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Journal articles on the topic 'Mind'

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Published: 4 June 2021

Last updated: 1 July 2024

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1

Hu, Zonglin, Cristian Saez, and Joe Lutkenhaus. "Recruitment of MinC, an Inhibitor of Z-Ring Formation, to the Membrane in Escherichia coli: Role of MinD and MinE." Journal of Bacteriology 185, no. 1 (January 1, 2003): 196–203. http://dx.doi.org/10.1128/jb.185.1.196-203.2003.

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ABSTRACT In Escherichia coli, the min system prevents division away from midcell through topological regulation of MinC, an inhibitor of Z-ring formation. The topological regulation involves oscillation of MinC between the poles of the cell under the direction of the MinDE oscillator. Since the mechanism of MinC involvement in the oscillation is unknown, we investigated the interaction of MinC with the other Min proteins. We observed that MinD dimerized in the presence of ATP and interacted with MinC. In the presence of a phospholipid bilayer, MinD bound to the bilayer and recruited MinC in an ATP-dependent manner. Addition of MinE to the MinCD-bilayer complex resulted in release of both MinC and MinD. The release of MinC did not require ATP hydrolysis, indicating that MinE could displace MinC from the MinD-bilayer complex. In contrast, MinC was unable to displace MinE bound to the MinD-bilayer complex. These results suggest that MinE induces a conformational change in MinD bound to the bilayer that results in the release of MinC. Also, it is argued that binding of MinD to the membrane activates MinC.

2

Zhou, Huaijin, and Joe Lutkenhaus. "The Switch I and II Regions of MinD Are Required for Binding and Activating MinC." Journal of Bacteriology 186, no. 5 (March 1, 2004): 1546–55. http://dx.doi.org/10.1128/jb.186.5.1546-1555.2004.

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ABSTRACT MinD and MinC cooperate to form an efficient inhibitor of Z-ring formation that is spatially regulated by MinE. MinD activates MinC by recruiting it to the membrane and targeting it to a septal component. To better understand this activation, we have isolated loss-of-function mutations in minD and carried out site-directed mutagenesis. Many of these mutations block MinC-MinD interaction; however, they also prevent MinD self-interaction and membrane binding, suggesting that they affect nucleotide interaction or protein folding. Two mutations in the switch I region (MinD box) and one mutation in the switch II region had little affect on most MinD functions, such as MinD self-interaction, membrane binding, and MinE stimulation; however, they did eliminate MinD-MinC interaction. Two additional mutations in the switch II region did not affect MinC binding. Further study revealed that one of these allowed the MinCD complex to target to the septum but was still deficient in blocking division. These results indicate that the switch I and II regions of MinD are required for interaction with MinC but not MinE and that the switch II region has a role in activating MinC.

3

Zhou, Huaijin, and Joe Lutkenhaus. "MinC Mutants Deficient in MinD- and DicB-Mediated Cell Division Inhibition Due to Loss of Interaction with MinD, DicB, or a Septal Component." Journal of Bacteriology 187, no. 8 (April 15, 2005): 2846–57. http://dx.doi.org/10.1128/jb.187.8.2846-2857.2005.

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ABSTRACT The min locus encodes a negative regulatory system that limits formation of the cytokinetic Z ring to midcell by preventing its formation near the poles. Of the three Min proteins, MinC is the inhibitor and prevents Z-ring formation by interacting directly with FtsZ. MinD activates MinC by recruiting it to the membrane and conferring a higher affinity on the MinCD complex for a septal component. MinE regulates the cellular location of MinCD by inducing MinD, and thereby MinC, to oscillate between the poles of the cell, resulting in a time-averaged concentration of MinCD on the membrane that is lowest at midcell. MinC can also be activated by the prophage-encoded protein DicB, which targets MinC to the septum without recruiting it first to the membrane. Previous studies have shown that the C-terminal domain of MinC is responsible for the interaction with MinD, DicB, and the septal component. In the present study, we isolated mutations in the C-terminal domain of MinC that affected its interaction with MinD, DicB, and the septal component. Among the mutations isolated, R133A and S134A are specifically deficient in the interaction with MinD, E156A is primarily affected in the interaction with DicB, and R172A is primarily deficient in the interaction with the septum. These mutations differentiate the interactions of MinC with its partners and further support the model of MinCD- and MinC-DicB-mediated cell division inhibition.

