Relevant bibliographies by topics / ERM PROTEINS

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'ERM PROTEINS'

Author: Grafiati
Published: 14 March 2023

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Journal articles on the topic "ERM PROTEINS"

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McClatchey, Andrea I. "ERM proteins." Current Biology 22, no. 18 (September 2012): R784—R785. http://dx.doi.org/10.1016/j.cub.2012.07.057.

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McClatchey, Andrea I. "ERM proteins at a glance." Journal of Cell Science 127, no. 15 (June 20, 2014): 3199–204. http://dx.doi.org/10.1242/jcs.098343.

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Clucas, J., and F. Valderrama. "ERM proteins in cancer progression." Journal of Cell Science 127, no. 2 (January 13, 2014): 267–75. http://dx.doi.org/10.1242/jcs.133108.

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Clucas, J., and F. Valderrama. "ERM proteins in cancer progression." Journal of Cell Science 128, no. 6 (March 15, 2015): 1253. http://dx.doi.org/10.1242/jcs.170027.

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Bagchi, M., M. Katar, W. K. Lo, R. Yost, C. Hill, and H. Maisel. "ERM proteins of the lens." Journal of Cellular Biochemistry 92, no. 3 (2004): 626–30. http://dx.doi.org/10.1002/jcb.20062.

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Kondo, Takahisa, Kosei Takeuchi, Yoshinori Doi, Shigenobu Yonemura, Shigekazu Nagata, Shoichiro Tsukita, and Sachiko Tsukita. "ERM (Ezrin/Radixin/Moesin)-based Molecular Mechanism of Microvillar Breakdown at an Early Stage of Apoptosis." Journal of Cell Biology 139, no. 3 (November 3, 1997): 749–58. http://dx.doi.org/10.1083/jcb.139.3.749.

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Breakdown of microvilli is a common early event in various types of apoptosis, but its molecular mechanism and implications remain unclear. ERM (ezrin/radixin/moesin) proteins are ubiquitously expressed microvillar proteins that are activated in the cytoplasm, translocate to the plasma membrane, and function as general actin filament/plasma membrane cross-linkers to form microvilli. Immunofluorescence microscopic and biochemical analyses revealed that, at the early phase of Fas ligand (FasL)–induced apoptosis in L cells expressing Fas (LHF), ERM proteins translocate from the plasma membranes of microvilli to the cytoplasm concomitant with dephosphorylation. When the FasL-induced dephosphorylation of ERM proteins was suppressed by calyculin A, a serine/threonine protein phosphatase inhibitor, the cytoplasmic translocation of ERM proteins was blocked. The interleukin-1β–converting enzyme (ICE) protease inhibitors suppressed the dephosphorylation as well as the cytoplasmic translocation of ERM proteins. These findings indicate that during FasL-induced apoptosis, the ICE protease cascade was first activated, and then ERM proteins were dephosphorylated followed by their cytoplasmic translocation, i.e., microvillar breakdown. Next, to examine the subsequent events in microvillar breakdown, we prepared DiO-labeled single-layered plasma membranes with the cytoplasmic surface freely exposed from FasL-treated or nontreated LHF cells. On single-layered plasma membranes from nontreated cells, ERM proteins and actin filaments were densely detected, whereas those from FasL-treated cells were free from ERM proteins or actin filaments. We thus concluded that the cytoplasmic translocation of ERM proteins is responsible for the microvillar breakdown at an early phase of apoptosis and that the depletion of ERM proteins from plasma membranes results in the gross dissociation of actin-based cytoskeleton from plasma membranes. The physiological relevance of this ERM protein–based microvillar breakdown in apoptosis will be discussed.
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Yonemura, Shigenobu, Takeshi Matsui, Shoichiro Tsukita, and Sachiko Tsukita. "Rho-dependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: an essential role for polyphosphoinositides in vivo." Journal of Cell Science 115, no. 12 (June 15, 2002): 2569–80. http://dx.doi.org/10.1242/jcs.115.12.2569.

