Relevant bibliographies by topics / LIM Protein

Academic literature on the topic 'LIM Protein'

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Published: 6 September 2023

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Journal articles on the topic "LIM Protein"

1

Matthews, Jacqueline M., Mugdha Bhati, Vanessa J. Craig, Janet E. Deane, Cy Jeffries, Christopher Lee, Amy L. Nancarrow, Daniel P. Ryan, and Margaret Sunde. "Competition between LIM-binding domains." Biochemical Society Transactions 36, no. 6 (November 19, 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-binding protein 1). In an attempt to understand the molecular mechanisms behind the LIM code, we have determined the molecular basis of binding of LMO and LIM-HD proteins for Ldb1LID through a series of structural, mutagenic and biophysical studies. These studies provide an explanation for why Ldb1 binds the LIM domains of the LMO/LIM-HD family, but not LIM domains from other proteins. The LMO/LIM-HD family exhibit a range of affinities for Ldb1, which influences the formation of specific functional complexes within cells. We have also identified an additional LIM interaction domain in one of the LIM-HD proteins, Isl1. Despite low sequence similarity to Ldb1LID, this domain binds another LIM-HD protein, Lhx3, in an identical manner to Ldb1LID. Through our and other studies, it is emerging that the multiple layers of competitive binding involving LMO and LIM-HD proteins and their partner proteins contribute significantly to cell fate specification and development.
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El Omari, Kamel, Sarah J. Hoosdally, Kapil Tuladhar, Dimple Karia, Paresh Vyas, Roger Patient, Catherine Porcher, and Erika J. Mancini. "Structure of the leukemia oncogene LMO2: implications for the assembly of a hematopoietic transcription factor complex." Blood 117, no. 7 (February 17, 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 crystal structure of LMO2 in complex with the LID domain of LDB1 at 2.4 Å resolution. We observe a largely unstructured LMO2 kept in register by the LID binding both LIM domains. Comparison of independently determined crystal structures of LMO2 reveals large movements around a conserved hinge between the LIM domains. We demonstrate that such conformational flexibility is necessary for binding of LMO2 to its partner protein SCL/TAL1 in vitro and for the function of this complex in vivo. These results, together with molecular docking and analysis of evolutionarily conserved residues, yield the first structural model of the DNA-binding complex containing LMO2, LDB1, SCL/TAL1, and GATA-1.
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Robertson, Neil O., Ngaio C. Smith, Athina Manakas, Mahiar Mahjoub, Gordon McDonald, Ann H. Kwan, and Jacqueline M. Matthews. "Disparate binding kinetics by an intrinsically disordered domain enables temporal regulation of transcriptional complex formation." Proceedings of the National Academy of Sciences 115, no. 18 (April 16, 2018): 4643–48. http://dx.doi.org/10.1073/pnas.1714646115.

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Intrinsically disordered regions are highly represented among mammalian transcription factors, where they often contribute to the formation of multiprotein complexes that regulate gene expression. An example of this occurs with LIM-homeodomain (LIM-HD) proteins in the developing spinal cord. The LIM-HD protein LHX3 and the LIM-HD cofactor LDB1 form a binary complex that gives rise to interneurons, whereas in adjacent cell populations, LHX3 and LDB1 form a rearranged ternary complex with the LIM-HD protein ISL1, resulting in motor neurons. The protein–protein interactions within these complexes are mediated by ordered LIM domains in the LIM-HD proteins and intrinsically disordered LIM interaction domains (LIDs) in LDB1 and ISL1; however, little is known about how the strength or rates of binding contribute to complex assemblies. We have measured the interactions of LIM:LID complexes using FRET-based protein–protein interaction studies and EMSAs and used these data to model population distributions of complexes. The protein–protein interactions within the ternary complexes are much weaker than those in the binary complex, yet surprisingly slow LDB1:ISL1 dissociation kinetics and a substantial increase in DNA binding affinity promote formation of the ternary complex over the binary complex in motor neurons. We have used mutational and protein engineering approaches to show that allostery and modular binding by tandem LIM domains contribute to the LDB1LID binding kinetics. The data indicate that a single intrinsically disordered region can achieve highly disparate binding kinetics, which may provide a mechanism to regulate the timing of transcriptional complex assembly.
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Cai, Ying, Zhixiong Xu, Lalitha Nagarajan, and Stephen J. Brandt. "Single-Stranded DNA-Binding Proteins (SSBPs) Regulate the Abundance of the LIM-Homeodomain Protein LHX2 and Augment Its Transcriptional Activity." Blood 110, no. 11 (November 16, 2007): 1239. http://dx.doi.org/10.1182/blood.v110.11.1239.1239.