4

Cadwallader, Gouverneur. "Reader Minds Mind Reading." Science News 156, no. 13 (September 25, 1999): 195. http://dx.doi.org/10.2307/4011776.

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5

Taviti, Ashoka Chary, and Tushar Kant Beuria. "MinD directly interacting with FtsZ at the H10 helix suggests a model for robust activation of MinC to destabilize FtsZ polymers." Biochemical Journal 474, no. 18 (September 8, 2017): 3189–205. http://dx.doi.org/10.1042/bcj20170357.

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Cell division in bacteria is a highly controlled and regulated process. FtsZ, a bacterial cytoskeletal protein, forms a ring-like structure known as the Z-ring and recruits more than a dozen other cell division proteins. The Min system oscillates between the poles and inhibits the Z-ring formation at the poles by perturbing FtsZ assembly. This leads to an increase in the FtsZ concentration at the mid-cell and helps in Z-ring positioning. MinC, the effector protein, interferes with Z-ring formation through two different mechanisms mediated by its two domains with the help of MinD. However, the mechanism by which MinD triggers MinC activity is not yet known. We showed that MinD directly interacts with FtsZ with an affinity stronger than the reported MinC–FtsZ interaction. We determined the MinD-binding site of FtsZ using computational, mutational and biochemical analyses. Our study showed that MinD binds to the H10 helix of FtsZ. Single-point mutations at the charged residues in the H10 helix resulted in a decrease in the FtsZ affinity towards MinD. Based on our findings, we propose a novel model for MinCD–FtsZ interaction, where MinD through its direct interaction with FtsZ would trigger MinC activity to inhibit FtsZ functions.

6

Zemach, Eddy. "Unconscious Mind or Conscious Minds?" Midwest Studies in Philosophy 10 (1986): 121–49. http://dx.doi.org/10.1111/j.1475-4975.1987.tb00537.x.

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7

Janssen, Jos. "Mathematical Tourists: Mind your Minds!" Mathematical Intelligencer 36, no. 2 (March 27, 2014): 50–53. http://dx.doi.org/10.1007/s00283-014-9449-1.

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8

Nagel, Michael. "Mind the Mind." International Journal of Learning: Annual Review 16, no. 2 (2009): 33–42. http://dx.doi.org/10.18848/1447-9494/cgp/v16i02/46109.

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9

Landau, Ofir, Rami Puzis, and Nir Nissim. "Mind Your Mind." ACM Computing Surveys 53, no. 1 (May 29, 2020): 1–38. http://dx.doi.org/10.1145/3372043.

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10

Taghbalout, Aziz, Luyan Ma, and Lawrence Rothfield. "Role Of MinD-Membrane Association in Min Protein Interactions." Journal of Bacteriology 188, no. 8 (April 15, 2006): 2993–3001. http://dx.doi.org/10.1128/jb.188.8.2993-3001.2006.

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ABSTRACT Division site placement in Escherichia coli involves interactions of the MinD protein with MinC and MinE and with other MinD molecules to form membrane-associated polymeric structures. In this work, as part of a study of these interactions, we established that heterologous membrane-associated proteins such as MinD can be targeted to the yeast nuclear membrane, dependent only on the presence of a membrane-binding domain and a nuclear targeting sequence. Targeting to the nuclear membrane was equally effective using the intrinsic MinD membrane-targeting domain or the completely unrelated membrane-targeting domain of cytochrome b 5. The chimeric proteins differing in their membrane-targeting sequences were then used to establish the roles of membrane association and specificity of the membrane anchor in MinD interactions, using the yeast two-hybrid system. The chimeric proteins were also used to show that the membrane association of MinD and MinE in E. coli cells had no specificity for the membrane anchor, whereas formation of MinDE polar zones and MinE rings required the presence of the native MinD membrane-targeting sequence.

11

Shuxratovna, Muxtorova Nasiba, Prabha Kiran, and Ekiz Erdogan. "Smart Tourism Triggers Tourist Minds-Do you have the mind to mind it?" International Journal Vallis Aurea 9, no. 1 (June 30, 2023): 19–36. http://dx.doi.org/10.2507/ijva.9.1.2.99.