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Ezrin/radixin/moesin (ERM) proteins crosslink actin filaments to plasma membranes and are involved in the organization of the cortical cytoskeleton,especially in the formation of microvilli. ERM proteins are reported to be activated as crosslinkers in a Rho-dependent manner and are stabilized when phosphorylated at their C-terminal threonine residue to create C-terminal threonine-phosphorylated ERM proteins (CPERMs). Using a CPERM-specific mAb, we have shown, in vivo, that treatment with C3 transferase (a Rho inactivator) or staurosporine (a protein kinase inhibitor) leads to the dephosphorylation of CPERMs, the translocation of ERM proteins from plasma membranes to the cytoplasm and microvillar breakdown. We further elucidated that ERM protein activation does not require C-terminal phosphorylation in A431 cells stimulated with epidermal growth factor. In certain types of kidney-derived cells such as MDCK cells, however, ERM proteins appear to be activated in the absence of Rho activation and remain active without C-terminal phosphorylation. Interestingly, microinjection of an aminoglycoside antibiotic, neomycin, which binds to polyphosphoinositides, such as phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P2],affected the activation of ERM proteins regardless of cell type. These findings not only indicate the existence of a Rho-independent activation mechanism of ERM proteins but also suggest that both Rho-dependent and-independent activation of ERM proteins require a local elevation of PtdIns(4,5)P2 concentration in vivo.
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Hirao, M., N. Sato, T. Kondo, S. Yonemura, M. Monden, T. Sasaki, Y. Takai, S. Tsukita, and S. Tsukita. "Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway." Journal of Cell Biology 135, no. 1 (October 1, 1996): 37–51. http://dx.doi.org/10.1083/jcb.135.1.37.

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The ERM proteins, ezrin, radixin, and moesin, are involved in the actin filament/plasma membrane interaction as cross-linkers. CD44 has been identified as one of the major membrane binding partners for ERM proteins. To examine the CD44/ERM protein interaction in vitro, we produced mouse ezrin, radixin, moesin, and the glutathione-S-transferase (GST)/CD44 cytoplasmic domain fusion protein (GST-CD44cyt) by means of recombinant baculovirus infection, and constructed an in vitro assay for the binding between ERM proteins and the cytoplasmic domain of CD44. In this system, ERM proteins bound to GST-CD44cyt with high affinity (Kd of moesin was 9.3 +/- 1.6nM) at a low ionic strength, but with low affinity at a physiological ionic strength. However, in the presence of phosphoinositides (phosphatidylinositol [PI], phosphatidylinositol 4-monophosphate [4-PIP], and phosphatidylinositol 4.5-bisphosphate [4,5-PIP2]), ERM proteins bound with a relatively high affinity to GST-CD44cyt even at a physiological ionic strength: 4,5-PIP2 showed a marked effect (Kd of moesin in the presence of 4,5-PIP2 was 9.3 +/- 4.8 nM). Next, to examine the regulation mechanism of CD44/ERM interaction in vivo, we reexamined the immunoprecipitated CD44/ERM complex from BHK cells and found that it contains Rho-GDP dissociation inhibitor (GDI), a regulator of Rho GTPase. We then evaluated the involvement of Rho in the regulation of the CD44/ERM complex formation. When recombinant ERM proteins were added and incubated with lysates of cultured BHK cells followed by centrifugation, a portion of the recombinant ERM proteins was recovered in the insoluble fraction. This binding was enhanced by GTP gamma S and markedly suppressed by C3 toxin, a specific inhibitor of Rho, indicating that the GTP form of Rho in the lysate is required for this binding. A mAb specific for the cytoplasmic domain of CD44 also markedly suppressed this binding, identifying most of the binding partners for exogenous ERM proteins in the insoluble fraction as CD44. Consistent with this binding analysis, in living BHK cells treated with C3 toxin, most insoluble ERM proteins moved to soluble compartments in the cytoplasm, leaving CD44 free from ERM. These findings indicate that Rho regulates the CD44/ERM complex formation in vivo and that the phosphatidylinositol turnover may be involved in this regulation mechanism.
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Yonemura, Shigenobu, Sachiko Tsukita, and Shoichiro Tsukita. "Direct Involvement of Ezrin/Radixin/Moesin (ERM)-binding Membrane Proteins in the Organization of Microvilli in Collaboration with Activated ERM Proteins." Journal of Cell Biology 145, no. 7 (June 28, 1999): 1497–509. http://dx.doi.org/10.1083/jcb.145.7.1497.

