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Academic literature on the topic 'Motifs riches en leucines'
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Journal articles on the topic "Motifs riches en leucines"
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Ollendorff, V., T. Noguchi, and D. Birnbaum. "Des protéines à motifs riches en leucine définissent une cinquième famille de molécules d'adhérence." médecine/sciences 9, no. 10 (1993): 1102. http://dx.doi.org/10.4267/10608/2814.
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Nufer, Oliver, Svend Guldbrandsen, Martin Degen, Felix Kappeler, Jean-Pierre Paccaud, Katsuko Tani, and Hans-Peter Hauri. "Role of cytoplasmic C-terminal amino acids of membrane proteins in ER export." Journal of Cell Science 115, no. 3 (February 1, 2002): 619–28. http://dx.doi.org/10.1242/jcs.115.3.619.
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Export of membrane proteins from the ER is believed to be selective and require transport signals, but the identity of such signals has remained elusive. The recycling type I membrane protein ERGIC-53 carries a C-terminal diphenylalanine motif that is required for efficient ER export. Here we show that this motif can be functionally substituted by a single phenylalanine or tyrosine at position -2, two leucines or isoleucines at position -1 and -2 or a single valine at position -1. These motifs are common among mammalian type I membrane proteins. A single C-terminal valine, but none of the other motifs,accelerates transport of inefficiently exported reporter constructs and hence operates as an export signal. The valine signal is position, but not context,dependent. All transport motifs mediate COPII binding in vitro with distinct preferences for the COPII subunits Sec23p, Sec24Bp, Sec24Cp and p125. These results suggest that cytoplasmic C-terminal amino-acid motifs, either alone or in conjunction with other transport determinants, accelerate ER export of numerous type I and probably polytopic membrane proteins by mediating interaction with COPII coat components.
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Zhang, Yue, and Joseph T. Barbieri. "A Leucine-Rich Motif Targets Pseudomonas aeruginosa ExoS within Mammalian Cells." Infection and Immunity 73, no. 12 (December 2005): 7938–45. http://dx.doi.org/10.1128/iai.73.12.7938-7945.2005.
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ABSTRACT Type III cytotoxins contribute to the ability of bacterial pathogens to subvert the host innate immune system. ExoS (453 amino acids) is a bifunctional type III cytotoxin produced by Pseudomonas aeruginosa. Residues 96 to 232 comprise a Rho GTPase activating protein domain, while residues 233 to 453 comprise a 14-3-3-dependent ADP-ribosyltransferase domain. An N-terminal domain (termed the membrane localization domain [MLD]) targets ExoS to the Golgi-endoplasmic reticulum (Golgi-ER) of mammalian cells. This study identifies an amino acid motif that is responsible for the membrane binding properties of the MLD. Deletion mapping showed that the MLD included a symmetrical leucine-rich motif within residues 51 to 77 of ExoS. The terminal dileucines and internal leucines and an isoleucine within the MLD, but not charged or other hydrophobic residues, targeted a reporter protein to the Golgi-ER region of HeLa cells. Mutations of the leucines within the MLD did not affect type III secretion or translocation into HeLa cells but limited the ability of ExoS to ADP-ribosylate Ras GTPases. Mutations of charged residues within the MLD did not affect type III secretion, delivery into HeLa cells, or the ability of ExoS to ADP-ribosylate Ras GTPases. The organization of the leucines within the MLD of ExoS is different from that of previously described leucine-rich motifs but is present in several other bacterial proteins. This implies a role for intracellular targeting in the efficient targeting of mammalian cells by type III cytotoxins.
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Gu, Howard H., Xiaohong Wu, Bruno Giros, Marc G. Caron, Michael J. Caplan, and Gary Rudnick. "The NH2-terminus of Norepinephrine Transporter Contains a Basolateral Localization Signal for Epithelial Cells." Molecular Biology of the Cell 12, no. 12 (December 2001): 3797–807. http://dx.doi.org/10.1091/mbc.12.12.3797.