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The essential aspect of Smart tourism is that it is transforming as a result of the digital revolution. The advancement of new technology has resulted in remarkable digital transformations in the tourist industry. Tourism was one of the most affected sectors during the ongoing pandemic situation. The sector is in need of drastic strategic decisions focusing on Tourist locations, complexes, goods, business experiences, and ecosystems as these are continuously evolving. This involves establishing and growing new business partnerships, business models, and capabilities in the tourist industry. The research aim is to analyse the role of smart tourism in emerging countries with a special focus on Uzbekistan and its challenges and to use a conceptual approach and focus on the travel and tourism business. Our study aims to identify the relationship between trust and Smart tourism dissemination in digital marketing through the lens of the theory of mind (ToM). ToM plays a mediating role in enhancing the image of a smart destination and consequently improves tourists’ behavioral intentions. The study findings have revealed that there exists a significant role in tourism innovations and their advantages and barriers in developing countries.

12

Johnson, Jay E., Laura L. Lackner, and Piet A. J. de Boer. "Targeting of DMinC/MinD and DMinC/DicB Complexes to Septal Rings in Escherichia coli Suggests a Multistep Mechanism for MinC-Mediated Destruction of Nascent FtsZ Rings." Journal of Bacteriology 184, no. 11 (June 1, 2002): 2951–62. http://dx.doi.org/10.1128/jb.184.11.2951-2962.2002.

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ABSTRACT The MinC protein is an important determinant of septal ring positioning in Escherichia coli. The N-terminal domain (ZMinC) suppresses septal ring formation by interfering with FtsZ polymerization, whereas the C-terminal domain (DMinC) is required for dimerization as well as for interaction with the MinD protein. MinD oscillates between the membrane of both cell halves in a MinE-dependent fashion. MinC oscillates along with MinD such that the time-integrated concentration of ZMinC at the membrane is minimal, and hence the stability of FtsZ polymers is maximal, at the cell center. MinC is cytoplasmic and fails to block FtsZ assembly in the absence of MinD, indicating that recruitment of MinC by MinD to the membrane enhances ZMinC function. Here, we present evidence that the binding of DMinC to MinD endows the MinC/MinD complex with a more specific affinity for a septal ring-associated target in vivo. Thus, MinD does not merely attract MinC to the membrane but also aids MinC in specifically binding to, or in close proximity to, the substrate of its ZMinC domain. MinC-mediated division inhibition can also be activated in a MinD-independent fashion by the DicB protein of cryptic prophage Kim. DicB shows little homology to MinD, and how it stimulates MinC function has been unclear. Similar to the results obtained with MinD, we find that DicB interacts directly with DMinC, that the DMinC/DicB complex has a high affinity for some septal ring target(s), and that MinC/DicB interferes with the assembly and/or integrity of FtsZ rings in vivo. The results suggest a multistep mechanism for the activation of MinC-mediated division inhibition by either MinD or DicB and further expand the number of properties that can be ascribed to the Min proteins.

13

WONG, Teresa. "Christ's Mind, Paul's Mind." Louvain Studies 17, no. 2 (July 1, 1992): 293–305. http://dx.doi.org/10.2143/ls.17.2.2013803.

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14

Singh, Gary. "Zen Mind, Machine Mind." IEEE Computer Graphics and Applications 40, no. 4 (July 1, 2020): 5–7. http://dx.doi.org/10.1109/mcg.2020.2995535.

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15

Whiten, Andrew. "Ape mind, monkey mind." Evolutionary Anthropology: Issues, News, and Reviews 5, no. 1 (1996): 3–4. http://dx.doi.org/10.1002/(sici)1520-6505(1996)5:1<3::aid-evan2>3.0.co;2-l.

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16

Wurm, Moritz F., D. Yves von Cramon, and Ricarda I. Schubotz. "Do we mind other minds when we mind other minds' actions? A functional magnetic resonance imaging study." Human Brain Mapping 32, no. 12 (January 21, 2011): 2141–50. http://dx.doi.org/10.1002/hbm.21176.

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17

Corona. "The Triune Brain: Limbic Mind Mind Plastic, Emotional Mind." American Medical Journal 2, no. 1 (January 1, 2011): 51–53. http://dx.doi.org/10.3844/amjsp.2011.51.53.

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18

Zhou, Huaijin, Ryan Schulze, Sandra Cox, Cristian Saez, Zonglin Hu, and Joe Lutkenhaus. "Analysis of MinD Mutations Reveals Residues Required for MinE Stimulation of the MinD ATPase and Residues Required for MinC Interaction." Journal of Bacteriology 187, no. 2 (January 15, 2005): 629–38. http://dx.doi.org/10.1128/jb.187.2.629-638.2005.