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Ezrin/radixin/moesin (ERM) proteins have been thought to play a central role in the organization of cortical actin-based cytoskeletons including microvillar formation through cross-linking actin filaments and integral membrane proteins such as CD43, CD44, and ICAM-2. To examine the functions of these ERM-binding membrane proteins (ERMBMPs) in cortical morphogenesis, we overexpressed ERMBMPs (the extracellular domain of E-cadherin fused with the transmembrane/cytoplasmic domain of CD43, CD44, or ICAM-2) in various cultured cells. In cultured fibroblasts such as L and CV-1 cells, their overexpression significantly induced microvillar elongation, recruiting ERM proteins and actin filaments. When the ERM-binding domains were truncated from these molecules, their ability to induce microvillar elongation became undetectable. In contrast, in cultured epithelial cells such as MTD-1A and A431 cells, the overexpression of ERMBMPs did not elongate microvilli. However, in the presence of EGF, overexpression of ERMBMPs induced remarkable microvillar elongation in A431 cells. These results indicated that ERMBMPs function as organizing centers for cortical morphogenesis by organizing microvilli in collaboration with activated ERM proteins. Furthermore, immunodetection with a phosphorylated ERM-specific antibody and site-directed mutagenesis suggested that ERM proteins phosphorylated at their COOH-terminal threonine residue represent activated ERM proteins.
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Michie, Katharine A., Adam Bermeister, Neil O. Robertson, Sophia C. Goodchild, and Paul M. G. Curmi. "Two Sides of the Coin: Ezrin/Radixin/Moesin and Merlin Control Membrane Structure and Contact Inhibition." International Journal of Molecular Sciences 20, no. 8 (April 23, 2019): 1996. http://dx.doi.org/10.3390/ijms20081996.

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The merlin-ERM (ezrin, radixin, moesin) family of proteins plays a central role in linking the cellular membranes to the cortical actin cytoskeleton. Merlin regulates contact inhibition and is an integral part of cell–cell junctions, while ERM proteins, ezrin, radixin and moesin, assist in the formation and maintenance of specialized plasma membrane structures and membrane vesicle structures. These two protein families share a common evolutionary history, having arisen and separated via gene duplication near the origin of metazoa. During approximately 0.5 billion years of evolution, the merlin and ERM family proteins have maintained both sequence and structural conservation to an extraordinary level. Comparing crystal structures of merlin-ERM proteins and their complexes, a picture emerges of the merlin-ERM proteins acting as switchable interaction hubs, assembling protein complexes on cellular membranes and linking them to the actin cytoskeleton. Given the high level of structural conservation between the merlin and ERM family proteins we speculate that they may function together.
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Dissertations / Theses on the topic "ERM PROTEINS"

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Hebert, Alan. "Functional Relationship between Merlin and the ERM Proteins." Thesis, Harvard University, 2012. http://dissertations.umi.com/gsas.harvard:10567.

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The ability to spatially restrict specific activities across the cell cortex functionally defines individual cells and tissues. This is achieved, in part, via the assembly of protein complexes that link the plasma membrane to the underlying cortical actin cytoskeleton. The neurofibromatosis type 2 (NF2) tumor suppressor Merlin and closely related ERM proteins (Ezrin, Radixin and Moesin) are a special class of such membrane:cytoskeleton associated proteins that function to organize specialized cortical domains. In addition to their high degree of similarity, mounting evidence suggests that Merlin/ERMs share a functional relationship, which is largely unexplored. Unlike Merlin, the ERMs are not known to inhibit cell proliferation; in fact, Ezrin is thought to promote tumor metastasis. Defining the relationship between Merlin and the ERMs is essential to appreciating their respective roles in cancer development. Here I demonstrate a novel role for Merlin and the ERMs in generating cortical asymmetry in the absence of external cues. Our data reveal that Merlin functions to restrict the cortical distribution of Ezrin, which in turn positions the interphase centrosome in single epithelial cells and 3D organotypic cultures. In the absence of Merlin, ectopic cortical Ezrin yields mispositioned centrosomes, misoriented spindles and aberrant epithelial architecture. Furthermore, in tumor cells with centrosome amplification, the failure to restrict cortical Ezrin abolishes centrosome clustering, yielding multipolar mitoses. Consistent with a functional relationship, I observe a strong genetic interaction between Nf2 and Ezrin in the mouse intestine in vivo. Finally, I begin to address the basis of their functional interaction by testing whether they are coordinately regulated by the Ste-20 like kinase SLK. Altogether, these data uncover fundamental roles for Merlin/ERM proteins in spatiotemporally organizing the cell cortex in vitro and in vivo and suggest that Merlin’s role in promoting cortical heterogeneity may contribute to tumorigenesis by disrupting cell polarity, spindle orientation and potentially genome stability.
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Machicoane, Michaël. "The role of ERM proteins in cell division." Paris 6, 2013. http://www.theses.fr/2013PA066285.

