Relevant bibliographies by topics / Helix

Academic literature on the topic 'Helix'

Author: Grafiati
Published: 4 June 2021
Last updated: 31 January 2023

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Journal articles on the topic "Helix"

1

Regan, L. "Helix is a helix is a helix?" Proceedings of the National Academy of Sciences 94, no. 7 (April 1, 1997): 2796–97. http://dx.doi.org/10.1073/pnas.94.7.2796.

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Ciarapica, Roberta, Jessica Rosati, Gianni Cesareni, and Sergio Nasi. "Molecular Recognition in Helix-Loop-Helix and Helix-Loop-Helix-Leucine Zipper Domains." Journal of Biological Chemistry 278, no. 14 (January 3, 2003): 12182–90. http://dx.doi.org/10.1074/jbc.m211991200.

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Walther, Dirk, Clayton Springer, and Fred E. Cohen. "Helix-helix packing angle preferences for finite helix axes." Proteins: Structure, Function, and Genetics 33, no. 4 (December 1, 1998): 457–59. http://dx.doi.org/10.1002/(sici)1097-0134(19981201)33:4<457::aid-prot1>3.0.co;2-l.

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Gibson, Toby J., Peter R. Sibbald, and Peter Rice. "Rop/Helix-loop-helix similarity." DNA Sequence 1, no. 3 (January 1991): 213–15. http://dx.doi.org/10.3109/10425179109020773.

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Croom, Anna, Kylie B. Manning, and Marcus Weck. "Supramolecular Helix–Helix Block Copolymers." Macromolecules 49, no. 19 (September 28, 2016): 7117–28. http://dx.doi.org/10.1021/acs.macromol.6b01410.

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Camps-fabrer, H. "Helix." Encyclopédie berbère, no. 22 (January 1, 2000): 3426–28. http://dx.doi.org/10.4000/encyclopedieberbere.1712.

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Xin, Doris, Stephen Macke, Litian Ma, Jialin Liu, Shuchen Song, and Aditya Parameswaran. "HELIX." Proceedings of the VLDB Endowment 12, no. 4 (December 2018): 446–60. http://dx.doi.org/10.14778/3297753.3297763.

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Stefankiewicz, Artur R., André De Cian, and Jack Harrowfield. "Helix-helix interactions – homochirality and heterochirality." CrystEngComm 13, no. 24 (2011): 7207. http://dx.doi.org/10.1039/c1ce06081c.

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Preissner, R., A. Goede, and C. Frömmel. "Spare parts for helix–helix interaction." Protein Engineering, Design and Selection 12, no. 10 (October 1999): 825–32. http://dx.doi.org/10.1093/protein/12.10.825.

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Ben-Tal, N., and B. Honig. "Helix-helix interactions in lipid bilayers." Biophysical Journal 71, no. 6 (December 1996): 3046–50. http://dx.doi.org/10.1016/s0006-3495(96)79498-5.

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Dissertations / Theses on the topic "Helix"

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Cabeza, Joaquin Zacarías. "Molecular mechanisms of helix-loop-helix proteins." Thesis, University of Essex, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.442527.

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Sieber, Martin Sieber Martin. "DNA binding reaction of basic-helix-loop-helix proteins /." [S.l.] : [s.n.], 2000. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=13578.

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Down, G. "Analysis of helix-loop-helix factors in the skin." Thesis, University of Cambridge, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.598622.

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There is little data regarding the action of HLH proteins in the skin. I have used RT-PCR Northern blotting analysis, immunocytochemistry (ICC) and in situ hybridisation (ISH) to determine the expression profiles of Id1, Id2, Id3 and Id4 and the Class A factors E2A, E2-2 and HEB mRNAs and proteins during human keratinocyte differentiation both in vivo and in monolayer and organotype in vitro differentiation culture models, and in the human anagen hair follicle, the rat hair follicle growth cycle, and the human sebaceous gland and eccrine sweat gland. Preliminary RT-PCR analysis determined that the Class A factors, E2A, E2-2 and HEB and Id1, Id2 and Id3, and to a very limited extent Id4 mRNAs, were expressed by the epidermis and skin appendages. Northern blotting analysis demonstrated that Ca2+ induced cell cycle withdrawal and differentiation of primary human keratinocytes, determined by an up regulation of p21cip1 and involucrin mRNA expression, was inversely correlated with Id1, Id2 and Id3 mRNA expression. ICC and ISH analysis of human and rat epidermis confirmed Id protein and mRNA expression in the most proliferative layers of the epidermis. The sub-cellular localisation of Id1 protein was predominantly cytoplasmic, whereas that of Id2 and Id3 proteins was predominantly nuclear. Interestingly, a sub-population of supra-basal, post-mitotic keratinocytes also expressed Id1, Id2 and Id3 proteins in which the sub-cellular localisation of each was predominantly nuclear. Supra-basal Id expressing keratinocytes were often seen arranged in stacks extending from the basal layer to the confirmed layers and these cells may be post-mitotic keratinocytes with maintained capacity to re-enter the cell cycle, and may delineate epidermal proliferative units.
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Fuchs, Angelika Johanna Maria. "Helix-helix interactions in membrane proteins : analysis, prediction and applications." kostenfrei, 2010. https://mediatum2.ub.tum.de/node?id=820985.

