Relevant bibliographies by topics / Alpha-solenoid proteins

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Alpha-solenoid proteins'

Author: Grafiati
Published: 25 May 2024
Last updated: 31 July 2025

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Journal articles on the topic "Alpha-solenoid proteins"

1

Fournier, David, Gareth A. Palidwor, Sergey Shcherbinin, et al. "Functional and Genomic Analyses of Alpha-Solenoid Proteins." PLoS ONE 8, no. 11 (2013): e79894. http://dx.doi.org/10.1371/journal.pone.0079894.

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2

Arrías, Paula Nazarena, Zarifa Osmanli, Estefanía Peralta, Patricio Manuel Chinestrad, Alexander Miguel Monzon, and Silvio C. E. Tosatto. "Diversity and structural‐functional insights of alpha‐solenoid proteins." Protein Science 33, no. 11 (2024). http://dx.doi.org/10.1002/pro.5189.

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AbstractAlpha‐solenoids are a significant and diverse subset of structured tandem repeat proteins (STRPs) that are important in various domains of life. This review examines their structural and functional diversity and highlights their role in critical cellular processes such as signaling, apoptosis, and transcriptional regulation. Alpha‐solenoids can be classified into three geometric folds: low curvature, high curvature, and corkscrew, as well as eight subfolds: ankyrin repeats; Huntingtin, elongation factor 3, protein phosphatase 2A, and target of rapamycin; armadillo repeats; tetratricope
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3

Izert, Matylda Anna, Patrycja Emanuela Szybowska, Maria Wiktoria Górna, and Matthew Merski. "The Effect of Mutations in the TPR and Ankyrin Families of Alpha Solenoid Repeat Proteins." Frontiers in Bioinformatics 1 (July 6, 2021). http://dx.doi.org/10.3389/fbinf.2021.696368.

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Protein repeats are short, highly similar peptide motifs that occur several times within a single protein, for example the TPR and Ankyrin repeats. Understanding the role of mutation in these proteins is complicated by the competing facts that 1) the repeats are much more restricted to a set sequence than non-repeat proteins, so mutations should be harmful much more often because there are more residues that are heavily restricted due to the need of the sequence to repeat and 2) the symmetry of the repeats in allows the distribution of functional contributions over a number of residues so that
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4

Pankiv, Serhiy, Anette Kathinka Dahl, Aleksander Aas, et al. "BEACH domain proteins function as cargo-sorting adaptors in secretory and endocytic pathways." Journal of Cell Biology 223, no. 12 (2024). http://dx.doi.org/10.1083/jcb.202408173.

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We identify BEACH domain–containing proteins (BDCPs) as novel membrane coat proteins involved in the sorting of transmembrane proteins (TMPs) on the trans-Golgi network and tubular sorting endosomes. The seven typical mammalian BDCPs share a predicted alpha-solenoid-beta propeller structure, suggesting they have a protocoatomer origin and function. We map the subcellular localization of seven BDCPs based on their dynamic colocalization with RAB and ARF small GTPases and identify five typical BDCPs on subdomains of dynamic tubular-vesicular compartments on the intersection of endocytic recyclin
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Dissertations / Theses on the topic "Alpha-solenoid proteins"

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Cattelin, Céline. "Exploration de la diversité des protéines à solénoïdes alpha, régulatrices de l'expression des gènes des organites dans les lignées eucaryotes photosynthétiques et étude de la dynamique conformationnelle des protéines à "PentatricoPeptide Repeats"." Electronic Thesis or Diss., Sorbonne université, 2023. http://www.theses.fr/2023SORUS158.

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Au sein des Archaeplastida (eucaryotes photosynthétiques ayant acquis un chloroplaste suite à une endosymbiose avec une cyanobactérie ancestrale) les génomes chloroplastiques et mitochondriaux des algues vertes et des plantes terrestres sont régulés de manière post-transcriptionnelle, principalement par des protéines à solénoïde alpha codées dans le noyau. Ces facteurs nucléaires sont composés de motifs répétés dégénérés (protéines PPR et OPR, respectivement pentatricopeptide repeat et octatricopeptide repeats) interagissant de façon spécifique avec une partie de la séquence de leur ARN cible
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Book chapters on the topic "Alpha-solenoid proteins"

1

Cheng Hung-Yi, Pai Tun-Wen, and Fujita Hamido. "An automatic structural detection system for alpha-solenoid repeats." In Frontiers in Artificial Intelligence and Applications. IOS Press, 2015. https://doi.org/10.3233/978-1-61499-522-7-157.

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Tandem repeat structures are widely distributed among all classes of proteins. Various basic structural units of repetitive nature possess functional diversity and reflect important influences on biological responses for different organisms. One of the most common types of protein repeat structure is the α-solenoid tandem repeat class which possesses low sequence similarity between any two repeat units within a structure. Therefore, a successful segmentation system for identifying each repeat unit cannot be achieved mainly based on sequence comparison approaches. For a comprehensive
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2

Wang Teng-Wei, Lo Ying-Tsang, Pai Tun-Wen, and Fujita Hamido. "A prediction system for ankyrin repeat domain family." In Frontiers in Artificial Intelligence and Applications. IOS Press, 2015. https://doi.org/10.3233/978-1-61499-522-7-168.

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Ankyrin Repeat Domain (ARD) is an alpha-solenoid repeat structure formed by cascading a series of ankyrin repeat units. These fundamental repeat units within a structure possess low sequence similarity but high structural conservation. An ARD serves as a protein–protein interaction platform in nature, and it is discovered as an important factor influencing hypoxia response through hydroxylation interaction with Factor Inhibiting HIF (FIH) enzymes which can repress HIF under normoxia environment. In this study, we designed a sequence based method incorporated with secondary structural
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