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Le contrôle de l’axe des divisions cellulaires assure le développement correct des organismes multicellulaires. Ce processus repose sur la localisation corticale de complexes protéiques capable de tirer sur les microtubules du fuseau mitotique. Notamment, le module conservé au court de l’évolution et formé des protéines Gαi / LGN / NuMA recrute le moteur Dynéine au cortex. De plus, des signaux intra- ou extracellulaires peuvent ensuite influencer ce complexe. Par exemple, l’organisation de l’actine corticale est essentielle à la localisation et l’activité des générateurs de force. L’identification des protéines capables d’organiser l’actine corticale en mitose est donc un enjeu majeur. Mon travail de thèse a consisté en l’exploration du rôle des ERM (Ezrine-Radixine-Moésine), des protéines liant l’actine à la membrane plasmique, dans l’orientation du fuseau mitotique. Nos travaux ont montré que, dans les cellules de mammifère, les ERM sont activés à l’entrée de mitose via une phosphorylation directe par la kinase SLK. Le rôle de l’activation des ERM dans l’orientation du fuseau mitotique a été démontré dans deux systèmes : des substrats adhésifs microfabriqués contrôlant l’adhésion des cellules en culture, et les progéniteurs apicaux du neuroépithélium murin. A l’échelle moléculaire, l’activation des ERM est nécessaire au recrutement cortical polarisé d’un membre des générateurs de force, NuMA. Ces travaux suggèrent donc que l’actine corticale et protéines organisatrices ERM jouent un rôle important au cortex mitotique, permettant le recrutement des générateurs de force à la membrane et en conséquence l’orientation correcte du fuseau mitotique
The control of cell division axis is crucial for embryogenesis, cell differentiation and adult tissue homeostasis, and relies on the cortical localization of protein complexes able to pull on the mitotic apparatus. One of these force generators is the evolutionary conserved Gαi / LGN / NuMA module, which recruits Dynein motors at the cortex. On top of this, intrinsic and extrinsic cues can then modulate the activity and localization of this complex. Particularly, the F-actin cortex has recently been involved in the dialogue between astral microtubules and force generators. Identifying the proteins involved in F-actin organization at the cortex is thus a major challenge. During my thesis work, I focused my attention on the proteins of the ERM (Ezrin-Radixin-Moesin) family. I investigated the role of these membrane-actin linkers in the orientation of the mitotic spindle during oriented cell division. Our work demonstrated that ERM are strongly and directly activated by the SLK kinase at mitotic entry in mammalian cells. Using micro-fabricated adhesive substrates to control the axis of cell division, we found that the activation of ERM plays a key role in guiding the orientation of the mitotic spindle. Accordingly, impairing ERM activation in apical progenitors of the mouse embryonic neocortex severely disturbed spindle orientation in vivo. At the molecular level, ERM activation promotes the polarized association at the mitotic cortex of NuMA. We propose that F-actin and activated ERM at the mitotic cortex are critical for the correct localization of force generator complexes and hence for proper spindle orientation
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Matsui, Takeshi. "Activation of ERM (ezrin/radixin/moesin) proteins by the small GTP binding protein Rho." Kyoto University, 2000. http://hdl.handle.net/2433/180838.

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Bissen, Philippe [Verfasser], and Volker [Akademischer Betreuer] Gerke. "ERM proteins - regulators of mitosis? / Philippe Bissen ; Betreuer: Volker Gerke." Münster : Universitäts- und Landesbibliothek Münster, 2019. http://d-nb.info/1181188873/34.

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Zarrouk, Marouan. "The role of ezrin/radixin/moesin(ERM) proteins in L-selectin-dependent signalling." Thesis, Imperial College London, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.510756.

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Olsson, Per-Anders. "MIR, a novel ERM-like protein in the nervous system." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2001. http://publications.uu.se/theses/91-554-5061-X/.

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Legg, James William. "Regulation of the hyaluronan receptor CD44 by the ezrin/radixin/moesin (ERM) family of proteins." Thesis, Imperial College London, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.392688.