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Abstract A small family of proteins with putative single-stranded DNA-binding activity has been shown to augment the biological actions of LIM-homeodomain (LIM-HD) transcription factors through the mediation of the LIM domain-binding protein LDB1. We recently established that two of these SSBPs, Ssbp2 and Ssbp3, were components of an E-box-GATA DNA-binding complex in murine erythroid progenitors containing transcription factors Tal1, E2A, and Gata-1 and LIM-only protein Lmo2 and showed that Ssbp2 stimulated E box-GATA DNA-binding activity by inhibiting Ldb1 ubiquitination and Ldb1 and Lmo2 turnover (Genes & Dev.21:942–955, 2007). Since LIM-HD proteins are substrates of different E3 ubiquitin ligases than LIM-only proteins and have the additional property of binding DNA, we sought to determine the effect of SSBPs on LIM-HD expression and function. Using the prototype LIM-HD protein Lhx2 and one of its best-characterized target genes, Cga, for analysis, we found that an Ssbp3-, Ldb1-, and Lhx2-containing complex associated with an Lhx2 binding element in the Cga promoter in vitro and in mouse pituitary cells (alphaT3-1 cell line) in vivo. We then showed that enforced expression of Ssbp2 and Ssbp3 in alphaT3-1 cells increased Lhx2 and Ldb1 protein abundance, Lhx2 DNA-binding activity, and Cga expression and augmented Lhx2 transcriptional activity in an Ldb1-dependent fashion. While Lhx2-Ldb1-Ssbp3 DNA-binding activity increased in Ssbp3- relative to vector-transfected cells, the affinity of this complex for DNA was unaltered. Similar to the effect of Ssbp2 on Lmo2 in murine erythroleukemia (MEL) cells, overexpressed Ssbp3 reduced Lhx2 protein turnover in cycloheximide-treated alphaT3-1 cells without affecting Lhx2 RNA levels. In contrast, knockdown of endogenous Ssbp3, but not Ssbp2 which is expressed at much lower levels in these cells, reduced Lhx2 and Ldb1 abundance, Lhx2 DNA-binding activity, Lhx2, Ldb1, and Ssbp3 loading onto the Cga promoter, Cga promoter activity, and endogenous Cga gene expression. Significantly, neither overexpression nor knockdown of Ssbp2 in MEL cells, which express both the LIM-only protein Lmo2 and LIM-HD protein Lhx2, affected Lhx2 protein abundance, and Lhx2 DNA-binding activity was undetectable in nuclear extracts from these cells despite the presence of immunoreactive Lhx2. These studies indicate that SSBP augmentation of LIM-HD function results from Ldb1-mediated inhibition of LIM-HD protein turnover and increased assembly of a LIM-HD/LDB1/SSBP DNA-binding complex. The much greater affinity for LDB1 of LIM-only compared to LIM-HD proteins is likely a major determinant of the SSBP effect on LIM-HD protein abundance. Finally, these findings are consistent with cell type-specific contributions of different SSBPs, even for similar LDB1-dependent actions.
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Jurata, L. W., and G. N. Gill. "Functional analysis of the nuclear LIM domain interactor NLI." Molecular and Cellular Biology 17, no. 10 (October 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 of NLI with nuclear LIM domains. In addition, NLI was shown to form high affinity homodimers through the amino-terminal 200 amino acids, but dimerization of NLI was not required for association with the LIM homeodomain protein Lmxl. Chemical cross-linking analysis revealed higher-order complexes containing multiple NLI molecules bound to Lmx1, indicating that dimerization of NLI does not interfere with LIM domain interactions. Additionally, NLI formed complexes with Lmx1 on the rat insulin I promoter and inhibited the LIM domain-dependent synergistic transcriptional activation by Lmx1 and the basic helix-loop-helix protein E47 from the rat insulin I minienhancer. These studies indicate that NLI contains at least two functionally independent domains and may serve as a negative regulator of synergistic transcriptional responses which require direct interaction via LIM domains. Thus, NLI may regulate the transcriptional activity of LIM homeodomain proteins by determining specific partner interactions.
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Goyal, Rakesh K., Phoebe Lin, Josna Kanungo, Aimee S. Payne, Anthony J. Muslin, and Gregory D. Longmore. "Ajuba, a Novel LIM Protein, Interacts with Grb2, Augments Mitogen-Activated Protein Kinase Activity in Fibroblasts, and Promotes Meiotic Maturation of Xenopus Oocytes in a Grb2- and Ras-Dependent Manner." Molecular and Cellular Biology 19, no. 6 (June 1, 1999): 4379–89. http://dx.doi.org/10.1128/mcb.19.6.4379.

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ABSTRACT LIM domain-containing proteins contribute to cell fate determination, the regulation of cell proliferation and differentiation, and remodeling of the cell cytoskeleton. These proteins can be found in the cell nucleus, cytoplasm, or both. Whether and how cytoplasmic LIM proteins contribute to the cellular response to extracellular stimuli is an area of active investigation. We have identified and characterized a new LIM protein, Ajuba. Although predominantly a cytosolic protein, in contrast to other like proteins, it did not localize to sites of cellular adhesion to extracellular matrix or interact with the actin cytoskeleton. Removal of the pre-LIM domain of Ajuba, including a putative nuclear export signal, led to an accumulation of the LIM domains in the cell nucleus. The pre-LIM domain contains two putative proline-rich SH3 recognition motifs. Ajuba specifically associated with Grb2 in vitro and in vivo. The interaction between these proteins was mediated by either SH3 domain of Grb2 and the N-terminal proline-rich pre-LIM domain of Ajuba. In fibroblasts expressing Ajuba mitogen-activated protein kinase activity persisted despite serum starvation and upon serum stimulation generated levels fivefold higher than that seen in control cells. Finally, when Ajuba was expressed in fully developed Xenopus oocytes, it promoted meiotic maturation in a Grb2- and Ras-dependent manner.
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Guy, Pamela M., Daryn A. Kenny, and Gordon N. Gill. "The PDZ Domain of the LIM Protein Enigma Binds to β-Tropomyosin." Molecular Biology of the Cell 10, no. 6 (June 1999): 1973–84. http://dx.doi.org/10.1091/mbc.10.6.1973.