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Nilsson, Jonas. "Cooperative reactive sites in designed helix-loop-helix polypeptide catalysts /." Linköping : Univ, 2002. http://www.bibl.liu.se/liupubl/disp/disp2002/tek759s.pdf.

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Bloor, A. J. C. "Proteins for the basic helix-loop-helix transcription factor SCL." Thesis, University of Cambridge, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.596727.

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Members of the basic Helix-Loop-Helix (bHLH) family of transcription factors play critical roles in the control of development processes in species ranging from yeast to humans. The product of the SCL (Stem Cell Leukaemia) gene is a bHLH protein that was first identified by its ectopic expression in a case of childhood acute leukaemia and it has subsequently been characterised as a key player in the regulation of the development of blood and endothelium. The mechanism by which SCL functions are unclear, however it is likely that it regulates target genes by the formation of cell specific multiprotein complexes. A number of such complexes have been identified, however only in a small number of cell types. The aim of this project was to identify novel SCL partner proteins in order to better understand how it functions both normally and as an oncogene. Over 300 potential SCL interaction partners were identified in a yeast 2-hybrid screen of an embryonic cDNA library. Of these, the interaction between SCL and RFP (Ret Finger Protein) was characterised in the greatest detail. RFP is a ubiquitously expressed TRIM (Tripartite Motif) protein and little was previously known about its cellular function. RFP interacts with SCL in vitro and a stable complex of the two proteins was isolated in both COS cells and the haemopoietic progenitor cell line of 416B. RFP also interacts with a subset of other bHLH proteins via the bHLH domain but not with other classes of transcription factors and functions to repress their ability to transactivate reporter genes. The expression pattern of RFP was studied in a panel of haemopoietic cell lines. The subcellular location of RFP correlates with the lineage and development stage of the cell and also appears to be cell cycle regulated which suggests a number of novel mechanisms by which it could regulate SCL or other bHLH factors. Moreover, RFP is able to inhibit the ability of myogenic bHLH factors to convert multipotent fibroblasts into muscle indicating that its interaction with bHLH proteins is biologically significant.
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Imabayashi, Takeshi. "Expression of basic helix-loop-helix proteins in the glomeruli." Kyoto University, 2001. http://hdl.handle.net/2433/150563.

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Saarikettu, Juha. "Calcium regulation and functions of basic Helix-Loop-Helix transcription factors." Doctoral thesis, Umeå : Department of Molecular Biology, Umeå University, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-537.

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King, Gavin W. "Investigating helix-helix interactions in the transmembrane domains of membrane proteins." Thesis, University of Warwick, 2009. http://wrap.warwick.ac.uk/3157/.

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Helix-helix interactions between membrane-spanning transmembrane (TM) domains have been shown to drive the assembly of α-helical membrane proteins within biological membranes. However, the rules that determine these interactions are not yet fully understood, despite such interactions being found in an increasing number of proteins. Recent work has implicated TM domain interactions in the formation of the protein complex Ii-MHC, formed from the association of Major Histocompatibility Complex Class II (MHC) and the MHC-associated-Invariant Chain (Ii) proteins. Following biosynthesis, three MHC α/βheterodimers bind to the Ii homotrimer to form a nonameric Ii-MHC complex within the endoplasmic reticulum. This is a critical step in the export of MHC molecules to the antigen presentation system and hence the activation of an immune response to a pathogen. In this study we have explored the TM domain interactions within the Ii-MHC complex. Results from in vivo and in vitro experiments revealed the TM domains of the α- and β-chains of MHC have a propensity to self-associate into homo-dimers and to associate with one another to form hetero-dimers. Highly conserved GxxxG motifs (known to drive dimerization) were implicated in these interactions. The TM domain of Ii was confirmed to self-associate to form trimers by in vivo and in vitro methods, but surprisingly also displayed additional oligomeric states suggesting the interaction is not as specific as was previously thought. Furthermore, we show that in vivo, the TM domain of Ii can associate with those of the α- and β-chains of MHC, whilst in vitro methods suggested Ii preferentially binds to α-chains. Collectively, these findings strongly suggest that the TM domains of Ii and MHC have a role to play in the assembly of the Ii-MHC complex, and hence the very important process of antigen presentation. Additionally, in this study we have undertaken development of NMR spectroscopy methods that have the potential to increase our understanding of not only the Ii-MHC complex, but protein-protein interactions in general.
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Ma, Philip Chun-Ming. "Structural studies on the basic-helix-loop-helix region from MyoD." Thesis, Massachusetts Institute of Technology, 1994. http://hdl.handle.net/1721.1/28070.

