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Relevant bibliographies by topics / Long alpha helix

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Academic literature on the topic 'Long alpha helix'

Author: Grafiati

Published: 3 June 2025

Last updated: 31 July 2025

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Journal articles on the topic "Long alpha helix"

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Funato, Noriko, Yuki Taga, Lindsay E. Laurie, Chisa Tometsuka, Masashi Kusubata, and Kiyoko Ogawa-Goto. "The Transcription Factor HAND1 Is Involved in Cortical Bone Mass through the Regulation of Collagen Expression." International Journal of Molecular Sciences 21, no. 22 (2020): 8638. http://dx.doi.org/10.3390/ijms21228638.

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Temporal and/or spatial alteration of collagen family gene expression results in bone defects. However, how collagen expression controls bone size remains largely unknown. The basic helix-loop-helix transcription factor HAND1 is expressed in developing long bones and is involved in their morphogenesis. To understand the functional role of HAND1 and collagen in the postnatal development of long bones, we overexpressed Hand1 in the osteochondroprogenitors of model mice and found that the bone volumes of cortical bones decreased in Hand1Tg/+;Twist2-Cre mice. Continuous Hand1 expression downregula

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Ruggiero, F., J. Comte, C. Cabanas, and R. Garrone. "Structural requirements for alpha 1 beta 1 and alpha 2 beta 1 integrin mediated cell adhesion to collagen V." Journal of Cell Science 109, no. 7 (1996): 1865–74. http://dx.doi.org/10.1242/jcs.109.7.1865.

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A large variety of cells adhere to and spread on specific regions within the triple helix of collagens, mainly via alpha 1 beta 1 and alpha 2 beta 1 integrins. Disruption of collagen triple helical integrity generally affects the efficiency of cell adhesion on different collagens including collagen V. This report addresses the question of the importance of the linear sequence of the constitutive alpha-chains versus the triple helical conformation in the recognition of collagen V binding sites. To investigate this question, in vitro renaturation of the isolated alpha 1 (V) and alpha 2 (V) chain

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DEWEY, T. GREGORY. "SEQUENCE GENERATING FUNCTIONS AND THE MULTIFRACTAL FORMALISM: APPLICATIONS TO BIOPOLYMERS." Fractals 03, no. 01 (1995): 9–22. http://dx.doi.org/10.1142/s0218348x95000035.

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Helix-coil configurations in biopolymers can be represented as a symbolic sequence of helix and coil units. A given configuration can be generated by progressing down the branches of a binary tree. The probability weighting of the branches in the tree will depend on the specific model under consideration. The multifractal nature of this binary tree can be described by an adaptation of a statistical mechanical formalism that uses sequence generating functions. It is seen that the sequence generating function approach is equivalent to transfer matrix methods for processes involving one-step memo

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Klein, G., CA Muller, E. Tillet, ML Chu, and R. Timpl. "Collagen type VI in the human bone marrow microenvironment: a strong cytoadhesive component." Blood 86, no. 5 (1995): 1740–48. http://dx.doi.org/10.1182/blood.v86.5.1740.bloodjournal8651740.

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Collagen type VI, which forms characteristic microfibrillar structures, is assembled from three individual alpha(VI) chains that form a short triple helix and two adjacent globular domains. Expression of all three alpha (VI) collagen chains in the human bone marrow (BM) microenvironment could be detected by chain-specific antibodies in tissue sections and in the adherent stromal layer of long-term BM cultures. In functional studies, collagen type VI was shown to be a strong adhesive substrate for various hematopoietic cell lines and light-density BM mononuclear cells. The adhesive site within

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Muljaningsih, Sri, Multifiah Multifiah, and Ajeng Kartika Galuh. "Synergicity of Triple Helix Creative Economy Model in Malang." MIMBAR : Jurnal Sosial dan Pembangunan 34, no. 1 (2018): 185–94. http://dx.doi.org/10.29313/mimbar.v34i1.3327.

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The Triple Helix concept, the government-academics-business relationship, has been established in response to the 2005-2025 Creative Economy Long-term National Development Plan, especially in the mission of economic value creation of creative innovation. This study explores the factors influencing sinergicity of the triple helix model with SMEs' organic product in Malang as its object. This research was conducted with mixed methodology of FGD and survey. Validity and reliability test were performed based on the Cronbach's Alpha value and after being fulfilled, continue with analysis factor. Th

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Cieślik-Boczula, Katarzyna. "Alpha-helix to beta-sheet transition in long-chain poly- l -lysine: Formation of alpha-helical fibrils by poly- l -lysine." Biochimie 137 (June 2017): 106–14. http://dx.doi.org/10.1016/j.biochi.2017.03.006.

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Yanaka-Okada, Saeko, Emiko Sano, Norio Naruse, et al. "Targeted-glycosylation of "non-core region" of interleukin-11 modulates its biological function. (57.15)." Journal of Immunology 186, no. 1_Supplement (2011): 57.15. http://dx.doi.org/10.4049/jimmunol.186.supp.57.15.

