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Relevant bibliographies by topics / Multi-protein assembly

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Journal articles

Academic literature on the topic 'Multi-protein assembly'

Author: Grafiati

Published: 6 September 2023

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Journal articles on the topic "Multi-protein assembly"

1

Siggers, Trevor, and Raluca Gordân. "Protein–DNA binding: complexities and multi-protein codes." Nucleic Acids Research 42, no. 4 (2013): 2099–111. http://dx.doi.org/10.1093/nar/gkt1112.

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Abstract Binding of proteins to particular DNA sites across the genome is a primary determinant of specificity in genome maintenance and gene regulation. DNA-binding specificity is encoded at multiple levels, from the detailed biophysical interactions between proteins and DNA, to the assembly of multi-protein complexes. At each level, variation in the mechanisms used to achieve specificity has led to difficulties in constructing and applying simple models of DNA binding. We review the complexities in protein–DNA binding found at multiple levels and discuss how they confound the idea of simple

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2

Li, Mei, Erik Dujardin, and Stephen Mann. "Programmed assembly of multi-layered protein/nanoparticle-carbon nanotube conjugates." Chemical Communications, no. 39 (2005): 4952. http://dx.doi.org/10.1039/b509109h.

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3

Tørresen, Ole K., Bastiaan Star, Pablo Mier, et al. "Tandem repeats lead to sequence assembly errors and impose multi-level challenges for genome and protein databases." Nucleic Acids Research 47, no. 21 (2019): 10994–1006. http://dx.doi.org/10.1093/nar/gkz841.

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Abstract The widespread occurrence of repetitive stretches of DNA in genomes of organisms across the tree of life imposes fundamental challenges for sequencing, genome assembly, and automated annotation of genes and proteins. This multi-level problem can lead to errors in genome and protein databases that are often not recognized or acknowledged. As a consequence, end users working with sequences with repetitive regions are faced with ‘ready-to-use’ deposited data whose trustworthiness is difficult to determine, let alone to quantify. Here, we provide a review of the problems associated with t

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4

Farrugia, Thomas, Adam W. Perriman, Kamendra P. Sharma, and Stephen Mann. "Multi-enzyme cascade reactions using protein–polymer surfactant self-standing films." Chemical Communications 53, no. 13 (2017): 2094–97. http://dx.doi.org/10.1039/c6cc09809f.

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5

Venkatraman, Vishwesh, and David W. Ritchie. "Predicting Multi-Component Protein Assemblies Using an Ant Colony Approach." International Journal of Swarm Intelligence Research 3, no. 3 (2012): 19–31. http://dx.doi.org/10.4018/jsir.2012070102.

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Many biological processes are governed by large assemblies of protein molecules. However, it is often very difficult to determine the three-dimensional structures of these assemblies using experimental biophysical techniques. Hence there is a need to develop computational approaches to fill this gap. This article presents an ant colony optimization approach to predict the structure of large multi-component protein complexes. Starting from pair-wise docking predictions, a multi-graph consisting of vertices representing the component proteins and edges representing candidate interactions is cons

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6

Xian, Yuejiao, Chitra B. Karki, Sebastian Miki Silva, Lin Li, and Chuan Xiao. "The Roles of Electrostatic Interactions in Capsid Assembly Mechanisms of Giant Viruses." International Journal of Molecular Sciences 20, no. 8 (2019): 1876. http://dx.doi.org/10.3390/ijms20081876.

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In the last three decades, many giant DNA viruses have been discovered. Giant viruses present a unique and essential research frontier for studies of self-assembly and regulation of supramolecular assemblies. The question on how these giant DNA viruses assemble thousands of proteins so accurately to form their protein shells, the capsids, remains largely unanswered. Revealing the mechanisms of giant virus assembly will help to discover the mysteries of many self-assembly biology problems. Paramecium bursaria Chlorella virus-1 (PBCV-1) is one of the most intensively studied giant viruses. Here,

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7

Terzo, Esteban A., Shawn M. Lyons, John S. Poulton, Brenda R. S. Temple, William F. Marzluff, and Robert J. Duronio. "Distinct self-interaction domains promote Multi Sex Combs accumulation in and formation of the Drosophila histone locus body." Molecular Biology of the Cell 26, no. 8 (2015): 1559–74. http://dx.doi.org/10.1091/mbc.e14-10-1445.

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Nuclear bodies (NBs) are structures that concentrate proteins, RNAs, and ribonucleoproteins that perform functions essential to gene expression. How NBs assemble is not well understood. We studied the Drosophila histone locus body (HLB), a NB that concentrates factors required for histone mRNA biosynthesis at the replication-dependent histone gene locus. We coupled biochemical analysis with confocal imaging of both fixed and live tissues to demonstrate that the Drosophila Multi Sex Combs (Mxc) protein contains multiple domains necessary for HLB assembly. An important feature of this assembly p

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8

Mozdy, A. D., J. M. McCaffery, and J. M. Shaw. "Dnm1p Gtpase-Mediated Mitochondrial Fission Is a Multi-Step Process Requiring the Novel Integral Membrane Component Fis1p." Journal of Cell Biology 151, no. 2 (2000): 367–80. http://dx.doi.org/10.1083/jcb.151.2.367.

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Yeast Dnm1p is a soluble, dynamin-related GTPase that assembles on the outer mitochondrial membrane at sites where organelle division occurs. Although these Dnm1p-containing complexes are thought to trigger constriction and fission, little is known about their composition and assembly, and molecules required for their membrane recruitment have not been isolated. Using a genetic approach, we identified two new genes in the fission pathway, FIS1 and FIS2. FIS1 encodes a novel, outer mitochondrial membrane protein with its amino terminus exposed to the cytoplasm. Fis1p is the first integral membr

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9

Guo, Zhen, Zhiwei Shen, Yujiao Wang, Tingyuan Tan, and Yi Zhang. "Peptides Co-Assembling into Hydrangea-Like Microstructures." Journal of Nanoscience and Nanotechnology 20, no. 5 (2020): 3239–45. http://dx.doi.org/10.1166/jnn.2020.17393.

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Supramolecular assembly in vitro is a simple and effective way to produce multi-level biostructures to mimic the self-assembly of biomolecules in organisms. The study on peptide assembly behaviors would benefit a lot to understand what goes on in life, as well as in the construction of plenty of functional biomaterials that have potential applications in various fields. Since cellular microenvironments are crowded and contain various biomolecules, studying protein and peptide co-assembly is of great interest. Here, we introduced the co-assembly of 5-FAM-ELVFFAE-NH2 (EE-7) and (CY5)-KLVFFAK-NH2

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10

Tang, Jiakun, Ye Liu, Dongmei Qi, et al. "Nucleus‐Targeted Delivery of Multi‐Protein Self‐Assembly for Combined Anticancer Therapy." Small 17, no. 25 (2021): 2101219. http://dx.doi.org/10.1002/smll.202101219.

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