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When expressed in epithelial cells, dopamine transporter (DAT) was detected predominantly in the apical plasma membrane, whereas norepinephrine transporter (NET) was found in the basolateral membrane, despite 67% overall amino acid sequence identity. To identify possible localization signals responsible for this difference, DAT–NET chimeras were expressed in MDCK cells and localized by immunocytochemistry and transport assays. The results suggested that localization of these transporters in MDCK cells depends on their highly divergent NH2-terminal regions. Deletion of the first 58 amino acids of DAT (preceding TM1) did not change its apical localization. However, the replacement of that region with corresponding sequence from NET resulted in localization of the chimeric protein to the basolateral membrane, suggesting that the NH2-terminus of NET, which contains two dileucine motifs, contains a basolateral localization signal. Mutation of these leucines to alanines in the context of a basolaterally localized NET/DAT chimera restored transporter localization to the apical membrane, indicating that the dileucine motifs are critical to the basolateral localization signal embodied within the NET NH2-terminal region. However, the same mutation in the context of wild-type NET did not disrupt basolateral localization, indicating the presence of additional signals in NET directing its basolateral localization within the plasma membrane.
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Singh, Nisha, Megha Ujinwal, Sapna Langyan, R. Z. Sayyed, Hesham Ali El Enshasy, and Ahmed A. Kenawy. "Genome-wide exploration of sugar transporter (sweet) family proteins in Fabaceae for Sustainable protein and carbon source." PLOS ONE 17, no. 5 (May 13, 2022): e0268154. http://dx.doi.org/10.1371/journal.pone.0268154.
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Sugar transporter proteins (STPs) are membrane proteins required for sugar transport throughout cellular membranes. They plays an imperative role in sugar transmission across the plant and determinants of crop yield. However, the analysis of these important STPs Sugars Will Eventually be Exported Transporters (SWEET) family in legumes is still not well-documented and remains unclear. Therefore, the in-silico analysis of STPs has been performed to unravel their cellular, molecular, and structural composition in legume species. This study conducted a systematic search for STPs in Cajanus cajan using the Blastp algorithm to understand its molecular basis. Here, we performed a comprehensive analysis of 155 identified SWEET proteins across 12 legumes species, namely (Cajanus cajan, Glycine max, Vigna radiate, Vigna angularis, Medicago truncatula, Lupinus angustifolius, Glycine soja, Spatholobus suberectus, Cicer arietinum, Arachis ipaensis, Arachis hypogaea, Arachis duranensis). The amino acid composition and motif analysis revealed that SWEET proteins are rich in essential amino acids such as leucine, valine, isoleucine, phenylalanine, and serine while less profuse in glutamine, tryptophan, cysteine, and histidine. A total of four main conserved motifs of SWEET proteins are also highly abundant in these amino acids. The present study deciphered the details on primary physicochemical properties, secondary, tertiary structure, and phylogenetic analysis of SWEETs protein. Majorities of SWEET proteins (72.26%) are in stable form with an average instability index of 36.5%, and it comprises a higher fraction of positively charged amino acid Arg + Lys residues. Secondary structure analysis shown that these proteins are richer in alpha-helix (40%) than extended strand (30%) and random coil (25%), respectively. Furthermore, to infer their mechanism at a structural and functional level which play an essential roles in growth, development, and stress responses. This study will be useful to examine photosynthetic productivity, embryo sugar content, seed quality, and yield enhancement in Fabaceae for a sustainable source of essential amino acids and carbon source.
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Alfiannurdin, Nurlaila, Pipin Tresna, and Cucu Ruhidawati. "WARISAN BUDAYA CIREBON: MENGUNGKAP SEJARAH DAN MOTIF BATIK TRUSMI." NUSRA: Jurnal Penelitian dan Ilmu Pendidikan 5, no. 1 (February 28, 2024): 415–23. http://dx.doi.org/10.55681/nusra.v5i1.2267.
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This article uses a literature study approach to explore in depth the history and motifs attached to Trusmi batik, one of the unique cultural heritages of Cirebon. Using a literature study method, this research details the evolution of Trusmi batik making techniques as well as identifying and analyzing the meaning behind its distinctive motifs. The research results illustrate how this textile art reflects the traditional values and rich culture of Cirebon. The implications of these findings not only provide in-depth insight into Trusmi batik art but also provide a strong basis for efforts to preserve and develop local culture. This article has value as a guide for researchers, artists, and cultural observers who are interested in preserving cultural riches through traditional art, especially in the context of Trusmi batik in Cirebon. We can better appreciate and preserve the uniqueness of Cirebon culture for future generations by studying the background and motifs of Trusmi batik. This cultural heritage shows how well Indonesia has done in cultivating regional customs that influence textile arts and highlights the diversity and resilience of Indonesian culture, both of which should be respected and preserved.
