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Relevant bibliographies by topics / LIM domains

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Journal articles

Academic literature on the topic 'LIM domains'

Author: Grafiati

Published: 20 February 2023

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Journal articles on the topic "LIM domains"

1

Matthews, Jacqueline M., Mugdha Bhati, Vanessa J. Craig, et al. "Competition between LIM-binding domains." Biochemical Society Transactions 36, no. 6 (2008): 1393–97. http://dx.doi.org/10.1042/bst0361393.

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LMO (LIM-only) and LIM-HD (LIM-homeodomain) proteins form a family of proteins that is required for myriad developmental processes and which can contribute to diseases such as T-cell leukaemia and breast cancer. The four LMO and 12 LIM-HD proteins in mammals are expressed in a combinatorial manner in many cell types, forming a transcriptional ‘LIM code’. The proteins all contain a pair of closely spaced LIM domains near their N-termini that mediate protein–protein interactions, including binding to the ∼30-residue LID (LIM interaction domain) of the essential co-factor protein Ldb1 (LIM domain

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2

RABBITTS, T. H., and T. BOEHM. "LIM domains." Nature 346, no. 6283 (1990): 418. http://dx.doi.org/10.1038/346418a0.

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3

El Omari, Kamel, Sarah J. Hoosdally, Kapil Tuladhar, et al. "Structure of the leukemia oncogene LMO2: implications for the assembly of a hematopoietic transcription factor complex." Blood 117, no. 7 (2011): 2146–56. http://dx.doi.org/10.1182/blood-2010-07-293357.

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Abstract The LIM only protein 2 (LMO2) is a key regulator of hematopoietic stem cell development whose ectopic expression in T cells leads to the onset of acute lymphoblastic leukemia. Through its LIM domains, LMO2 is thought to function as the scaffold for a DNA-binding transcription regulator complex, including the basic helix-loop-helix proteins SCL/TAL1 and E47, the zinc finger protein GATA-1, and LIM-domain interacting protein LDB1. To understand the role of LMO2 in the formation of this complex and ultimately to dissect its function in normal and aberrant hematopoiesis, we solved the cry

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4

Breen, Joseph J., Alan D. Agulnick, Heiner Westphal, and Igor B. Dawid. "Interactions between LIM Domains and the LIM Domain-binding Protein Ldb1." Journal of Biological Chemistry 273, no. 8 (1998): 4712–17. http://dx.doi.org/10.1074/jbc.273.8.4712.

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5

SCHMEICHEL, Karen L., and Mary C. BECKERLE. "LIM domains of cysteine-rich protein 1 (CRP1) are essential for its zyxin-binding function." Biochemical Journal 331, no. 3 (1998): 885–92. http://dx.doi.org/10.1042/bj3310885.

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Previous studies have demonstrated that the adhesion-plaque protein, zyxin, interacts specifically with a 23 kDa protein, called the cysteine-rich protein 1 (CRP1), which has been implicated in myogenesis. Primary sequence analyses have revealed that both zyxin and CRP1 exhibit multiple copies of a structural motif called the LIM domain. LIM domains, which are defined by the consensus CX2CX16–23HX2CX2CX2CX16–23CX2–3(C,H,D), are found in a variety of proteins that are involved in cell growth and differentiation. Recent studies have established that LIM domains are zinc-binding structures that m

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6

Jurata, L. W., and G. N. Gill. "Functional analysis of the nuclear LIM domain interactor NLI." Molecular and Cellular Biology 17, no. 10 (1997): 5688–98. http://dx.doi.org/10.1128/mcb.17.10.5688.

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LIM homeodomain and LIM-only (LMO) transcription factors contain two tandemly arranged Zn2+-binding LIM domains capable of mediating protein-protein interactions. These factors have restricted patterns of expression, are found in invertebrates as well as vertebrates, and are required for cell type specification in a variety of developing tissues. A recently identified, widely expressed protein, NLI, binds with high affinity to the LIM domains of LIM homeodomain and LMO proteins in vitro and in vivo. In this study, a 38-amino-acid fragment of NLI was found to be sufficient for the association o

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7

Winkelman, Jonathan D., Caitlin A. Anderson, Cristian Suarez, David R. Kovar, and Margaret L. Gardel. "Evolutionarily diverse LIM domain-containing proteins bind stressed actin filaments through a conserved mechanism." Proceedings of the National Academy of Sciences 117, no. 41 (2020): 25532–42. http://dx.doi.org/10.1073/pnas.2004656117.

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The actin cytoskeleton assembles into diverse load-bearing networks, including stress fibers (SFs), muscle sarcomeres, and the cytokinetic ring to both generate and sense mechanical forces. The LIM (Lin11, Isl- 1, and Mec-3) domain family is functionally diverse, but most members can associate with the actin cytoskeleton with apparent force sensitivity. Zyxin rapidly localizes via its LIM domains to failing SFs in cells, known as strain sites, to initiate SF repair and maintain mechanical homeostasis. The mechanism by which these LIM domains associate with stress fiber strain sites (SFSS) is n

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8

O'Keefe, D. D., S. Thor, and J. B. Thomas. "Function and specificity of LIM domains in Drosophila nervous system and wing development." Development 125, no. 19 (1998): 3915–23. http://dx.doi.org/10.1242/dev.125.19.3915.

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LIM domains are found in a variety of proteins, including cytoplasmic and nuclear LIM-only proteins, LIM-homeodomain (LIM-HD) transcription factors and LIM-kinases. Although the ability of LIM domains to interact with other proteins has been clearly established in vitro and in cultured cells, their in vivo function is unknown. Here we use Drosophila to test the roles of the LIM domains of the LIM-HD family member Apterous (Ap) in wing and nervous system development. Using a rescuing assay of the ap mutant phenotype, we have found that the LIM domains are essential for Ap function. Furthermore,

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9

Thomas, Clément, Flora Moreau, Monika Dieterle, et al. "The LIM Domains of WLIM1 Define a New Class of Actin Bundling Modules." Journal of Biological Chemistry 282, no. 46 (2007): 33599–608. http://dx.doi.org/10.1074/jbc.m703691200.

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Actin filament bundling, i.e. the formation of actin cables, is an important process that relies on proteins able to directly bind and cross-link subunits of adjacent actin filaments. Animal cysteine-rich proteins and their plant counterparts are two LIM domain-containing proteins that were recently suggested to define a new family of actin cytoskeleton regulators involved in actin filament bundling. We here identified the LIM domains as responsible for F-actin binding and bundling activities of the tobacco WLIM1. The deletion of one of the two LIM domains reduced significantly, but did not en

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10

NAGATA, Kyoko, Kazumasa OHASHI, Neng YANG, and Kensaku MIZUNO. "The N-terminal LIM domain negatively regulates the kinase activity ofLIM-kinase 1." Biochemical Journal 343, no. 1 (1999): 99–105. http://dx.doi.org/10.1042/bj3430099.

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LIM-kinase 1 (LIMK1, where LIM is an acronym of the three gene products Lin-11, Isl-1 and Mec-3) is a serine/threonine kinase that phosphorylates cofilin and regulates actin cytoskeletal reorganization. LIMK1 contains two LIM domains and a PDZ (an acronym of the three proteins PSD-95, Dlg and ZO-1) domain in the N-terminal half and a kinase domain in the C-terminal half. In this study we examined the role of the extra-catalytic region in the regulation of kinase activity of LIMK1. Limited proteolysis of LIMK1 resulted in the production of the 35-40-kDa kinase core fragments with 3.5-5.5-fold i

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