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PDZ and LIM domains are modular protein interaction motifs present in proteins with diverse functions. Enigma is representative of a family of proteins composed of a series of conserved PDZ and LIM domains. The LIM domains of Enigma and its most related family member, Enigma homology protein, bind to protein kinases, whereas the PDZ domains of Enigma and family member actin-associated LIM protein bind to actin filaments. Enigma localizes to actin filaments in fibroblasts via its PDZ domain, and actin-associated LIM protein binds to and colocalizes with the actin-binding protein α-actinin-2 at Z lines in skeletal muscle. We show that Enigma is present at the Z line in skeletal muscle and that the PDZ domain of Enigma binds to a skeletal muscle target, the actin-binding protein tropomyosin (skeletal β-TM). The interaction between Enigma and skeletal β-TM was specific for the PDZ domain of Enigma, was abolished by mutations in the PDZ domain, and required the PDZ-binding consensus sequence (Thr-Ser-Leu) at the extreme carboxyl terminus of skeletal β-TM. Enigma interacted with isoforms of tropomyosin expressed in C2C12 myotubes and formed an immunoprecipitable complex with skeletal β-TM in transfected cells. The association of Enigma with skeletal β-TM suggests a role for Enigma as an adapter protein that directs LIM-binding proteins to actin filaments of muscle cells.
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Johnson, J. D., W. Zhang, A. Rudnick, W. J. Rutter, and M. S. German. "Transcriptional synergy between LIM-homeodomain proteins and basic helix-loop-helix proteins: the LIM2 domain determines specificity." Molecular and Cellular Biology 17, no. 7 (July 1997): 3488–96. http://dx.doi.org/10.1128/mcb.17.7.3488.

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LIM-homeodomain proteins direct cellular differentiation by activating transcription of cell-type-specific genes, but this activation requires cooperation with other nuclear factors. The LIM-homeodomain protein Lmx1 cooperates with the basic helix-loop-helix (bHLH) protein E47/Pan-1 to activate the insulin promoter in transfected fibroblasts. In this study, we show that two proteins originally called Lmx1 are the closely related products of two distinct vertebrate genes, Lmx1.1 and Lmx1.2. We have used yeast genetic systems to delineate the functional domains of the Lmx1 proteins and to characterize the physical interactions between Lmx1 proteins and E47/Pan-1 that produce synergistic transcriptional activation. The LIM domains of the Lmx1 proteins, and particularly the second LIM domain, mediate both specific physical interactions and transcriptional synergy with E47/Pan-1. The LIM domains of the LIM-homeodomain protein Isl-1, which cannot mediate transcriptional synergy with E47/Pan-1, do not interact with E47/Pan-1. In vitro studies demonstrate that the Lmx1.1 LIM2 domain interacts specifically with the bHLH domain of E47/Pan-1. These studies provide the basis for a model of the assembly of LIM-homeodomain-containing complexes on DNA elements that direct cell-type-restricted transcription in differentiated tissues.
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Jo, Kiwon, Bart Rutten, Robert C. Bunn, and David S. Bredt. "Actinin-Associated LIM Protein-Deficient Mice Maintain Normal Development and Structure of Skeletal Muscle." Molecular and Cellular Biology 21, no. 5 (March 1, 2001): 1682–87. http://dx.doi.org/10.1128/mcb.21.5.1682-1687.2001.

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ABSTRACT The actinin-associated LIM protein, ALP, is the prototype of a large family of proteins containing an N-terminal PDZ domain and a C-terminal LIM domain. These PDZ-LIM proteins are components of the muscle cytoskeleton and occur along the Z lines owing to interaction of the PDZ domain with the spectrin-like repeats of α-actinin. Because PDZ and LIM domains are typically found in proteins that mediate cellular signaling, PDZ-LIM proteins are suspected to participate in muscle development. Interestingly the ALP gene occurs at 4q35 near the heterochromatic region mutated in facioscapulohumeral muscular dystrophy, indicating a possible role for ALP in this disease. Here, we describe the generation and analysis of mice lacking the ALP gene. Surprisingly, the ALP knockout mice show no gross histological abnormalities and maintain sarcolemmal integrity as determined by serum pyruvate kinase assays. The absence of a dystrophic phenotype in these mice suggests that down-regulation of ALP does not participate in facioscapulohumeral muscular dystrophy. These data suggest that ALP does not participate in muscle development or that an alternative PDZ-LIM protein can compensate for the lack of ALP.
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Rath, Nibedita, Zhishan Wang, Min Min Lu, and Edward E. Morrisey. "LMCD1/Dyxin Is a Novel Transcriptional Cofactor That Restricts GATA6 Function by Inhibiting DNA Binding." Molecular and Cellular Biology 25, no. 20 (October 15, 2005): 8864–73. http://dx.doi.org/10.1128/mcb.25.20.8864-8873.2005.