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Jusman, Yessi, Iqbal Tawaqal, and Maryza Intan Rahmawati. "Classification of Weaving Motifs Based on Their Area of Origin Using the Support Vector Machine Algorithm." E3S Web of Conferences 519 (2024): 03034. http://dx.doi.org/10.1051/e3sconf/202451903034.
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Indonesia has many cultural riches in the form of traditional fabrics, one of which is woven fabrics. Woven fabrics from each region showcase distinctive motifs, manifesting the local community’s daily life, culture, natural conditions, and beliefs. The diverse weaving motifs pose a challenge in determining the origin of the woven fabrics. It highlights the necessity of a system to detect and identify woven fabrics. Texture analysis was performed using the Gray Level Co-occurrence Matrix (GLCM). A classification method based on a Support Vector Machine (SVM) consisting of four models: Linear SVM, Quadratic SVM, Cubic SVM, and Fine Gaussian SVM was developed in this research. The images of woven fabrics came from three regions in Indonesia: Sumatra, Kalimantan, and Nusa Tenggara. This research utilized 240 training images and 12 testing images. The testing results unveiled that the Cubic SVM model, which achieved a 100% accuracy rate in 1.0835s, was the optimum SVM model for the weaving classification.
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HAYES, H. "ADN et chromosomes." INRAE Productions Animales 13, HS (December 22, 2000): 13–20. http://dx.doi.org/10.20870/productions-animales.2000.13.hs.3806.
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Chaque chromosome contient une seule molécule d’ADN. L’ADN déroulé d’un noyau de cellule humaine mesurerait environ 1,8 m : chaque molécule d’ADN est enroulée et compactée en plusieurs étapes, grâce à l’association de différentes protéines, et loge dans le noyau de 6 µm de diamètre. Le degré de condensation de l’ADN est variable selon les régions chromosomiques et les régions les moins condensées sont les plus riches en gènes. L’ADN est composé d’une variété de séquences codantes ou non et répétées ou non dont l’organisation dans le chromosome est caractéristique de la métaphase. Certaines séquences peuvent être corrélées en partie avec les motifs de bandes spécifiques de chaque paire chromosomique produits par les techniques de marquage chromosomique.
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Hwang, Moonsun, Jae-kyun Ko, Noah Weisleder, Hiroshi Takeshima, and Jianjie Ma. "Redox-dependent oligomerization through a leucine zipper motif is essential for MG53-mediated cell membrane repair." American Journal of Physiology-Cell Physiology 301, no. 1 (July 2011): C106—C114. http://dx.doi.org/10.1152/ajpcell.00382.2010.
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We recently discovered that MG53, a muscle-specific tripartite motif (TRIM) family protein, functions as a sensor of oxidation to nucleate the assembly of cell membrane repair machinery. Our data showed that disulfide bond formation mediated by Cys242 is critical for MG53-mediated translocation of intracellular vesicles toward the injury sites. Here we test the hypothesis that leucine zipper motifs in the coiled-coil domain of MG53 constitute an additional mechanism that facilitates oligomerization of MG53 during cell membrane repair. Two leucine zipper motifs in the coiled-coil domain of MG53 (LZ1 - L176/L183/L190/V197 and LZ2 - L205/L212/L219/L226) are highly conserved across the different animal species. Chemical cross-linking studies show that LZ1 is critical for MG53 homodimerization, whereas LZ2 is not. Mutations of the conserved leucines into alanines in LZ1, not in LZ2, diminish the redox-dependent oligomerization of MG53. Live cell imaging studies demonstrate that the movement of green fluorescent protein (GFP)-tagged MG53 mutants (GFP-LA1 and GFP-LA2) is partially compromised in response to mechanical damage of the cell membrane, and the GFP-LA1/2 double mutant is completely ineffective in translocation toward the injury sites. In addition to the leucine zipper-mediated intermolecular interaction, redox-dependent cross talk between MG53 appears to be an obligatory step for cell membrane repair, since in vivo modification of cysteine residues with alkylating reagents can prevent the movement of MG53 toward the injury sites. Our data show that oxidation of the thiol group of Cys242 and leucine zipper-mediated interaction among the MG53 molecules both contribute to the nucleation process for MG53-mediated cell membrane repair.
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Anderson, Damon S., Pratima Adhikari, Katherine D. Weaver, Alvin L. Crumbliss, and Timothy A. Mietzner. "The Haemophilus influenzae hFbpABC Fe3+ Transporter: Analysis of the Membrane Permease and Development of a Gallium-Based Screen for Mutants." Journal of Bacteriology 189, no. 14 (May 11, 2007): 5130–41. http://dx.doi.org/10.1128/jb.00145-07.