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Hayashi, Ken. "Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues : application of a novel fixation protocol using trichloroacetic acid (TCA) as a fixative." Kyoto University, 1999. http://hdl.handle.net/2433/181750.

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BRUNO, MARINA. "ROLE OF BIOACTIVE SPHINGOLIPIDS IN INNER EAR AND SKELETAL MUSCLE BIOLOGY." Doctoral thesis, Università di Siena, 2019. http://hdl.handle.net/11365/1072579.

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Sphingolipids are a class of complex lipids known to be not only structural components of biological membranes, but also bioactive molecules involved in several processes, such as cell differentiation, proliferation, motility and cell survival. Between them, we focused on sphingosine 1-phosphate (S1P) and ceramide 1-phosphate (C1P). S1P is intracellularly produced by sphingosine kinase (SK) 1 and SK2 and exerts many of its action consequently to its ligation to S1P specific receptors (S1PR), S1P1–5, whereas C1P is generated by the action of ceramide kinase and it is able to via activation of different signalling pathways. Recent experimental findings demonstrate an emerging role for S1P signalling axis in the maintenance of auditory function. WHO reported that age-related sensorineural hearing loss (SNHL) affects more than 360 million people worldwide, and the current unique available treatment is cochlear implant, which has important use limitations. Our main aim was to investigate S1P signalling axis role in this biological context: in the first paper, we demonstrated that the fibroblast growth factor 2 (FGF2)-induced proliferative action in US/VOT-N33 auditory neuroblasts was dependent on SK1, SK2 as well as S1P1 and S1P2. Moreover, the pro-survival effect of FGF2 from apoptotic cell death induced by staurosporine treatment was dependent on SK but not on S1PR. In addition, ERK1/2 and Akt signaling pathways were found to mediate the mitogenic and survival action of FGF2, respectively. In the second paper, we focused on the emerging role of bioactive sphingolipids as regulators of ERM (ezrin-radixin-moesin) proteins. ERM are a family of cross-linker adaptors between plasma membrane and actin cytoskeleton, playing a crucial role in cell morphology and signal transduction. S1P was found to activate ERM in a S1P2-dependent manner in US/VOT-E36 auditory epithelial progenitors and S1P-induced ERM activation potently contributed to actin cytoskeletal remodeling and to the appearance of electrophysiological changes typical of more differentiated cells. Moreover, PKC and Akt activation was found to mediate S1P-induced ERM phosphorylation. Taken together, our findings demonstrate a crucial role for S1P signalling axis in inner ear biology and disclose potential innovative therapeutic approaches for hearing loss prevention and treatment. In order to develop new methodologies to solve the difficulties of getting drugs inside the inner ear, we studied solid lipid nanoparticles (SLN) as attractive biocompatible nanocarriers for the delivery of drugs with low solubility in aqueous media. In our third paper, we showed that SLN based on stearic acid are efficiently incorporated by HEI-OC1 cells and are not ototoxic at the doses studied. The SLN loaded with glucocorticoids were more effective in protecting cells by the cisplatin-induced damage than glucocorticoids alone. Preliminary in vivo studies also indicate that intratympanic SLN are able to reach the inner ear. These results indicate that SLN are highly efficient vehicles for inner ear drug-delivery and specifically for the administration of glucocorticoids. During my Ph.D. course I have also contributed to a parallel research focused on the role of sphingolipid signalling in skeletal muscle biology. Skeletal muscle is able to regenerate thanks to the presence of satellite cells that upon trauma enter into the cell cycle and start proliferating. Starting from the previously demonstrated positive role of C1P in myoblast proliferation, in the fourth paper we showed that C1P stimulates C2C12 myoblast proliferation via LPA signalling axis. Moreover, C1P via phospholipase A2 activation leads to LPA1 and LPA3 engagement, which in turn drive Akt and ERK1/2 activation, thus stimulating DNA synthesis. The present findings highlight a new key role for bioactive sphingolipids in skeletal muscle and provide further support to the possibility of using them as therapeutic targets for its regeneration.
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Tan, Yu Pei. "The development of Lactococcus lactis as an antimicrobial agent." Thesis, Queensland University of Technology, 2010. https://eprints.qut.edu.au/39143/1/Yu_Pei_Tan_Thesis.pdf.