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ABSTRACT The activity of GATA factors is regulated, in part, at the level of protein-protein interactions. LIM domain proteins, first defined by the zinc finger motifs found in the Lin11, Isl-1, and Mec-3 proteins, act as coactivators of GATA function in both hematopoietic and cardiovascular tissues. We have identified a novel GATA-LIM interaction between GATA6 and LMCD1/dyxin. The LIM domains and cysteine-rich domains in LMCD1/dyxin and the carboxy-terminal zinc finger of GATA6 mediate this interaction. Expression of LMCD1/dyxin is remarkably similar to that of GATA6, with high-level expression observed in distal airway epithelium of the lung, vascular smooth muscle, and myocardium. In contrast to other GATA-LIM protein interactions, LMCD1/dyxin represses GATA6 activation of both lung and cardiac tissue-specific promoters. Electrophoretic mobility shift and chromatin immunoprecipitation assays show that LMCD1/dyxin represses GATA6 function by inhibiting GATA6 DNA binding. These data reveal an interaction between GATA6 and LMCD1/dyxin and demonstrate a novel mechanism through which LIM proteins can assert their role as transcriptional cofactors of GATA proteins.
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Dissertations / Theses on the topic "LIM Protein"

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Schwartz, Christine. "Muscle LIM protein and Nesprin-1 in Mechanotransduction." Thesis, Paris 6, 2016. http://www.theses.fr/2016PA066374/document.

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J’ai étudié trois protéines qui participent à deux vois différentes de méchano-transduction qui est la conversion des stimuli physiques en un signal biochimique.Dans une culture cellulaire en 2D, lorsque les cardiomyocytes sont étirés, MLP est transloqué vers le noyau. Sans translocation, les cellules ne parviennent pas à répondre à la stimulation. Les patients porteurs de mutations dans MLP développent une cardiomyopathie comme les souris MLP knock-out (MLP-/-). Mon objectif a été d’élucider le rôle de MLP dans ces cardiomyopathies en surexprimant des mutations de MLP dans les cardiomyocytes isolés des souris MLP-/- néonataux. Dans les cultures 2D mais pas 3D, MLP n’était pas transloqué vers le noyau après l’étirement des cellules. Bien que je n’aie pas pu résoudre ce problème, j’ai mis au point les expériences nécessaires à la poursuite de ce projet.Nesprins s’intègrent dans un complexe transmembranaire de l’enveloppe nucléaire (EN), le LINC complexe, qui connecte le cytosquelette à l’intérieur du noyau. Les myoblastes isolés des patients porteurs des mutations de Nesprin ou de Lamin, qui est associé au LINC complexe, ont présenté des noyaux déformés ainsi que des anomalies de réponses méchanosensibles : Si cultivées sur supports mous, les cellules affichaient un niveau élevé de fibres musculaires stressées et d’adhésions focales. Le knock-down de FHOD, une cible en aval de ROCK et SRC, qui également étaient actives dans ces myoblastes, a réduit ce phénotype. Bien que l’on ait émis l’hypothèse que les mutations dans Nesprins et Lamins conduisent à une instabilité mécanique de l’EN, ces résultats indiquent que les voies de signalisation par l’EN sont perturbées aussi
I studied three striated muscle proteins that are participating in two different pathways of mechanotransduction, which is the translation of a physical stimulus into a biochemical signal.When isolated cardiomyocytes are stretched in 2D, MLP shuttles to the nucleus. Without shuttling MLP, these cells fail to respond to the stretch stimulus. Human patients with MLP-mutations develop cardiomyopathies, as well as mice with a knock-out of MLP (MLP-/-). By expressing mutated MLP in neonatal cardiomyocytes of MLP-/- mice, I wanted to elucidate the role of mutant MLP. Surprisingly, MLP did shuttle after stretching of 2D but not 3D cell cultures. Although I could not solve this issue, I prepared the setup for subsequent experiments.Nesprins are part of the nuclear envelope (NE) spanning LINC complex, which connects the cytoskeleton with the nucleus. Myoblasts from patients with mutations in Nesprins or LINC-associated Lamins displayed deformed nuclei and had defects in mechanosensitive responses with an elevated level of stress fibers and focal adhesions on soft surfaces. This phenotype could be rescued by knock-down of formin FHOD1, a downstream target of ROCK and SRC, which also were highly active in the mutant cells. While mutations in Nesprins and Lamins are thought to lead to mechanical instability of the NE, these results indicate that signaling pathways through the NE are disturbed as well
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Smith, Ngaio Charlotte. "Investigating the role of protein-protein and protein-DNA interactions in the function of Isl1." Thesis, The University of Sydney, 2019. http://hdl.handle.net/2123/20655.

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LIM-homeodomain (LIM-HD) transcription factors act as key developmental regulators, through their ability to both bind DNA through homeodomain-DNA interactions, and to form larger complexes through protein-protein interactions. Many interactions that have been characterised are formed using their LIM domains, but likely also involve other regions, which have not yet been described for many LIM-HD proteins. The LIM-HD protein Isl1 has been implicated in the development of many tissues. However, relatively little detail is known about how Isl1 functions in these systems and the pathways in which it acts. The first part of this thesis aimed to identify and characterise novel binding partners for Isl1. An earlier project isolated ~180 potential binding partners through use of yeast two-hybrid mating screens; throughout this thesis further methodology was developed to identify additional proteins in a medium throughput manner. Validation protocols were then applied to determine which interactors were likely to represent biologically relevant interaction partners for Isl1. The second part of this thesis focussed on the mechanisms by which Isl1 and Lhx3 direct cell fate determination in the developing central nervous system. These proteins, along with Ldb1, interact via LIM:LID interactions to form cell-specific transcriptional complexes that target genes different to those targeted by either LIM-HD protein alone. It was not known if the homeodomains target these different sites solely because of the LIM:LID interactions or if the homeodomains themselves bind cooperatively to DNA. The DNA-binding behaviour of various iterations of the Lhx3/Isl1/Ldb1 complex are described, and structural characterisation of the Isl1/Lhx3 DNA-binding unit has been pursued. These data provide new insights into the mechanisms by which Isl1 and Lhx3 work together in regulating gene expression.
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Schwartz, Christine [Verfasser]. "Muscle LIM Protein and Nesprin-1 in Mechanotransduction / Christine Schwartz." Berlin : Freie Universität Berlin, 2017. http://d-nb.info/112815062X/34.

