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Relevant bibliographies by topics / Molecular evolution / Journal articles

Journal articles on the topic 'Molecular evolution'

To see the other types of publications on this topic, follow the link: Molecular evolution.

Author: Grafiati

Published: 4 June 2021

Last updated: 31 August 2024

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1

Del Cortona, Andrea, and Frederik Leliaert. "Molecular evolution and morphological diversification of ulvophytes (Chlorophyta)." Perspectives in Phycology 5, no. 1 (June 1, 2018): 27–43. http://dx.doi.org/10.1127/pip/2017/0075.

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2

Flook, Paul. "Molecular evolution." Journal of Evolutionary Biology 12, no. 3 (May 1999): 628–29. http://dx.doi.org/10.1046/j.1420-9101.1999.0072b.x.

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3

MacIntyre, Ross J. "Molecular Evolution." BioEssays 21, no. 3 (March 29, 1999): 265–66. http://dx.doi.org/10.1002/(sici)1521-1878(199903)21:3<265::aid-bies14>3.0.co;2-j.

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4

CLEGG, M. T. "Molecular Evolution: Molecular Evolutionary Genetics." Science 235, no. 4788 (January 30, 1987): 599. http://dx.doi.org/10.1126/science.235.4788.599.

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5

Trifonov, Edward N. "Early Molecular Evolution." Israel Journal of Ecology and Evolution 52, no. 3-4 (April 12, 2006): 375–87. http://dx.doi.org/10.1560/ijee_52_3-4_375.

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Four fundamentally novel, recent developments make a basis for the Theory of Early Molecular Evolution. The theory outlines the molecular events from the onset of the triplet code to the formation of the earliest sequence/structure/function modules of proteins. These developments are: (1) Reconstruction of the evolutionary chart of codons; (2) Discovery of omnipresent protein sequence motifs, apparently conserved since the last common ancestor; (3) Discovery of closed loops—standard structural modules of modern proteins; (4) Construction of protein sequence space of module size fragments, with far-reaching evolutionary implications. The theory generates numerous predictions, confirmed by massive nucleotide and protein sequence analyses, such as existence of two distinct classes of amino acids, and their periodical distribution along the sequences. The emerging picture of the earliest molecular evolutionary events is outlined: consecutive engagement of codons, formation of the earliest short peptides, and growth of the polypeptide chains to the size of loop closure, 25-30 residues.

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6

Joyce, Gerald F. "Directed Molecular Evolution." Scientific American 267, no. 6 (December 1992): 90–97. http://dx.doi.org/10.1038/scientificamerican1292-90.

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7

Kauffman, Stuart A. "Applied molecular evolution." Journal of Theoretical Biology 157, no. 1 (July 1992): 1–7. http://dx.doi.org/10.1016/s0022-5193(05)80753-2.

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8

Posada, David. "Cancer Molecular Evolution." Journal of Molecular Evolution 81, no. 3-4 (August 20, 2015): 81–83. http://dx.doi.org/10.1007/s00239-015-9695-7.

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9

Lin, Shu-Kun. "Molecular diversity evolution." Molecular Diversity 10, no. 1 (February 2006): 1. http://dx.doi.org/10.1007/s11030-006-5684-5.

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10

Easteal, Simon. "Disciplining molecular evolution." Trends in Ecology & Evolution 13, no. 8 (August 1998): 336. http://dx.doi.org/10.1016/s0169-5347(98)01404-9.

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11

Wang, Conan K., and David J. Craik. "Linking molecular evolution to molecular grafting." Journal of Biological Chemistry 296 (January 2021): 100425. http://dx.doi.org/10.1016/j.jbc.2021.100425.

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12

FUSHIMI, YUZURU. "Molecular evolution engineering of protein. 1. Definition of molecular evolution engineering." Kagaku To Seibutsu 37, no. 10 (1999): 678–84. http://dx.doi.org/10.1271/kagakutoseibutsu1962.37.678.

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13

Stoll, Claude. "Chromosomal evolution: Molecular cytogenetic evolution of mammals." European Journal of Human Genetics 21, no. 11 (October 17, 2013): 1330. http://dx.doi.org/10.1038/ejhg.2013.4.

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14

Trevors, J. T. "Mistakes & Molecular Evolution." American Biology Teacher 60, no. 4 (April 1, 1998): 248–49. http://dx.doi.org/10.2307/4450466.

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15

Yamaguchi, Yumi, and Takashi Gojobori. "Molecular evolution of viruses." Uirusu 46, no. 1 (1996): 1–6. http://dx.doi.org/10.2222/jsv.46.1.

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16

Ito, Yasuhiko. "Molecular Evolution of Paramyxoviruses." Uirusu 46, no. 1 (1996): 35–41. http://dx.doi.org/10.2222/jsv.46.35.

