87—II. Elsevier, 2003. http://dx.doi.org/10.1016/s1874-6047(04)80004-0.

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Tanaka, Y., and N. Hirokawa. "Kinesin Superfamily Proteins (KIFs) as a Fundamental Component of Life: Intracellular Transport and Beyond." In Encyclopedia of Cell Biology, 608–19. Elsevier, 2016. http://dx.doi.org/10.1016/b978-0-12-394447-4.20060-6.

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