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Taniguchi, Yoshihito. "LIM protein KyoT2 negatively regulates transcription by association with the RBP-J DNA-binding protein." Kyoto University, 1998. http://hdl.handle.net/2433/182239.

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Diefenbacher, Markus Elmar. "The transcriptional co-activator function of the LIM-domain protein nTrip6." Eggenstein-Leopoldshafen Forschungszentrum Karlsruhe GmbH, 2010. http://d-nb.info/1002907535/34.

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Robertson, Neil. "Development and application of simple FRET-based methods for aggregation-prone LIM domain interactions." Thesis, The University of Sydney, 2017. http://hdl.handle.net/2123/16912.

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LIM-only (LMO) and LIM-homeodomain (LIM-HD) proteins are important mediators of cell specification, proliferation and differentiation. These transcription factors all contain two tandem LIM domains (LIM1+2), which are non-classical zinc finger motifs that mediate protein-protein interactions. Many co-factors of these proteins contain LIM interacting domains (LIDs). The LID is a ~30-residue intrinsically disordered region (IDR) that folds upon binding to LIM1+2 domains. LID:LIM1+2 interactions and the competition established through different combinations of different binding partners play an important role in neural development and breast cancer. The ability to estimate affinities for these interactions would help provide mechanistic insight into LMO and LIM-HD complex formation and regulation. However, the propensity of LIM1+2 domains from LMO/LIM-HD proteins to aggregate and precipitate during recombinant protein production have made it difficult to measure binding affinities for LID:LIM1+2 interactions. This thesis outlines the design, optimisation and application of a series of Förster Resonance Energy Transfer (FRET)-based approaches to study LID:LIM1+2 interactions. LIM1+2 aggregation is prevented by tethering the domains to a LID using a flexible polypeptide linker. The interacting domains are in turn fused to fluorescent proteins that are optimised for FRET. Specific proteolytic cleavage of the linker allows equilibrium binding constants and dissociation rates to be determined using homologous competition and dilution-based approaches. Through the application of these simple FRET-based binding methods, this thesis reveals previously unappreciated and unknown properties of LMO and LIM-HD proteins. This work provides tools for studying other aggregation-prone proteins, as well as general implications for the activity of transcription factors and IDR interactions.
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Han, Li. "G protein coupled receptor signaling to phospholipase D1 mediated by G12 type G proteins, LIM kinase and cofilin." [S.l.] : [s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=968929923.

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Lorenzen-Schmidt, Ilka. "The role of cytoskeletal LIM protein deficiency in the development of dilated cardiomyopathy /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2003. http://wwwlib.umi.com/cr/ucsd/fullcit?p3099547.

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Khurana, Bharat. "Characterization of DLIM1, a novel cytoskeleton-associated LIM domain containing protein of Dictyostelium discoideum." [S.l. : s.n.], 2000. http://deposit.ddb.de/cgi-bin/dokserv?idn=961945737.

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Diefenbacher, Markus Elmar [Verfasser]. "The transcriptional co-activator function of the LIM-domain protein nTrip6 / Markus Elmar Diefenbacher." Eggenstein-Leopoldshafen : Forschungszentrum Karlsruhe GmbH, 2010. http://d-nb.info/1002907535/34.

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Books on the topic "LIM Protein"

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Nikolaevich, Avdeev Boris, and Avdeeva Aleksandra Ivanovna, eds. Lik voĭny: Molodezhʹ v russkoĭ kontrrevoli͡u︡t͡s︡ii. Moskva: "Evrazii͡a︡ +", 2002.

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Khalīfah, ʻAbd al-Raʼūf. al-ʻĀlam al-sirrī lil-ḥarakāt al-iḥtijājīyah: Ruʼyah lil-wāqiʻ, Miṣr 2005-2013. al-Qāhirah: Samā lil-Nashr wa-al-Tawzīʻ, 2021.

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Sheng wu ji suan: Sheng wu xu lie de fen xi fang fa yu ying yong. Beijing: Ke xue chu ban she, 2010.

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al-Rabīʻ al-ʻArabī-- ilá ayna?: Ufuq jadīd lil-taghyīr al-dīmuqrāṭī. Bayrūt: Markaz Dirāsāt al-Waḥdah al-ʻArabīyah, 2011.

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Darwīsh, Marwān Muḥammad. al-Iḥtijāj al-Shīʻī fī Filasṭīn: Al-mustaqbal al-majhūl lil-muqāwamah ghayr al-musallaḥah. Bayrūt: Muʼassasat al-Dirāsāt al-Filasṭīnīyah, 2018.

