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Journal articles on the topic '060802 Animal Cell and Molecular Biology'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Wright, G. J. "Animal magic uncloaked: Molecular Principles of Animal Development." Journal of Cell Science 116, no. 1 (January 1, 2003): 5—a—6. http://dx.doi.org/10.1242/jcs.00188.

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2

Ghose, Piya, and Shai Shaham. "Cell death in animal development." Development 147, no. 14 (July 15, 2020): dev191882. http://dx.doi.org/10.1242/dev.191882.

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ABSTRACTCell death is an important facet of animal development. In some developing tissues, death is the ultimate fate of over 80% of generated cells. Although recent studies have delineated a bewildering number of cell death mechanisms, most have only been observed in pathological contexts, and only a small number drive normal development. This Primer outlines the important roles, different types and molecular players regulating developmental cell death, and discusses recent findings with which the field currently grapples. We also clarify terminology, to distinguish between developmental cell death mechanisms, for which there is evidence for evolutionary selection, and cell death that follows genetic, chemical or physical injury. Finally, we suggest how advances in understanding developmental cell death may provide insights into the molecular basis of developmental abnormalities and pathological cell death in disease.

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3

Takeichi, M. "The cadherins: cell-cell adhesion molecules controlling animal morphogenesis." Development 102, no. 4 (April 1, 1988): 639–55. http://dx.doi.org/10.1242/dev.102.4.639.

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Cadherins are a family of glycoproteins involved in the Ca2+-dependent cell-cell adhesion mechanism which is detected in most kinds of tissues. Inhibition of the cadherin activity with antibodies induces dissociation of cell layers, indicating a fundamental importance of these molecules in maintaining the multicellular structure. Cadherins are divided into subclasses, including E-, N- and P-cadherins. While all subclasses are similar in molecular weight, Ca2+- and protease-sensitivity, each subclass is characterized by a unique tissue distribution pattern and immunological specificity. Analysis of amino acid sequences deduced from cDNA encoding these molecules showed that they are integral membrane proteins of 723–748 amino acids long and share common sequences; similarity in the sequences between subclasses is in a range of 50–60% when compared within a single animal species. L cells, with very little endogenous cadherin activity, transfected with the cadherin cDNA acquired high cadherin-mediated aggregating activity. Their colony morphology was altered by the ectopic expression of cadherins from the dispersed type to the compact type, providing direct evidence for a key role of cadherins in cell-cell adhesion. It has been suggested that cadherins bind cells by their homophilic interactions at the extracellular domain and are associated with actin bundles at the cytoplasmic domain. It appears that each cadherin subclass has binding specificity and this molecular family is involved in selective cell-cell adhesion. In development, the expression of each cadherin subclass is spatiotemporally regulated and associated with a variety of morphogenetic events; e.g. the termination or initiation of expression of a cadherin subclass in a given cell collective is correlated with its segregation from or connection with other cell collectives. Antibodies to cadherins were shown to perturb the morphogenesis of some embryonic organs in vitro. These observations suggest that cadherins play a crucial role in construction of tissues and the whole animal body.

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4

KNIGHT, D., G. SHAH, and G. GOUGH. "Methods in molecular biology, vol. 5: Animal cell cultures." Trends in Biotechnology 8 (1990): 371. http://dx.doi.org/10.1016/0167-7799(90)90237-r.

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5

Clynes, M. "Animal cell culture (methods in molecular biology, volume 5)." FEBS Letters 287, no. 1-2 (August 5, 1991): 231. http://dx.doi.org/10.1016/0014-5793(91)80066-c.

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6

Burridge, A. "Molecular Principles of Animal Development." International Journal of Biochemistry & Cell Biology 35, no. 1 (January 2003): 111. http://dx.doi.org/10.1016/s1357-2725(02)00073-0.

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7

Moss, Eric G., and Jennifer Romer-Seibert. "Cell-intrinsic timing in animal development." Wiley Interdisciplinary Reviews: Developmental Biology 3, no. 5 (July 24, 2014): 365–77. http://dx.doi.org/10.1002/wdev.145.

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8

Merten, Otto-Wilhelm. "Animal cell culture: A practical approach." Trends in Biochemical Sciences 11, no. 10 (October 1986): 412. http://dx.doi.org/10.1016/0968-0004(86)90170-2.

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9

Bliem, Rudolf F. "Animal cell technology — principles and products." Trends in Biochemical Sciences 13, no. 8 (August 1988): 325–26. http://dx.doi.org/10.1016/0968-0004(88)90134-x.