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ABSTRACT The obligate human pathogen Haemophilus influenzae utilizes a siderophore-independent (free) Fe3+ transport system to obtain this essential element from the host iron-binding protein transferrin. The hFbpABC transporter is a binding protein-dependent ABC transporter that functions to shuttle (free) Fe3+ through the periplasm and across the inner membrane of H. influenzae. This investigation focuses on the structure and function of the hFbpB membrane permease component of the transporter, a protein that has eluded prior characterization. Based on multiple-sequence alignments between permease orthologs, a series of site-directed mutations targeted at residues within the two conserved permease motifs were generated. The hFbpABC transporter was expressed in a siderophore-deficient Escherichia coli background, and effects of mutations were analyzed using growth rescue and radiolabeled 55Fe3+ transport assays. Results demonstrate that mutation of the invariant glycine (G418A) within motif 2 led to attenuated transport activity, while mutation of the invariant glycine (G155A/V/E) within motif 1 had no discernible effect on activity. Individual mutations of well-conserved leucines (L154D and L417D) led to attenuated and null transport activities, respectively. As a complement to site-directed methods, a mutant screen based on resistance to the toxic iron analog gallium, an hFbpABC inhibitor, was devised. The screen led to the identification of several significant hFbpB mutations; V497I, I174F, and S475I led to null transport activities, while S146Y resulted in attenuated activity. Significant residues were mapped to a topological model of the hFbpB permease, and the implications of mutations are discussed in light of structural and functional data from related ABC transporters.
Dissertations / Theses on the topic "Motifs riches en leucines"
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Zmarlak, Natalia Marta. "Regulation of immune signalling in the malaria mosquito vector, Anopheles : the secreted mosquito leucine-rich repeat protein APL1C is a pathogen binding factor essential for immunity to Plasmodium ookinetes and sporozoites." Electronic Thesis or Diss., Sorbonne université, 2021. http://www.theses.fr/2021SORUS053.
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L’anophèle est le moustique vecteur du parasite Plasmodium, responsable du paludisme. Chez ce moustique, des protéines de type LRR (à motifs riches en leucine) ont été décrites comme antagonistes cruciaux du développement de Plasmodium. L’une d’entre elles, APL1C (Anopheles Plasmodium-responsive factor) protège spécifiquement le moustique contre les parasites Plasmodium de rongeurs en collaboration avec la protéine TEP1 du complément. En combinant des approches de biologie cellulaire et de génomique fonctionnelle, mon travail de thèse montre que le repas sanguin des moustiques induit le recrutement d’APL1C au niveau du pôle basal de l’épithélium digestif. Ce positionnement d’APL1C lui permet de se lier aux stades ookinètes du parasite émergeant du côté basal de l’épithélium, et ce, indépendamment de la fonction de TEP1. Néanmoins, cette action d’APL1C requiert la contribution des phagocytes et de la Nitration. Par ailleurs, mon travail montre que l’action d’APL1C ne se restreint pas à l'ookinète car elle agit aussi contre le dernier stade de développement de Plasmodium, les sporozoïtes. Avec la capacité de se lier aux sporozoites, APL1C contrôle la prévalence d’infection des glandes salivaires du moustique, mais avec des partenaires différents de ceux agissant sur les ookinètes. Finalement, une étude transcriptomique m’a permis d’identifier des facteurs agissant en aval d’APL1C. L’ensemble de ces résultats génère de nouvelles connaissances relatives à la fonction de cette famille de protéines LRR en tant que récepteurs de reconnaissance d'agents pathogènes capable de déclencher une réponse immunitaire dans différents compartiments tissulaires du moustiqueAnopheles mosquito is a vector of Plasmodium parasite, the causative agent of malaria. The Anopheles leucine-rich repeat (LRR) proteins were described as key antagonists of Plasmodium parasites in Anopheles mosquito midgut. APL1C (Anopheles Plasmodium-responsive factor) is a representative of LRR members which specifically protects against rodent malaria parasites by stabilizing the complement-like protein TEP1. By combining cell biology with functional genomic approaches, this study shows that mosquito bloodmeal induce the presence of an extracellular layer of APL1C protein surrounding the midgut beneath of the basal lamina. Consistently with the formation of this layer, APL1C binds to the ookinetes that emerged on the basal side of the midgut. This presence occurs independently from TEP1 function, requires the contribution of the phagocytic cells and nitration pathway. In addition, APL1C defence function is not restricted to the ookinete in the midgut but it also acts against the latest Plasmodium stage, the sporozoites. APL1C inhibits salivary glands infection prevalence, and consistently, it also binds to the surface of the sporozoites in the hemocoel. However, unlike to the midgut stages, anti-sporozoites APL1C-dependent mechanism involves different partners. Moreover, RNAseq study revealed APL1C gene targets, including genes with immune-like function. These results generate novel biological insight for the function of APL1C, and probably other LRR family members, as a pathogen recognition receptor inducing immune response against pathogens that come in contact with mosquito hemolymph compartment
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Calvié, Julien. "La représentation des riches et des pauvres en Grèce dans la littérature grecque du IVème siècle avant J. -C." Grenoble 2, 2000. http://www.theses.fr/2000GRE2A011.