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Rabīʻ al-mughaffalīn: Al-nihāyah al-mumanhajah lil-ʻArab fī (jiyū-stirātījīyah) ḥukūmat al-ʻālam al-jadīd. al-Qāhirah: Shams lil-Nashr wa-al-Tawzīʻ, 2014.

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al-Manẓūmah al-siyāsīyah lil-dawlah al-waṭanīyah wa-al-iḥtijājāt al-shaʻbīyah. al-Qāhirah: Dār al-Ḥikmah Ṭibaʻah wa-al-Nashr wa-al-Tawzīʻ, 2014.

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al-Thawarāt al-ʻArabīyah lam taktamil--: Masārāt wa-istiʻṣāʼāt. al-Qāhirah: Dār al-Thaqāfah al-Jadīdah, 2015.

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DNA he dan bai zhi xu lie shu ju fen xi gong ju: Tools for analysis of DNA and protein sequence data. 2nd ed. Beijing: Ke xue chu ban she, 2010.

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Venkatasubramanian, Lalanti. Topographical Projections of Limb-Innervating Motor Neurons in Drosophila melanogaster Specified by Morphological Transcription Factors and Downstream Cell Surface Proteins. [New York, N.Y.?]: [publisher not identified], 2019.

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Book chapters on the topic "LIM Protein"

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Jurata, L. W., and G. N. Gill. "Structure and Function of LIM Domains." In Protein Modules in Signal Transduction, 75–113. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-80481-6_4.

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Pantelis, D., J. Kirfel, R. Büttner, A. Hirner, and J. C. Kalff. "Role of four and one half LIM domain protein FHL2 on intestinal anastomotic healing." In Deutsche Gesellschaft für Chirurgie, 9–10. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-00625-8_4.

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Caroni, Pico. "Mice Deficient in Muscle LIM Protein (MLP) Reveal a Pathway to Dilated Cardiomyopathy and Heart Failure." In Developments in Cardiovascular Medicine, 27–33. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-015-9321-2_4.

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Schessl, Joachim. "Scapuloperoneal Disorders and Reducing Body Myopathy Associated with the Four and Half LIM Domain Protein 1." In Muscle Disease, 175–77. Oxford, UK: John Wiley & Sons, Ltd, 2013. http://dx.doi.org/10.1002/9781118635469.ch19.

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Alonso, Nivaldo, and Julia Amundson. "Bone Substitute: Alveolar Bone Grafting (ABG) with rhBMP-2 (Recombinant Bone Morphogenic Protein-2)." In Cleft Lip and Palate Treatment, 263–68. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-63290-2_17.

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Blundell, Patricia A., Jose-Luis de la Pompa, J. H. Carel Meijers, Andreas Trumpp, and Rolf Zeller. "The Limb Deformity Gene Encodes Evolutionarily Highly Conserved Proteins." In Developmental Patterning of the Vertebrate Limb, 25–30. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3310-8_4.

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Oudkhir, M., I. Martelly, M. Castagna, J. Moraczewski, and B. Boilly. "Protein Kinase C Activity During Limb Regeneration of Amphibians." In Recent Trends in Regeneration Research, 69–79. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-9057-2_7.

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Kozlowski, Gerald P., Gajanan Nilaver, and Berislav V. Zlokovič. "Immunoneurology: A Serum Protein Afferent Limb to the CNS." In Advances in Experimental Medicine and Biology, 345–70. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5799-5_22.

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Wang, Wei, Cynthia C. Bartholomae, Richard Gabriel, Annette Deichmann, and Manfred Schmidt. "The LAM-PCR Method to Sequence LV Integration Sites." In Lentiviral Vectors and Exosomes as Gene and Protein Delivery Tools, 107–20. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3753-0_9.

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Zhao, Yangu, Nasir Malik, and Heiner Westphal. "Functions of LIM-Homeodomain Proteins in the Development of the Nervous System." In Transcription Factors in the Nervous System, 75–94. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2006. http://dx.doi.org/10.1002/3527608036.ch4.

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Conference papers on the topic "LIM Protein"

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Dahan, Jennifer, Florence Levillayer, Catherine Werts, Grégory Jouvion, Yann Nouët, Minou Adib-Conquy, Anne-Marie Cassard-Doulcier, et al. "Abstract 2337: Loss of the LIM-only protein FHL2 enhances TGF-β expression and fibrogenesis." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2337.

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Fowler, Sandy Wan S., Diego Loayza, and Pascal Maguin. "Abstract 1408: LIM protein Ajuba participates in the ATR response by direct interaction with RPA70." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-1408.

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Tanaka, Ichidai, Hirotaka Osada, Makiko Fujii, and Yoshitaka Sekido. "Abstract 4313: A LIM protein ajuba suppresses malignant mesothelioma cell proliferation via Hippo signaling cascade." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4313.

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Sommer, J., C. Dorn, R. Weiskirchen, and C. Hellerbrand. "Expression and Function of Four-and-a-Half LIM-domain protein 2 (FHL2) in Hepatic Fibrosis." In 36. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0039-3402114.

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Sommer, J., and C. Hellerbrand. "Expression and Function of Four-and-a-Half LIM-domain protein 2 (FHL2) in Hepatocellular Carcinoma." In 36. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0039-3402218.