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10

Ricci, Lorenzo, and Mansi Srivastava. "Wound-induced cell proliferation during animal regeneration." Wiley Interdisciplinary Reviews: Developmental Biology 7, no. 5 (May 2, 2018): e321. http://dx.doi.org/10.1002/wdev.321.

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11

Fabry, M. E. "Transgenic animal models of sickle cell disease." Experientia 49, no. 1 (January 1993): 28–36. http://dx.doi.org/10.1007/bf01928785.

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12

Gabius, Hans-Joachim. "Animal Lectins." European Journal of Biochemistry 243, no. 3 (February 1997): 543–76. http://dx.doi.org/10.1111/j.1432-1033.1997.t01-1-00543.x.

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13

Moon, Richard C. "Animal models." Journal of Cellular Biochemistry 53, S17F (1993): 82. http://dx.doi.org/10.1002/jcb.240531011.

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14

Flint, Jonathan. "Animal models of anxiety and their molecular dissection." Seminars in Cell & Developmental Biology 14, no. 1 (February 2003): 37–42. http://dx.doi.org/10.1016/s1084-9521(02)00170-2.

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15

Fentem, Julia H. "Book Review: Methods in Molecular Biology Volume 5: Animal Cell Culture." Alternatives to Laboratory Animals 20, no. 1 (January 1992): 177. http://dx.doi.org/10.1177/026119299202000128.

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16

Timpson, Paul, Ewan J. McGhee, and Kurt I. Anderson. "Imaging molecular dynamics in vivo – from cell biology to animal models." Journal of Cell Science 124, no. 17 (August 30, 2011): 2877–90. http://dx.doi.org/10.1242/jcs.085191.

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17

Perrino, Fred W., and Lawrence A. Loeb. "Animal cell DNA polymerases in DNA repair." Mutation Research/DNA Repair 236, no. 2-3 (September 1990): 289–300. http://dx.doi.org/10.1016/0921-8777(90)90012-t.

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18

Allen, Elizabeth A., and Eric H. Baehrecke. "Autophagy in animal development." Cell Death & Differentiation 27, no. 3 (January 27, 2020): 903–18. http://dx.doi.org/10.1038/s41418-020-0497-0.

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19

Weis, William I. "Cell-surface carbohydrate recognition by animal and viral lectins." Current Opinion in Structural Biology 7, no. 5 (October 1997): 624–30. http://dx.doi.org/10.1016/s0959-440x(97)80070-x.

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20

Jacobson, Michael D., Miguel Weil, and Martin C. Raff. "Programmed Cell Death in Animal Development." Cell 88, no. 3 (February 1997): 347–54. http://dx.doi.org/10.1016/s0092-8674(00)81873-5.

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21

Nicoll, Charles S., and Sharon M. Russell. "Animal rights, animal research, and human obligations." Molecular and Cellular Neuroscience 3, no. 4 (August 1992): 271–77. http://dx.doi.org/10.1016/1044-7431(92)90023-u.

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22

Lindenbach, Brett D., and Charles M. Rice. "RNAi Targeting an Animal Virus." Molecular Cell 9, no. 5 (May 2002): 925–27. http://dx.doi.org/10.1016/s1097-2765(02)00539-7.

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23

Harding, John, R. Roberts, and Oleg Mirochnitchenko. "Large animal models for stem cell therapy." Stem Cell Research & Therapy 4, no. 2 (2013): 23. http://dx.doi.org/10.1186/scrt171.

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24

Salvesen, Guy S., Anne Hempel, and Nuria S. Coll. "Protease signaling in animal and plant-regulated cell death." FEBS Journal 283, no. 14 (December 31, 2015): 2577–98. http://dx.doi.org/10.1111/febs.13616.

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25

Mozdziak, Paul E., James N. Petitte, and Susan D. Carson. "An introductory undergraduate course covering animal cell culture techniques." Biochemistry and Molecular Biology Education 32, no. 5 (September 2004): 319–22. http://dx.doi.org/10.1002/bmb.2004.494032050381.

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26

Trobridge, G. D., and H.-P. Kiem. "Large animal models of hematopoietic stem cell gene therapy." Gene Therapy 17, no. 8 (April 29, 2010): 939–48. http://dx.doi.org/10.1038/gt.2010.47.

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27

Lukas, Jiri. "Animal cell electroporation and electrofusion protocols. Methods in molecular biology, Vol. 48." FEBS Letters 381, no. 3 (March 4, 1996): 263. http://dx.doi.org/10.1016/s0014-5793(96)90653-5.