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17

Shirakata, Masaki, and Kanji Hirai. "Molecular evolution of herpesviruses." Uirusu 46, no. 1 (1996): 43–48. http://dx.doi.org/10.2222/jsv.46.43.

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18

Piast, Michał, Irena Kustrzeba-Wójcicka, Małgorzata Matusiewicz, and Teresa Banaś. "Molecular evolution of enolase." Acta Biochimica Polonica 52, no. 2 (May 15, 2005): 507–13. http://dx.doi.org/10.18388/abp.2005_3466.

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Enolase (EC 4.2.1.11) is an enzyme of the glycolytic pathway catalyzing the dehydratation reaction of 2-phosphoglycerate. In vertebrates the enzyme exists in three isoforms: alpha, beta and gamma. The amino-acid and nucleotide sequences deposited in the GenBank and SwissProt databases were subjected to analysis using the following bioinformatic programs: ClustalX, GeneDoc, MEGA2 and S.I.F.T. (sort intolerant from tolerant). Phylogenetic trees of enolases created with the use of the MEGA2 program show evolutionary relationships and functional diversity of the three isoforms of enolase in vertebrates. On the basis of calculations and the phylogenetic trees it can be concluded that vertebrate enolase has evolved according to the "birth and death" model of evolution. An analysis of amino acid sequences of enolases: non-neuronal (NNE), neuron specific (NSE) and muscle specific (MSE) using the S.I.F.T. program indicated non-uniform number of possible substitutions. Tolerated substitutions occur most frequently in alpha-enolase, while the lowest number of substitutions has accumulated in gamma-enolase, which may suggest that it is the most recently evolved isoenzyme of enolase in vertebrates.

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19

WILLIAMS, JOHN. "Molecular Evolution and Protobiology." Biochemical Society Transactions 13, no. 4 (August 1, 1985): 798. http://dx.doi.org/10.1042/bst0130798.

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20

Karavanich, C. A., and R. R. Anholt. "Molecular evolution of olfactomedin." Molecular Biology and Evolution 15, no. 6 (June 1, 1998): 718–26. http://dx.doi.org/10.1093/oxfordjournals.molbev.a025975.

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21

Davidson, C. J., E. G. D. Tuddenham, and J. H. McVey. "Molecular evolution of haemostasis." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A185. http://dx.doi.org/10.1042/bst028a185a.

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22

Hiramatsu, Keiichi. "Molecular Evolution of MRSA." Microbiology and Immunology 39, no. 8 (August 1995): 531–43. http://dx.doi.org/10.1111/j.1348-0421.1995.tb02239.x.

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23

KRICHELDORF, HANS R., MICHAEL AU, and THOMAS MANG. "Models of molecular evolution." International Journal of Peptide and Protein Research 26, no. 2 (January 12, 2009): 149–57. http://dx.doi.org/10.1111/j.1399-3011.1985.tb03191.x.

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24

Babkin, I. V., and S. N. Shchelkunov. "Molecular evolution of poxviruses." Russian Journal of Genetics 44, no. 8 (August 2008): 895–908. http://dx.doi.org/10.1134/s1022795408080036.

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25

Thomas, Richard H. "Molecular Evolution and Phylogenetics." Heredity 86, no. 3 (March 2001): 385. http://dx.doi.org/10.1046/j.1365-2540.2001.0923a.x.

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26

Torkar, Michaela. "Molecular evolution of language." Genome Biology 3 (2002): spotlight—20020815–01. http://dx.doi.org/10.1186/gb-spotlight-20020815-01.

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27

Lloyd, A. "Fundamentals of Molecular Evolution." Briefings in Bioinformatics 1, no. 2 (January 1, 2000): 202–4. http://dx.doi.org/10.1093/bib/1.2.202.

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28

Irwin, David M. "Molecular evolution of proglucagon." Regulatory Peptides 98, no. 1-2 (April 2001): 1–12. http://dx.doi.org/10.1016/s0167-0115(00)00232-9.

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29

Brookfield, John F. Y. "Molecular Evolution: Retroposon revivals." Current Biology 5, no. 3 (March 1995): 255–56. http://dx.doi.org/10.1016/s0960-9822(95)00053-4.

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30

Schuster, Peter. "Landscapes and molecular evolution." Physica D: Nonlinear Phenomena 107, no. 2-4 (September 1997): 351–65. http://dx.doi.org/10.1016/s0167-2789(97)00104-8.

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31

Woolley, Paul. "Molecular evolution of life." FEBS Letters 238, no. 1 (September 26, 1988): 218–19. http://dx.doi.org/10.1016/0014-5793(88)80263-1.

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32

Domingo, Esteban, Mauricio G. Mateu, Cristina Escarmis, Encarnacion Martinez-Salas, David Andreu, Ernest Giralt, Nuria Verdaguer, and Ignasi Fita. "Molecular evolution of aphthoviruses." Virus Genes 11, no. 2-3 (June 1995): 197–207. http://dx.doi.org/10.1007/bf01728659.