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ABSTRACT The MinD ATPase is critical to the oscillation of the Min proteins, which limits formation of the Z ring to midcell. In the presence of ATP, MinD binds to the membrane and recruits MinC, forming a complex that can destabilize the cytokinetic Z ring. MinE, which is also recruited to the membrane by MinD, displaces MinC and stimulates the MinD ATPase, resulting in the oscillation of the Min proteins. In this study we have investigated the role of lysine 11, present in the deviant Walker A motif of MinD, and the three residues in helix 7 (E146, S148, and D152) that interact electrostatically with lysine 11. Lysine 11 is required for interaction of MinD with the membrane, MinC, MinE, and itself. In contrast, the three residues in helix 7 that interact with lysine 11 are not required for binding to the membrane or activation of MinC. They are also not required for MinE binding; however, they are required for MinE to stimulate the MinD ATPase. Interestingly, the D152A mutant self-interacts, binds to the membrane, and recruits MinC and MinE in the presence of ADP as well as ATP. This mutant provides evidence that dimerization of MinD is sufficient for MinD to bind the membrane and recruit its partners.

19

Huang, Haiyan, Ping Wang, Li Bian, Masaki Osawa, Harold P. Erickson, and Yaodong Chen. "The cell division protein MinD fromPseudomonas aeruginosadominates the assembly of the MinC–MinD copolymers." Journal of Biological Chemistry 293, no. 20 (April 2, 2018): 7786–95. http://dx.doi.org/10.1074/jbc.ra117.001513.

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20

Schwitzgebel, Eric. "Against the mind package view of minds: Comments on Carrie Figdor's Pieces of mind." Mind & Language 35, no. 5 (November 2020): 671–76. http://dx.doi.org/10.1111/mila.12288.

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21

Notsu, Sota. "Employee's minds that promote creativity: Comparison of “mind to organization” and “mind to job”." Japanese Journal of Administrative Science 34, no. 3 (2023): 95–110. http://dx.doi.org/10.5651/jaas.34.95.

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22

Stockwell, Peter. "Mind-modelling literary personas." Journal of Literary Semantics 51, no. 2 (September 29, 2022): 131–46. http://dx.doi.org/10.1515/jls-2022-2056.

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Abstract This article takes its cue from David Miall’s influential 2011 paper, ‘Enacting the other: towards an aesthetics of feeling in literary reading’, in Elisabeth Schellekens and Peter Goldie (eds) The Aesthetic Mind: Philosophy and Psychology, Oxford: Oxford University Press, pp. 285–298. There, Miall considers the workings of readerly empathy with fictional people. He draws on work from philosophy, psychology, cognitive poetics, and both empirical and textual analysis to explore the complexities of how real readerly minds interact with fictional minds and the minds of real but remote authors. In this article, I revisit these arguments with the benefit of recent insights into the cognition of fictional minds. The key mechanism underlying characterisation, empathy, hostility, and engagement, I argue, is mind-modelling. With its origins in Theory of Mind, but extrapolated far from that simple phenomenon, mind-modelling captures the aesthetic and ethical relationships between minds both fictional and natural. I consider literary reading as a broader ecosystem: the reading mind as being embodied, enacted, and extended to include the imagined authorial mind. In recognition of Miall’s literary critical work, I will present a particular example from the poem ‘Ode on a Grecian Urn’ by John Keats – not only for the analytical demonstration but also in order to show the echoes between Romantic notions of holistic engagement with nature and recent work in cognition and literature. The analysis suggests a solution to a literary critical debate around its ending. An approach situated in mind-modelling offers a principled exploration of both fictional, poetic minds as well as authorial positioning.

23

Zimmer, C. "COGNITION: How the Mind Reads Other Minds." Science 300, no. 5622 (May 16, 2003): 1079–80. http://dx.doi.org/10.1126/science.300.5622.1079.

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24

Barrett, Justin L. "From theory of mind to divine minds." Trends in Cognitive Sciences 15, no. 6 (June 2011): 244–45. http://dx.doi.org/10.1016/j.tics.2011.03.008.

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25

Saka, Paul. "Mind and paradox: paradoxes depend on minds." Journal of Experimental & Theoretical Artificial Intelligence 25, no. 3 (September 2013): 377–87. http://dx.doi.org/10.1080/0952813x.2013.783152.

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26

Terada, Kazunori. "Social Mind and Mechanical Mind." Journal of the Robotics Society of Japan 31, no. 9 (2013): 846–49. http://dx.doi.org/10.7210/jrsj.31.846.