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28

McCartney, M. "Animal Behavior Follows Rewards." Science Signaling 7, no. 345 (September 30, 2014): ec273-ec273. http://dx.doi.org/10.1126/scisignal.2005961.

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29

Öztürk, Nuri, Sang-Hun Song, Christopher P. Selby, and Aziz Sancar. "Animal Type 1 Cryptochromes." Journal of Biological Chemistry 283, no. 6 (December 5, 2007): 3256–63. http://dx.doi.org/10.1074/jbc.m708612200.

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30

Bertrand, Vincent. "β‐catenin‐driven binary cell fate decisions in animal development." Wiley Interdisciplinary Reviews: Developmental Biology 5, no. 3 (March 7, 2016): 377–88. http://dx.doi.org/10.1002/wdev.228.

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31

Smith, J. C., K. Symes, J. Heasman, A. Snape, and C. C. Wylie. "My favourite cell. TheXenopus animal pole blastomere." BioEssays 7, no. 5 (November 1987): 229–34. http://dx.doi.org/10.1002/bies.950070509.

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32

Ben-Ze've, Avri. "Animal cell shape changes and gene expression." BioEssays 13, no. 5 (May 1991): 207–12. http://dx.doi.org/10.1002/bies.950130502.

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33

Kageura, H., and K. Yamana. "Pattern formation in 8-cell composite embryos of Xenopus laevis." Development 91, no. 1 (February 1, 1986): 79–100. http://dx.doi.org/10.1242/dev.91.1.79.

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We have shown in defect experiments that an 8-cell embryo of Xenopus laevis consists of three kinds of cells, that is, animal, vegetal dorsal and vegetal ventral cells, and that cells of different kinds are distinctly different in their developmental capacity. Complete pattern formation occurs in any defect embryo which contains at least two animal, one vegetal dorsal and one vegetal ventral cell. In the present transplantation experiments, we replaced one or two cells of one 8-cell embryo by those of another to obtain 29 series of composite embryos, in which the cell composition of an embryo and/or the dorsoventral orientation of individual cells differed from those of a normal 8-cell embryo. The resulting embryos were examined macroscopically when controls reached stage 26 (tailbud stage) and later. The results showed that both the two animal dorsal cells or one vegetal dorsal cell could be replaced by animal ventral cells or a vegetal ventral cell, respectively, without any detectable effect on pattern formation, irrespective of the ventrodorsal direction of the ventral cells. On the other hand, replacement of an animal ventral or a vegetal ventral cell by an animal dorsal or a vegetal dorsal cell, respectively, made most composite embryos twins. Twins were also formed when a left-handed vegetal dorsal cell was replaced by a right-handed counterpart and vice versa. In these composite embryos, the dorsoventral orientation of the transplanted cell was different from that of a resident dorsal cell or cells of a recipient, and several lines of evidence show that the dorsal cell transplanted in an off-axis orientation is responsible for twin formation. Thus, dorsal cells have the capacity to form dorsal axial structures at later stages and this capacity is localized on the dorsal side, and endows the cells with polarity. On the other hand, ventral cells did not have this capacity or polarity, judging from the fact that their orientation had no effect on pattern formation. One vegetal dorsal or ventral cell could be replaced by an animal dorsal or ventral cell, respectively, without any marked effect. However, replacement of two vegetal cells by animal ones and of one or two animal cells by vegetal ones resulted in deficiency of vegetal cells and oedema and in deficiency of animal cells and incomplete invagination, respectively. Twin formation in composite embryos with animal dorsal cells in place of animal ventral ones is discussed in consideration of findings in recombination experiments by Nieuwkoop.

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34

Sartin, J. L. "CELL BIOLOGY SYMPOSIUM: Molecular Basis for Feed Efficiency12." Journal of Animal Science 91, no. 4 (April 1, 2013): 1580–81. http://dx.doi.org/10.2527/jas.2013-6365.

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35

Eisenstein, Michael. "Natural animal magnetism." Nature Methods 2, no. 5 (May 2005): 328. http://dx.doi.org/10.1038/nmeth0505-328a.

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36

Ciuffi, Angela, Keshet Ronen, Troy Brady, Nirav Malani, Gary Wang, Charles C. Berry, and Frederic D. Bushman. "Methods for integration site distribution analyses in animal cell genomes." Methods 47, no. 4 (April 2009): 261–68. http://dx.doi.org/10.1016/j.ymeth.2008.10.028.