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Books on the topic "Helix"

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Littlewood, Trevor D. Helix-loop-helix transcription factors. 3rd ed. Oxford: Oxford University Press, 1998.

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Littlewood, Trevor D. Transcription factors 2: helix-loop-helix. London: Academic Press, 1995.

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Littlewood, Trevor D. Transcription factors 2: helix-loop-helix. London: Academic Press, 1994.

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Balthasar, Burkhard. Helix aspersa. Gent: Imschoot, Uitgevers voor IC, 1991.

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Dawn, Robyn. Double helix. [S.l.]: Marquette Press, 1998.

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Jones, Steve. Single Helix. S.l: Abacus, 2006.

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1971-, Millar Jay, ed. Double helix. Toronto: Mercury Press, 2006.

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Double helix. New York: Dial Books, 2004.

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Double helix. Pittsburgh, PA: [Pemberton Mysteries, 2009.

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Copyright Paperback Collection (Library of Congress), ed. Steel helix. New York: Ballantine Books, 2003.

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Book chapters on the topic "Helix"

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Gooch, Jan W. "Helix-Loop-Helix Motif." In Encyclopedic Dictionary of Polymers, 897. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13886.

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Gooch, Jan W. "Helix-Turn-Helix Motif." In Encyclopedic Dictionary of Polymers, 897. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13887.

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Weik, Martin H. "helix." In Computer Science and Communications Dictionary, 718. Boston, MA: Springer US, 2000. http://dx.doi.org/10.1007/1-4020-0613-6_8302.

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Blundell, B. G., C. N. Daskalakis, N. A. E. Heyes, and T. P. Hopkins. "HELIX." In An Introductory Guide to Silvar Lisco and HILO Simulators, 97–124. London: Macmillan Education UK, 1987. http://dx.doi.org/10.1007/978-1-349-09748-7_5.

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Murre, C. "The Helix-Loop-Helix Motif." In Nucleic Acids and Molecular Biology, 102–11. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-77356-3_6.

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Engelman, D. M., B. Adair, A. Brunger, J. Hunt, T. Kahn, M. Lemmon, K. MacKenzie, and H. Treutlein. "Helix-helix interactions inside membranes." In Biochemistry of Cell Membranes, 297–310. Basel: Birkhäuser Basel, 1995. http://dx.doi.org/10.1007/978-3-0348-9057-1_21.

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Orzáez, Mar, Francisco J. Taberner, Enrique Pérez-Payá, and Ismael Mingarro. "Helix-Helix Packing Between Transmembrane Fragments." In Methods in Proteome and Protein Analysis, 1–14. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-662-08722-0_1.

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Hill, Keith, Tom Baranowski, Walter Schmidt, Nicole Prommer, Michel Audran, Philippe Connes, Ramiro L. Gutiérrez, et al. "Basic Helix-Loop-Helix (bHLH) proteins." In Encyclopedia of Exercise Medicine in Health and Disease, 116. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2139.

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Turiault, Marc, Caroline Cohen, Guy Griebel, David E. Nichols, Britta Hahn, Gary Remington, Ronald F. Mucha, et al. "Transmembrane Helix." In Encyclopedia of Psychopharmacology, 1335. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_1897.

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Gooch, Jan W. "Double Helix." In Encyclopedic Dictionary of Polymers, 241. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_3954.

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Conference papers on the topic "Helix"

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Hassanzadeh, Oktie, Songyun Duan, Achille Fokoue, Anastasios Kementsietsidis, Kavitha Srinivas, and Michael J. Ward. "Helix." In the 20th international conference companion. New York, New York, USA: ACM Press, 2011. http://dx.doi.org/10.1145/1963192.1963295.

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Sidi, Lior, Yisroel Mirsky, Asaf Nadler, Yuval Elovici, and Asaf Shabtai. "Helix." In CIKM '20: The 29th ACM International Conference on Information and Knowledge Management. New York, NY, USA: ACM, 2020. http://dx.doi.org/10.1145/3340531.3416022.