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Abstract Human interleukin-11 (hIL-11) is a pleiotropic cytokine administered to patients for recovering low platelet counts. From a structural point of view hIL-11 belongs to the long-helix cytokine superfamily, which is characterized by a conserved core motif consisting of four alpha-helices. We have investigated the region of hIL-11 that does not belong to the alpha-helical bundle motif, which we have termed “non-core region”. The interleukin was N- or O-glycosylated at specific positions within the non-core region, and the functional consequences of these modifications were examined in cel

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Weinzierl, Robert O. J. "The Bridge Helix of RNA Polymerase Acts as a Central Nanomechanical Switchboard for Coordinating Catalysis and Substrate Movement." Archaea 2011 (2011): 1–7. http://dx.doi.org/10.1155/2011/608385.

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The availability ofin vitroassembly systems to produce recombinant archaeal RNA polymerases (RNAPs) offers one of the most powerful experimental tools for investigating the still relatively poorly understood molecular mechanisms underlying RNAP function. Over the last few years, we pioneered new robot-based high-throughput mutagenesis approaches to study structure/function relationships within various domains surrounding the catalytic center. The Bridge Helix domain, which appears in numerous X-ray structures as a 35-amino-acid-long alpha helix, coordinates the concerted movement of several ot

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Keller, Paul W., Marc C. Johnson, and Volker M. Vogt. "Mutations in the Spacer Peptide and Adjoining Sequences in Rous Sarcoma Virus Gag Lead to Tubular Budding." Journal of Virology 82, no. 14 (2008): 6788–97. http://dx.doi.org/10.1128/jvi.00213-08.

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ABSTRACT All orthoretroviruses encode a single structural protein, Gag, which is necessary and sufficient for the assembly and budding of enveloped virus-like particles from the cell. The Gag proteins of Rous sarcoma virus (RSV) and human immunodeficiency virus type 1 (HIV-1) contain a short spacer peptide (SP or SP1, respectively) separating the capsid (CA) and nucleocapsid (NC) domains. SP or SP1 and the residues immediately upstream are known to be critical for proper assembly. Using mutagenesis and electron microscopy analysis of insect cells or chicken cells overexpressing RSV Gag, we def

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Batebi, Hossein, Guillermo Pérez-Hernández, Sabrina N. Rahman, et al. "Mechanistic insights into G-protein coupling with an agonist-bound G-protein-coupled receptor." Nature Structural & Molecular Biology 31, no. 11 (2024): 1692–701. https://doi.org/10.1038/s41594-024-01334-2.

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G-protein-coupled receptors (GPCRs) activate heterotrimeric G proteins by promoting guanine nucleotide exchange. Here, we investigate the coupling of G proteins with GPCRs and describe the events that ultimately lead to the ejection of GDP from its binding pocket in the Gα subunit, the rate-limiting step during G-protein activation. Using molecular dynamics simulations, we investigate the temporal progression of structural rearrangements of GDP-bound G<sub>s</sub> protein (G<sub>s</sub>·GDP; hereafter G<sub>s</sub><sup>GDP</sup>) upon coupling to the β<sub>2</sub>-adrene

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Dissertations / Theses on the topic "Long alpha helix"

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Hauck, Nastasja C. [Verfasser]. "No escape mutants and decreased variability of viral quasispecies after immunization against long alpha helix of pandemic H1N1 in a mouse model study / Nastasja Christine Hauck." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2020. http://d-nb.info/1218530227/34.

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Hauck, Nastasja Christine [Verfasser]. "No escape mutants and decreased variability of viral quasispecies after immunization against long alpha helix of pandemic H1N1 in a mouse model study / Nastasja Christine Hauck." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2020. http://d-nb.info/1218530227/34.

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Book chapters on the topic "Long alpha helix"

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Pizza, M., M. R. Fontana, and R. Rappuoli. "Cholera toxin (Vibrio cholerae)." In Guidebook to Protein Toxins and Their Use in Cell Biology. Oxford University PressOxford, 1997. http://dx.doi.org/10.1093/oso/9780198599555.003.0009.

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Abstract CT is composed of two subunits, A and B, of 27 and 57.5 kDa respectively, held together by noncovalent interactions. The B subunit which contains the receptor binding site, is formed by five identical monomers, each of 11.5 kDa which assemble into a ring like oligomeric structure having a central hole. The CT receptor is the glycosfingolipid, GM1 ganglioside. The A subunit is composed of the enzymatically active A1 domain that is connected to the B subunit through the A2 domain, a long alpha helix inserted into the central hole of the B subunit (Fig. 1) (Rappuoli and Pizza 1991; Sixma

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Dewey, T. Gregory. "Fractal Aspects of Protein Structure." In Fractals In Molecular Biophysics. Oxford University PressNew York, NY, 1998. http://dx.doi.org/10.1093/oso/9780195084474.003.0002.

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Abstract Proteins are individually sculpted molecules the three-dimensional structure of which is dictated by their amino acid sequence. They are heteropolymers with a variable composition of 20 different amino acids. The amino acid sequence is referred to as the primary structure. For most proteins, the information contained in the primary structure is sufficient to dictate the three-dimensional folding of the protein. The peptide linkages that join the amino acid residues are planar and have two characteristic dihedral angles associated with them. These bond rotations are referred to as the

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