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37

Trobridge, Grant, Brian C. Beard, and Hans-Peter Kiem. "Hematopoietic Stem Cell Transduction and Amplification in Large Animal Models." Human Gene Therapy 16, no. 12 (December 2005): 1355–66. http://dx.doi.org/10.1089/hum.2005.16.1355.

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38

Yang, Xiang-Jiao. "MOZ and MORF acetyltransferases: Molecular interaction, animal development and human disease." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1853, no. 8 (August 2015): 1818–26. http://dx.doi.org/10.1016/j.bbamcr.2015.04.014.

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39

Spier, R. E. "Advances in Animal Cell Biology and Technology for Bioprocesses." Vaccine 7, no. 1 (February 1989): 85–86. http://dx.doi.org/10.1016/0264-410x(89)90038-8.

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40

Griffin, Gilly. "Book Review: Animal Cell Technology." Alternatives to Laboratory Animals 16, no. 1 (September 1988): 98. http://dx.doi.org/10.1177/026119298801600120.

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41

Sun, Qi-An, Francesca Zappacosta, Valentina M. Factor, Peter J. Wirth, Dolph L. Hatfield, and Vadim N. Gladyshev. "Heterogeneity within Animal Thioredoxin Reductases." Journal of Biological Chemistry 276, no. 5 (November 1, 2000): 3106–14. http://dx.doi.org/10.1074/jbc.m004750200.

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42

Mushegian, Alexandra A. "How bacteria induce animal metamorphosis." Science Signaling 9, no. 445 (September 13, 2016): ec211-ec211. http://dx.doi.org/10.1126/scisignal.aaj1824.

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43

Mushegian, Alexandra A. "Sources of variation: Animal microbiota." Science Signaling 10, no. 467 (February 21, 2017): eaam9011. http://dx.doi.org/10.1126/scisignal.aam9011.

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44

Faurie, Cécile, Muriel Golzio, Pernille Moller, Justin Teissié, and Marie-Pierre Rols. "Cell and Animal Imaging of Electrically Mediated Gene Transfer." DNA and Cell Biology 22, no. 12 (December 2003): 777–83. http://dx.doi.org/10.1089/104454903322624984.

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45

Rowland, Douglas J., Jason S. Lewis, and Michael J. Welch. "Molecular imaging: The application of small animal positron emission tomography." Journal of Cellular Biochemistry 87, S39 (2002): 110–15. http://dx.doi.org/10.1002/jcb.10417.

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46

Dobrynin, Mikhail A., Ekaterina O. Bashendjieva, and Natella I. Enukashvily. "Germ Granules in Animal Oogenesis." Journal of Developmental Biology 10, no. 4 (October 9, 2022): 43. http://dx.doi.org/10.3390/jdb10040043.

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In eukaryotic cells, many macromolecules are organized as membraneless biomolecular condensates (or biocondensates). Liquid–liquid and liquid–solid phase transitions are the drivers of the condensation process. The absence of membrane borders makes biocondensates very flexible in their composition and functions, which vary in different cells and tissues. Some biocondensates are specific for germ line cells and are, thus, termed germ granules. This review summarizes the recent data on the composition of germ granules and their functions in gametes. According to these data, germ granules are involved in the determination of germline cells in some animals, such as Amphibia. In other animals, such as Mammalia, germ granules are involved in the processes of transposons inactivation and sequestration of mRNA and proteins to temporarily decrease their activity. The new data on germ granules composition and functions sheds light on germ cell differentiation and maturation properties.

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47

Matova, Nina, and Lynn Cooley. "Comparative Aspects of Animal Oogenesis." Developmental Biology 231, no. 2 (March 2001): 291–320. http://dx.doi.org/10.1006/dbio.2000.0120.

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48

Koestner, Adalbert. "Prognostic Role of Cell Morphology of Animal Tumors." Toxicologic Pathology 13, no. 2 (February 1985): 90–94. http://dx.doi.org/10.1177/019262338501300205.

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49

Clark, Andrew G., Ortrud Wartlick, Guillaume Salbreux, and Ewa K. Paluch. "Stresses at the Cell Surface during Animal Cell Morphogenesis." Current Biology 24, no. 10 (May 2014): R484—R494. http://dx.doi.org/10.1016/j.cub.2014.03.059.

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50

Ruvkun, Gary. "ABSTRACT The taxonomy of animal developmental controlgenes revealed by the first complete animal genome sequence." Biochemistry and Cell Biology 78, no. 5 (October 1, 2000): 650. http://dx.doi.org/10.1139/o00-048.

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