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Campanoni, Simone, Timothy Jones, Glenn Holloway, Vijay Janapa Reddi, Gu-Yeon Wei, and David Brooks. "HELIX." In the Tenth International Symposium. New York, New York, USA: ACM Press, 2012. http://dx.doi.org/10.1145/2259016.2259028.

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Lou, Qian, Sarath Chandra Janga, and Lei Jiang. "Helix." In PACT '20: International Conference on Parallel Architectures and Compilation Techniques. New York, NY, USA: ACM, 2020. http://dx.doi.org/10.1145/3410463.3414626.

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Zaicu, Nicu Florin, Matthew Luckie, Richard Nelson, and Marinho Barcellos. "Helix." In SOSR '21: The ACM SIGCOMM Symposium on SDN Research. New York, NY, USA: ACM, 2021. http://dx.doi.org/10.1145/3482898.3483354.

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Del Signore, Marcella, Giuseppe Morando, and Elena Del Signore. "HELIX." In ACADIA 2014: Design Agency. ACADIA, 2014. http://dx.doi.org/10.52842/conf.acadia.2014.047.

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Mineo, Mauro, and Claudio Paoloni. "Helix TWT yield improvement by helix pitch optimization." In 2009 IEEE International Vacuum Electronics Conference (IVEC). IEEE, 2009. http://dx.doi.org/10.1109/ivelec.2009.5193485.

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Slater, Mike, and C. W. Trueman. "Helix Design for cylindrical helix antennas with matching sections." In Symposium on Antenna Technology and Applied Electromagnetics [ANTEM 2000]. IEEE, 2000. http://dx.doi.org/10.1109/antem.2000.7851725.

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Bímová, Daniela. "Teaching helix and problems connected with helix using GeoGebra." In PROCEEDINGS OF THE 43RD INTERNATIONAL CONFERENCE APPLICATIONS OF MATHEMATICS IN ENGINEERING AND ECONOMICS: (AMEE’17). Author(s), 2017. http://dx.doi.org/10.1063/1.5014002.

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K. McMullen, David. "Helix Pedestrian Bridge." In Structures Congress 2005. Reston, VA: American Society of Civil Engineers, 2005. http://dx.doi.org/10.1061/40753(171)25.

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Reports on the topic "Helix"

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WAYNE STATE UNIV DETROIT MI. Triple Helix. Fort Belvoir, VA: Defense Technical Information Center, August 2008. http://dx.doi.org/10.21236/ada485466.

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Pyster, Art, Deva Henry, Nicole Hutchsion, Kahina Lasfer, and Stan Rifkin. The Helix Project. Fort Belvoir, VA: Defense Technical Information Center, May 2013. http://dx.doi.org/10.21236/ada589302.

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Moroz, P. E. Double-helix stellarator. Office of Scientific and Technical Information (OSTI), September 1997. http://dx.doi.org/10.2172/537394.

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Rodriguez, Michelle M. Helix Tool Introduction Laboratories. Fort Belvoir, VA: Defense Technical Information Center, January 2012. http://dx.doi.org/10.21236/ada585593.

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Luccio, A. FIELD OF A HELIX. Office of Scientific and Technical Information (OSTI), August 1994. http://dx.doi.org/10.2172/1151306.

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Prohofsky, E. W. A Spectroscopy of Helix Melting. Fort Belvoir, VA: Defense Technical Information Center, January 1992. http://dx.doi.org/10.21236/ada252739.

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Pyster, Art, Ricardo Pineda, Devanandham Henry, and Nicole Hutchison. Helix - Phases 1 and 2. Fort Belvoir, VA: Defense Technical Information Center, December 2013. http://dx.doi.org/10.21236/ada603048.

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Wang, Ru T. Electromagnetic Scattering from a Helix. Fort Belvoir, VA: Defense Technical Information Center, September 1986. http://dx.doi.org/10.21236/ada173608.

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Rainer Meinke, Ph D., Carl Goodzeit, and Ph D. Millicent Ball. Concentric Titled Double-Helix Dipole Magnets. Office of Scientific and Technical Information (OSTI), September 2003. http://dx.doi.org/10.2172/817768.

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Davison, Jack W., John C. Knight, Michele Co, Jason D. Hiser, and Anh Nguyen-Tuong. Kevlar: Transitioning Helix for Research to Practice. Fort Belvoir, VA: Defense Technical Information Center, March 2016. http://dx.doi.org/10.21236/ad1005651.

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