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Mise, Nikica, Haiying Yu, Naftali Kaminski, and Oliver Eickelberg. "The LIM Protein Zyxin Modulates TGF²1-Induced Alveolar Epithelial Cell Motility Via Integrin ±5²1." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a5563.

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Peng, Hongzhuang, Zhaoyuan Hou, Mei He, Electron Kebebew, Torben F. Orntoft, Meenhard Herlyn, Andrew J. Caton, William J. Fredericks, Bruce Malkowicz, and Frank J. Rauscher. "Abstract 5219: The LIM protein LIMD2 functions as an effector and biomarker for metastasis in multiple tumor types." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-5219.

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Sommer, Judith, and Claus Hellerbrand. "Four-and-a-half LIM-domain protein (FHL2) affects diet induced obesity, diabetes and hepatic steatosis and inflammation." In 38. Jahrestagung der Deutsche Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag, 2022. http://dx.doi.org/10.1055/s-0041-1740736.

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Venkitachalam, Srividya, Fu-Yu Chueh, and Chao-Lan Yu. "Abstract 4008: Nuclear localization of Lymphocyte-specific protein tyrosine kinase (Lck) and its role in regulating LIM domain only 2 (LMO2) gene." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4008.

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Tsui, Stephen Kwok-Wing, and Cyanne Ye Cao. "Abstract 4435: Functional role of four-and-a-half LIM protein 2 in the alternative splicing of cancer hallmark genes of hepatocellular carcinoma." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-4435.

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Reports on the topic "LIM Protein"

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Dickman, Martin B., and Oded Yarden. Phosphorylative Transduction of Developmental and Pathogenicity-Related Cues in Sclerotinia Sclerotiorum. United States Department of Agriculture, April 2004. http://dx.doi.org/10.32747/2004.7586472.bard.

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Sclerotinia sclerotiorum (Lib.) de Bary is among the world's most successful and omnivorous fungal plant pathogens. Included in the more than 400 species of plants reported as hosts to this fungus are canola, alfalfa, soybean, sunflower, dry bean, and potato. The general inability to develop resistant germplasm with these economically important crops to this pathogen has focused attention on the need for a more detailed examination of the pathogenic determinants involved in disease development. This proposal involved experiments that examined the involvement of protein phosphorylation during morphogenesis (hyphal elongation and sclerotia formation) and pathogenesis (oxalic acid). Data obtained from our laboratories during the course of this project substantiates the fact that kinases and phosphatases are involved and important for these processes. A mechanistic understanding of the successful strategy(ies) used by S . sclerotiorum in infecting and proliferating in host plants and this linkage to fungal development will provide targets and/or novel approaches with which to design resistant crop plants including interference with fungal pathogenic development. The original objectives of this grant included: I. Clone the cyclic AMP-dependent protein kinase A (PKA) catalytic subunit gene from S.sclerotiorum and determine its role in fungal pathogenicity, OA production (OA) and/or morphogenesis (sclerotia formation). II. Clone and characterize the catalytic and regulatory subunits of the protein phosphatase PP2A holoenzyme complex and determine their role in fungal pathogenicity and/or morphogenesis as well as linkage with PKA-regulation of OA production and sclerotia formation. III. Clone and characterize the adenylate cyclase-encoding gene from S . sclerotiorum and detennine its relationship to the PKA/PP2A-regulated pathway. IV. Analyze the expression patterns of the above-mentioned genes and their products during pathogenesis and determine their linkage with infection and fungal growth.
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Bleuel, D. L., and R. J. Donahue. Optimization of the {sup 7}Li(p,n) proton beam energy for BNCT applications. Office of Scientific and Technical Information (OSTI), February 1996. http://dx.doi.org/10.2172/212700.

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Bleuel, B. L., and R. J. Donahue. Optimization of the {sup 7}Li(p,n) proton beam energy for BNCT applications. Office of Scientific and Technical Information (OSTI), May 1996. http://dx.doi.org/10.2172/273022.

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Chamovitz, Daniel A., and Xing-Wang Deng. Developmental Regulation and Light Signal Transduction in Plants: The Fus5 Subunit of the Cop9 Signalosome. United States Department of Agriculture, September 2003. http://dx.doi.org/10.32747/2003.7586531.bard.

