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Relevant bibliographies by topics / Motifs riches en leucines

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Journal articles

Academic literature on the topic 'Motifs riches en leucines'

Author: Grafiati

Published: 25 May 2024

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Journal articles on the topic "Motifs riches en leucines"

1

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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2

Nufer, Oliver, Svend Guldbrandsen, Martin Degen, et al. "Role of cytoplasmic C-terminal amino acids of membrane proteins in ER export." Journal of Cell Science 115, no. 3 (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 othe

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3

Zhang, Yue, and Joseph T. Barbieri. "A Leucine-Rich Motif Targets Pseudomonas aeruginosa ExoS within Mammalian Cells." Infection and Immunity 73, no. 12 (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 bind

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4

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 (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

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5

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 (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 u

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6

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 (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 p

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7

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 S

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8

HAYES, H. "ADN et chromosomes." INRAE Productions Animales 13, HS (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 séq

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9

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 (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

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10

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 (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 pe

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