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Epp, Anna. "Role of a novel C-terminal motif in Pannexin 1 trafficking and oligomerization." Thesis, 2019. http://hdl.handle.net/1828/10748.
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Pannexin 1 (Panx1) is a metabolite channel enriched in the brain and known to localize to the cell surface, where it is involved in a variety of neuronal processes including cell proliferation and differentiation. The mechanisms through which Panx1 is trafficked or stabilized at the surface, however, are not fully understood. The proximal Panx1 C-terminus (Panx1CT), upstream of a caspase-cleavage site has been demonstrated to be required for Panx1 cell-surface expression. We discovered a previously unreported putative leucine-rich repeat (LRR) motif within the proximal Panx1CT. I investigated the involvement of this putative LRR motif on Panx1 localization and oligomerization. Deletion of the putative LRR motif or uniquely the highly conserved segment of the putative LRR motif resulted in a significant loss of Panx1 cell surface expression. Finally, ectopic expression of Panx1-EGFP in HEK293T cells increased cell proliferation, which was not recapitulated by a Panx1 deletion mutant lacking the putative LRR motif. Overall the findings presented in this thesis provide new insights into the molecular determinants of Panx1 trafficking and oligomerization.Graduate
2020-02-14
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Arun, Vedant. "Validation and Functional Characterization of Novel Neurofibromin Interacting Proteins." Thesis, 2013. http://hdl.handle.net/1807/35166.
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Neurofibromin (NF1) is a 2,818aa protein encoded by the very large NF1 tumour suppressor gene located on chromosome 17q11.2. Loss of function mutations and deletions in NF1 underlie Neurofibromatosis type-1 (NF-1) - the most common inherited syndrome of the nervous system in humans with a birth incidence of 1:3,000. The most visible feature of NF-1 is the neoplastic manifestations known as neurofibromas, however, the syndrome is also characterized by pigmentary defects, peripheral motor dysfunction, learning disabilities and several developmental abnormalities. The molecular etiology of many of these non-neoplastic phenotypes remains unknown. Here we demonstrate that the Tubulin Binding Domain (TBD) of NF1 is a binding partner of the Leucine Rich Pentatrico Peptide Repeat motif-Containing protein (LRPPRC) and cytoplasmic Dynein Heavy Chain (DHC). The NF1-LRPPRC interaction is of high significance as it links NF-1 with Leigh’s Syndrome, French Canadian variant (LSFC) – an autosomal recessive neurodegenerative disorder that arises due to mutations in the LRPPRC gene. This interaction occurs as part of an RNA granule complex, and use of transgenic mouse models establishes an important role of NF1 and LRPPRC in peripheral nerve development. The NF1-DHC interaction is of importance in melanocytes where our studies suggest a possible role in melanosome localization, disruptions in which may underlie the abnormal pigmentary features known as café-au-lait macules that are commonly associated with NF-1. The validation of LRPPRC and DHC as novel NF1 interactors reveal new roles of NF1, which open the door to better understanding the molecular mechanisms that underlie the myriad of NF-1 manifestations.
Books on the topic "Motifs riches en leucines"
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D. I. Y. Productions pour tous. Coloriage Antistress de Fleurs et Motifs Floraux Pour Adulte. Volume 1: Cahier de 36 Planches de Dessin Riches en détails SoignéS. une Activité Artistique d'art Thérapie Qui Aide Au lâcher Prise. Independently Published, 2022.
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