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27

Filson, Gerald. "Mind." Journal of Bahá’í Studies 32, no. 3-4 (July 4, 2023): 9–53. http://dx.doi.org/10.31581/jbs-32.3-4.337(2022).

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This paper correlates Bahá’í concepts of the mind with insights from philosophy. It presents arguments from both sources for a non-reductive understanding of the human mind and argues that, although science can help us advance our understanding of the mind, it is not sufficient in this pursuit, as it cannot capture fully how the human mind experiences reality. The paper reviews the mind’s conceptual way of knowing, explores the implications of language for philosophy of mind, and considers how the pursuit of science and the phenomenon of religion both shed light on the capacities and nature of the mind. After suggesting that the process of learning in which the global Bahá’í community has embarked may serve as a model for engaging the human mind in a collective enterprise for the betterment of the world, it turns back to philosophy to submit that, while many contemporary philosophers persuasively argue that the human mind is not reducible to physical causality, the philosophical resistance to a spiritual dimension of the human mind is excessively limiting. The minds of human beings demonstrate capacities that lie beyond nature, and a conception of the mind as “the power of the human spirit” or “rational soul” can not only be a fruitful way of understanding the mind, but lead to an orientation by human beings in the world, demonstrated through the learning process discussed earlier in the paper, that holds promise for the future of humanity.

28

Cusack, Paul T. E. "Mind, Body, and Soul." Journal of Clinical Case Reports and Studies 1, no. 4 (September 8, 2020): 01–11. http://dx.doi.org/10.31579/2690-8808/028.

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In this paper we uses AT Math and electrical engineering equations to prove that the mind, body and soul evolved to match up with the universal signal. Questions as to whether there is a creator or not is mentioned as well as the nature of consciousness.

29

Johnson, Jay E., Laura L. Lackner, Cynthia A. Hale, and Piet A. J. de Boer. "ZipA Is Required for Targeting of DMinC/DicB, but Not DMinC/MinD, Complexes to Septal Ring Assemblies in Escherichia coli." Journal of Bacteriology 186, no. 8 (April 15, 2004): 2418–29. http://dx.doi.org/10.1128/jb.186.8.2418-2429.2004.

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ABSTRACT The MinC division inhibitor is required for accurate placement of the septal ring at the middle of the Escherichia coli cell. The N-terminal domain of MinC (ZMinC) interferes with FtsZ assembly, while the C-terminal domain (DMinC) mediates both dimerization and complex formation with either MinD or DicB. Binding to either of these activators greatly enhances the division-inhibitory activity of MinC in the cell. The MinD ATPase plays a crucial role in the rapid pole-to-pole oscillation of MinC that is proposed to force FtsZ ring formation to midcell. DicB is encoded by one of the cryptic prophages on the E. coli chromosome (Qin) and is normally not synthesized. Binding of MinD or DicB to DMinC produces complexes that have high affinities for one or more septal ring-associated targets. Here we show that the FtsZ-binding protein ZipA is required for both recruitment of the DMinC/DicB complex to FtsZ rings and the DicB-inducible division block normally seen in MinC+ cells. In contrast, none of the known FtsZ-associated factors, including ZipA, FtsA, and ZapA, appear to be specifically required for targeting of the DMinC/MinD complex to rings, implying that the two MinC/activator complexes must recognize distinct features of FtsZ assemblies. MinD-dependent targeting of MinC may occur in two steps of increasing topological specificity: (i) recruitment of MinC from the cytoplasm to the membrane, and (ii) specific targeting of the MinC/MinD complex to nascent septal ring assemblies on the membrane. Using membrane-tethered derivatives of MinC, we obtained evidence that both of these steps contribute to the efficiency of MinC/MinD-mediated division inhibition.

30

Pengelly, Theresa. "Mind." Nursing Children and Young People 29, no. 8 (October 10, 2017): 15. http://dx.doi.org/10.7748/ncyp.29.8.15.s17.

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31

Reck, Andrew J. "Mind." International Studies in Philosophy 19, no. 1 (1987): 87–89. http://dx.doi.org/10.5840/intstudphil198719129.

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32

Dopson, Laurence. "Mind." Nursing Standard 26, no. 14 (December 7, 2011): 30. http://dx.doi.org/10.7748/ns2011.12.26.14.30.p7195.