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Plants adjust their growth and development in a manner optimal for the prevailing light conditions. The molecular mechanisms by which light signals are transduced and integrated with other environmental and developmental signals are an area of intense research. (Batschauer, 1999; Quail, 2002) One paradigm emerging from this work is the interconnectedness of discrete physiological responses at the biochemical level, for instance, between auxin and light signaling (Colon-Carmona et al., 2000; Schwechheimer and Deng, 2001; Tian and Reed, 1999) and between light signaling and plant pathogen interactions (Azevedo et al., 2002; Liu et al., 2002). The COP9 signalosome (CSN) protein complex has a central role in the light control of plant development. Arabidopsis mutants that lack this complex develop photomorphogenically even in the absence of light signals (reviewed in (Karniol and Chamovitz, 2000; Schwechheimer and Deng, 2001). Thus the CSN was hypothesized to be a master repressor of photomorphogenesis in darkness, and light acts to bypass or eliminate this repression. However, the CSN regulates more than just photomorphogenesis as all mutants lacking this complex die near the end of seedling development. Moreover, an essentially identical complex was subsequently discovered in animals and yeast, organisms whose development is not light responsive, exemplifying how plant science can lead the way to exciting discoveries in biomedical model species (Chamovitz and Deng, 1995; Freilich et al., 1999; Maytal-Kivity et al., 2002; Mundt et al., 1999; Seeger et al., 1998; Wei et al., 1998). Our long-term objective is to determine mechanistically how the CSN controls plant development. We previously that this complex contains eight subunits (Karniol et al., 1998; Serino et al., 1999) and that the 27 ilia subunit is encoded by the FUS5/CSN7 locus (Karniol et al., 1999). The CSN7 subunit also has a role extraneous to the COP9 signalosome, and differential kinase activity has been implicated in regulating CSN7 and the COP9 signalosome (Karniol et al., 1999). In the present research, we further analyzed CSN7, both in terms of interacting proteins and in terms of kinases that act on CSN7. Furthermore we completed our analysis of the CSN in Arabidopsis by analyzing the remaining subunits. Outline of Original Objectives and Subsequent Modifications The general goal of the proposed research was to study the CSN7 (FUS5) subunit of the COP9 signalosome. To this end we specifically intended to: 1. Identify the residues of CSN7 that are phosphorylated. 2. Monitor the phosphorylation of CSN7 under different environmental conditions and under different genetic backgrounds. 3. Generate transgenic plants with altered CSN7 phosphorylation sites. 4. Purify CSN7 kinase from cauliflower. 5. Clone the Arabidopsis cDNA encoding CSN7 kinase 6. Isolate and characterize additional CSN7 interacting proteins. 7. Characterize the interaction of CSN7 and the COP9 signalosome with the HY5-COP1 transcriptional complex. Throughout the course of the research, emphasis shifted from studying CSN7 phosphorylation (Goals 1-3), to studying the CSN7 kinase (Goal 4 and 5), an in depth analysis of CSN7 interactions (Goal 6), and the study of additional CSN subunits. Goal 7 was also abandoned as no data was found to support this interaction.
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Corriveau-Bourque, Alexandre, Fernanda Almeida, and Alain Frechette. Uncertainty and Opportunity: The Status of Forest Carbon Rights and Governance Frameworks in Over Half of the World’s Tropical Forests. Rights and Resources Initiative, March 2018. http://dx.doi.org/10.53892/fnpn5361.

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Most of the world’s remaining tropical forests lie in areas that are customarily managed and/or legally owned by Indigenous Peoples and local communities. In the context of climate change and global efforts to protect and enhance the capacity of forests to capture and store greenhouse gas emissions, the question of who owns the trees and the carbon stored therein is paramount. Clarifying this question is crucial, both for the future of the planet, and for up to 1.7 billion people worldwide who rely on forests for their livelihoods. This brief presents a review of the nominal progress made in the national-level laws and regulations that govern the carbon trade and define the rights of parties —across a sample of 24 countries in Africa, Asia and Latin America. These countries collectively hold more than 50 percent of global tropical and subtropical forests. This brief also examines the design and establishment of safeguard mechanisms concerning benefit sharing, providing redress and resolution to disputes related to carbon-based schemes, and the operationalization of carbon registries for each of these countries.
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Shani, Moshe, and C. P. Emerson. Genetic Manipulation of the Adipose Tissue via Transgenesis. United States Department of Agriculture, April 1995. http://dx.doi.org/10.32747/1995.7604929.bard.

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The long term goal of this study was to reduce caloric and fat content of beef and other red meats by means of genetic modification of the animal such that fat would not be accumulated. This was attempted by introducing into the germ line myogenic regulatory genes that would convert fat tissue to skeletal muscle. We first determined the consequences of ectopic expression of the myogenic regulatory gene MyoD1. It was found that deregulation of MyoD1 did not result in ectopic skeletal muscle formation but rather led to embryonic lethalities, probably due to its role in the control of the cell cycle. This indicated that MyoD1 should be placed under stringent control to allow survival. Embryonic lethalities were also observed when the regulatory elements of the adipose-specific gene adipsin directed the expression of MyoD1 or myogenin cDNAs, suggesting that these sequences are probably not strong enough to confer tissue specificity. To determine the specificity of the control elements of another fat specific gene (adipocyte protein 2-aP2), we fused them to the bacterial b-galactosidase reporter gene and established stable transgenic strains. The expression of the reporter gene in none of the strains was adipose specific. Each strain displayed a unique pattern of expression in various cell lineages. Most exciting results were obtained in a transgenic strain in which cells migrating from the ventro-lateral edge of the dermomyotome of developing somites to populate the limb buds with myoblasts were specifically stained for lacZ. Since the control sequences of the adipsin or aP2 genes did not confer fat specificity in transgenic mice we have taken both molecular and genetic approaches as an initial effort to identify genes important in the conversion of a multipotential cell such as C3H10T1/2 cell to adipoblast. Several novel adipocyte cell lines have been established that differ in the expression of transcription factors of the C/EBP family known to be markers for adipocyte differentiation. These studies revealed that one of the genetic programming changes which occur during 10T1/2 conversion from multipotential cell to a committed adipoblast is the ability to linduce C/EBPa gene expression. It is expected that further analysis of this gene would identify elements which regulate this lineage-specific expression. Such elements might be good candidates in future attempts to convert adipoblasts to skeletal muscle cells in vivo.
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