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33

Goodman, Morris. "Workshop on molecular evolution." Molecular Phylogenetics and Evolution 1, no. 1 (March 1992): 83. http://dx.doi.org/10.1016/1055-7903(92)90038-i.

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34

Marks, Jon. "Molecular evolution of life." Journal of Human Evolution 16, no. 3 (March 1987): 315–16. http://dx.doi.org/10.1016/0047-2484(87)90009-1.

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35

Finkel, D., and L. Finkel. "Molecular evolution and protobiology." Mathematical Modelling 7, no. 9-12 (1986): 1659. http://dx.doi.org/10.1016/0270-0255(86)90104-1.

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36

Schuster, Peter. "Dynamics of molecular evolution." Physica D: Nonlinear Phenomena 22, no. 1-3 (October 1986): 100–119. http://dx.doi.org/10.1016/0167-2789(86)90236-8.

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37

Gillespie, J. H. "Rates of Molecular Evolution." Annual Review of Ecology and Systematics 17, no. 1 (November 1986): 637–65. http://dx.doi.org/10.1146/annurev.es.17.110186.003225.

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38

Bulmer, M. G. "Molecular evolution of life." Endeavour 11, no. 4 (January 1987): 221. http://dx.doi.org/10.1016/0160-9327(87)90314-0.

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39

Riera, A. "Evolution of molecular structure." Journal of Molecular Structure 300 (December 1993): 93–104. http://dx.doi.org/10.1016/0022-2860(93)87009-x.

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40

Trevors, J. T. "Molecular evolution in bacteria." Antonie van Leeuwenhoek 67, no. 4 (1995): 315–24. http://dx.doi.org/10.1007/bf00872929.

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41

Kambhampati, Srinivas. "Fundamentals of Molecular Evolution." American Entomologist 39, no. 1 (1993): 47. http://dx.doi.org/10.1093/ae/39.1.47.

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42

Li, Li, Makoto Kobayashi, Hiroshi Kaneko, Yaeko Nakajima-Takagi, Yuko Nakayama, and Masayuki Yamamoto. "Molecular Evolution of Keap1." Journal of Biological Chemistry 283, no. 6 (December 5, 2007): 3248–55. http://dx.doi.org/10.1074/jbc.m708702200.

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43

Sugden, A. M. "ECOLOGY/EVOLUTION: Molecular Latitude." Science 299, no. 5613 (March 14, 2003): 1627d—1627. http://dx.doi.org/10.1126/science.299.5613.1627d.

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44

Ohta, Tomoko. "Mechanisms of molecular evolution." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 355, no. 1403 (November 29, 2000): 1623–26. http://dx.doi.org/10.1098/rstb.2000.0724.

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Both drift and selection are important for nucleotide substitutions in evolution. The nearly neutral theory was developed to clarify the effects of these processes. In this article, the nearly neutral theory is presented with special reference to the nature of weak selection. The mean selection coefficient is negative, and the variance is dependent on the environmental diversity. Some facts relating to the theory are reviewed. As well as nucleotide substitutions, illegitimate recombination events such as duplications, deletions and gene conversions leave indelible marks on molecular evolution. Gene duplication and conversion are sources of the evolution of new gene functions. Positive selection is necessary for the evolution of novel functions. However, many examples of current gene families suggest that both drift and selection are at work on their evolution.

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45

Schuster, Peter. "Molecular insights into evolution." Artificial Life and Robotics 3, no. 1 (March 1999): 19–23. http://dx.doi.org/10.1007/bf02481482.

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46

Brookfield, John F. Y., and Paul M. Sharp. "Processes of molecular evolution." Trends in Ecology & Evolution 3, no. 10 (October 1988): 250–51. http://dx.doi.org/10.1016/0169-5347(88)90056-0.

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47

Doyon, C., G. Drouin, V. L. Trudeau, and T. W. Moon. "Molecular Evolution of Leptin." General and Comparative Endocrinology 124, no. 2 (November 2001): 188–98. http://dx.doi.org/10.1006/gcen.2001.7701.

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48

Doyon, C., G. Drouin, V. L. Trudeau, and T. W. Moon. "Molecular Evolution of Leptin." General and Comparative Endocrinology 126, no. 1 (March 2002): 123. http://dx.doi.org/10.1006/gcen.2002.7815.

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49

FORST, CHRISTIAN V. "Molecular Evolution of Catalysis." Journal of Theoretical Biology 205, no. 3 (August 2000): 409–31. http://dx.doi.org/10.1006/jtbi.2000.2076.

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50

Schuster, Peter, and Peter F. Stadler. "Networks in molecular evolution." Complexity 8, no. 1 (September 2002): 34–42. http://dx.doi.org/10.1002/cplx.10052.

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