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33

Foulkes, S. H. "`Mind'." Group Analysis 36, no. 3 (September 2003): 315–21. http://dx.doi.org/10.1177/05333164030363001.

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34

Sullivan, Erin. "Mind." Lancet 375, no. 9721 (April 2010): 1155. http://dx.doi.org/10.1016/s0140-6736(10)60501-6.

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35

Wardrop, Daneen. "mind." Ploughshares 45, no. 4 (2020): 154. http://dx.doi.org/10.1353/plo.2020.0014.

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36

Halberstadt, Carol Snyder. "Mind." JAMA 313, no. 22 (June 9, 2015): 2288. http://dx.doi.org/10.1001/jama.2015.5722.

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37

Holloway, Jack. "Mind." Trends in Urology & Men's Health 2, no. 6 (November 2011): 41. http://dx.doi.org/10.1002/tre.235.

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38

Shapiro, Larry. "Adapted Minds." Canadian Journal of Philosophy Supplementary Volume 27 (2001): 85–101. http://dx.doi.org/10.1080/00455091.2001.10715997.

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Minds are obscure things. This is especially obvious and especially onerous to those interested in understanding the mind. One way to begin an investigation of mind, given its abstruseness, is to explore the implications of something we believe must be true of minds. This is the approach I take in this paper. Whatever uncertainties we have about the mind, it's a safe bet that the mind is an adaptation. So, I begin with this truth about minds: minds are the product of evolution by natural selection. In what follows, I trace some of the consequences of this fact. Doing so will take us some distance toward answering a variety of questions about the mind.In exploring the consequences of the mind's origin I will speak of the mind generally. While I grant that this adds an element of vagueness to the project at hand, it does not in any way cast doubt on the conclusions I draw. This is so because the inferences I make about minds follow not from any assumptions about the nature of mind but are derived purely from the nature of adaptation.

39

Petrova, Ekaterina Evgenievna, and Elena Sergeevna Solntseva. "Special aspects of representation of the MIND concept in C. Wilson’s novel “The Mind Parasites”." Philology. Issues of Theory and Practice 16, no. 11 (November 24, 2023): 3981–86. http://dx.doi.org/10.30853/phil20230607.

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The aim of the research is to identify the individual author’s features of the linguistic representation and semantic content of the MIND concept in the science fiction novel “The Mind Parasites” by the British writer C. Wilson. The scientific originality lies in the fact that the MIND concept in this work has become the subject of a special study for the first time, which made it possible to identify its content structure and ways of representation. Based on conceptual, descriptive-analytical methods and quantitative analysis, the main semantic features of the artistic concept under study and the means of its verbalization are being identified; the types of metaphors characteristic of C. Wilson’s texts representing the figurative layer of the concept are being highlighted. As a result of the research, it was found that the artistic concept of MIND differs significantly from the corresponding linguistic one, which is connected with the main idea of the novel about the limitless possibilities of the human mind. The concept under study is most often verbalized through multi-component individual-author figurative constructions – phrases, syntagmas, sentences and superphrasal unities containing metaphors and figurative comparisons.

40

Noble, Christopher. "Mindsets, mind sets and mind sense." Prometheus 33, no. 4 (October 2, 2015): 411–20. http://dx.doi.org/10.1080/08109028.2016.1199379.

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41

Strauss, Claudia. "The Literary Mind.:The Literary Mind." Journal of Linguistic Anthropology 7, no. 2 (December 1997): 235–36. http://dx.doi.org/10.1525/jlin.1997.7.2.235.

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42

O'Sullivan, Michael. "Designing with the mind in mind." ACM SIGSOFT Software Engineering Notes 36, no. 5 (September 30, 2011): 52. http://dx.doi.org/10.1145/2020976.2021005.

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43

Fingelkurts, Andrew A., Alexander A. Fingelkurts, and Carlos F. H. Neves. "Mind the physics: Physics of mind." Physics of Life Reviews 25 (August 2018): 75–77. http://dx.doi.org/10.1016/j.plrev.2018.01.012.

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44

Dragos, Chris. "Changing your mind, closing your mind." Metascience 28, no. 1 (August 21, 2018): 33–35. http://dx.doi.org/10.1007/s11016-018-0350-y.

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45

Tollefsen, Deborah Perron. "From extended mind to collective mind." Cognitive Systems Research 7, no. 2-3 (June 2006): 140–50. http://dx.doi.org/10.1016/j.cogsys.2006.01.001.

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46

Kwan, Irene, Joseph Fong, Fion Chan, and Jim Ngan. "Web-based mind learning system using mind mapping and mind scheduling." International Journal of Information and Operations Management Education 1, no. 1 (2005): 100. http://dx.doi.org/10.1504/ijiome.2005.007443.

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Juarez, Jennifer R., and William Margolin. "Changes in the Min Oscillation Pattern before and after Cell Birth." Journal of Bacteriology 192, no. 16 (June 11, 2010): 4134–42. http://dx.doi.org/10.1128/jb.00364-10.

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ABSTRACT The Min system regulates the positioning of the cell division site in many bacteria. In Escherichia coli, MinD migrates rapidly from one cell pole to the other. In conjunction with MinC, MinD helps to prevent unwanted FtsZ rings from assembling at the poles and to stabilize their positioning at midcell. Using time-lapse microscopy of growing and dividing cells expressing a gfp-minD fusion, we show that green fluorescent protein (GFP)-MinD often paused at midcell in addition to at the poles, and the frequency of midcell pausing increased as cells grew longer and cell division approached. At later stages of septum formation, GFP-MinD often paused specifically on only one side of the septum, followed by migration to the other side of the septum or to a cell pole. About the time of septum closure, this irregular pattern often switched to a transient double pole-to-pole oscillation in the daughter cells, which ultimately became a stable double oscillation. The splitting of a single MinD zone into two depends on the developing septum and is a potential mechanism to explain how MinD is distributed equitably to both daughter cells. Septal pausing of GFP-MinD did not require MinC, suggesting that MinC-FtsZ interactions do not drive MinD-septal interactions, and instead MinD recognizes a specific geometric, lipid, and/or protein target at the developing septum. Finally, we observed regular end-to-end oscillation over very short distances along the long axes of minicells, supporting the importance of geometry in MinD localization.

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Ebdon, Susan Austin, Mary McGee Coakley, and Danielle Legnard. "Mathematical Mind Journeys: Awakening Minds to Computational Fluency." Teaching Children Mathematics 9, no. 8 (April 2003): 486–87. http://dx.doi.org/10.5951/tcm.9.8.0486.

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Have you ever wondered what your students are really thinking as they do mathematics? Do you wish that you could stimulate and excite your students while building the fundamental skills necessary for their future? Join us as we take our students on a Mathematical Mind Journey. This learning adventure does not require time-intensive planning or expensive props and materials. Mathematical Mind Journeys are “think aloud” strategies that demystify computation. Students use metacognition to explain the paths that their brains take when solving a problem and rely on mathematical memory rather than memorization. Whether you have a few minutes or a class period, a Mathematical Mind Journey will empower and engage every student in your class.

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Gunderson, Keith. "What neuron doctrines might never explain." Behavioral and Brain Sciences 22, no. 5 (October 1999): 837–38. http://dx.doi.org/10.1017/s0140525x99302193.

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My focus is on the inability of neuron doctrines to provide an explanatory context for aspects of consciousness that give rise to the mind–body and other minds problem(s). Neuroscience and related psychological sciences may be viewed as richly contributing to our taxonomic understanding of the mind and conditions underlying consciousness, without illuminating mind–body and other minds perplexities.

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Raskin, David M., and Piet A. J. de Boer. "MinDE-Dependent Pole-to-Pole Oscillation of Division Inhibitor MinC in Escherichia coli." Journal of Bacteriology 181, no. 20 (October 15, 1999): 6419–24. http://dx.doi.org/10.1128/jb.181.20.6419-6424.1999.

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ABSTRACT By inhibiting FtsZ ring formation near the cell ends, the MinC protein plays a critical role in proper positioning of the division apparatus in Escherichia coli. MinC activity requires that of MinD, and the MinE peptide provides topological specificity by suppressing MinC-MinD-mediated division inhibition specifically at the middle of the cell. We recently presented evidence that MinE not only accumulates in an FtsZ-independent ring structure at the cell’s middle but also imposes a unique dynamic localization pattern upon MinD in which the latter accumulates alternately in either one of the cell halves in what appears to be a rapidly oscillating membrane association-dissociation cycle. Here we show that functional green fluorescent protein-MinC displays a very similar oscillatory behavior which is dependent on both MinD and MinE and independent of FtsZ. The results support a model in which MinD recruits MinC to its site of action and in which FtsZ ring assembly at each of the cell ends is blocked in an intermittent and alternate fashion.