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Non-pathogenic lactic acid bacteria are economically important Gram-positive bacteria used extensively in the food industry. Due to their “generally regarded as safe” status, certain species from the genera Lactobacillus and Lactococcus are also considered desirable as candidates for the production and secretion of recombinant proteins, particular those with therapeutic applications. The hypothesis examined by this thesis is that Lactococcus lactis can be modified to be an effective antimicrobial agent. Therefore, the aims of this thesis were to investigate the optimisation of the expression, secretion and/or activities of potential heterologous antimicrobial proteins by the model lactic acid bacterium, Lactococcus lactis subsp. cremoris MG1363. L. lactis strains were engineered to express and secrete the recombinant CyuC surface protein from Lactobacillus reuteri BR11, and a fusion protein consisting of CyuC and lysostaphin using the Sep promoter and secretion signal. CyuC has been characterised as a cystine-binding protein, but has also been demonstrated to have fibronectin binding activity. Lysostaphin is a bacteriolytic enzyme with specific activity against the Gram-positive pathogen, Staphylococcus aureus. These modified L. lactis strains were then investigated to see if they had the ability to inhibit the adhesion of S. aureus to host extracellular matrix (ECM) proteins. It was observed that the cell extracts of the L. lactis strain with the vector only (pGhost9:ISS1) was able to inhibit the adhesion of S. aureus to fibronectin, whilst the cell extracts of the L. lactis strain expressing lysostaphin was able to inhibit adhesion to keratin. Finally, this thesis has identified specific lactococcal genes that affect the secretion of lysostaphin through the use of random transposon mutagenesis. Ten mutants with higher lysostaphin activity contained insertions in four different genes encoding: (i) an uncharacterised putative transmembrane protein (llmg_0609), (ii) an enzyme catalysing the first step in peptidoglycan biosynthesis (murA2), (iii) a homolog of the oxidative defence regulator (trmA), and (iv) an uncharacterised putative enzyme involved in ubiquinone biosynthesis (llmg_2148). The higher lysostaphin activity observed in these mutants was found to be due to higher amounts of lysostaphin being secreted. The findings of this thesis contribute to the development of this organism as an antimicrobial agent and also to our understanding of L. lactis genetics.
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Books on the topic "ERM PROTEINS"

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G protein-coupled receptor genetics: Research and methods in the post-genomic era. New York: Humana Press, 2014.

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Kihara, Daisuke, ed. Protein Function Prediction for Omics Era. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-0881-5.

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Brazauskas, Gintaras, Gražina Statkevičiūtė, and Kristina Jonavičienė, eds. Breeding Grasses and Protein Crops in the Era of Genomics. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-89578-9.

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N, Kholodenko Boris, and Westerhoff Hans V, eds. Metabolic engineering in the post genomic era. Wymondham, Norfolk, England: Horizon Bioscience, 2004.

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J, Blencowe Benjamin, and Graveley Brenton R, eds. Alternative splicing in the postgenomic era. New York: Springer Science+Business Media, 2007.

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Commonwealth Scientific and Industrial Research Organization, ed. Nutrient requirements of domesticated ruminants. Collingwood: CSIRO Publishing, 2007.

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Garlin, Sender. Three American radicals: John Swinton, crusading editor : Charles P. Steinmetz, scientist and socialist : William Dean Howells and the Haymarket Era. Boulder: Westview Press, 1991.

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Zdeněk, Deyl, ed. Advanced chromatographic and electromigration methods in biosciences. Amsterdam: Elsevier, 1998.

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Handbook of detection of enzymes on electrophoretic gels. 2nd ed. Boca Raton: CRC Press, 2003.

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Manchenko, Gennady P. Handbook of detection of enzymes on electrophoretic gels. 2nd ed. Boca Raton, FL: CRC Press, 2002.

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Book chapters on the topic "ERM PROTEINS"

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Ren, Ling, and Chand Khanna. "ERM Proteins." In Encyclopedia of Cancer, 1–3. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-27841-9_1990-2.

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Ren, Ling, and Chand Khanna. "ERM Proteins." In Encyclopedia of Cancer, 1612–14. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-662-46875-3_1990.

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Ren, Ling, and Chand Khanna. "ERM Proteins." In Encyclopedia of Cancer, 1310–12. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_1990.

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Ren, L., and C. Khanna. "Merlin/NF2 Tumor Suppressor and Ezrin–Radixin–Moesin (ERM) Proteins in Cancer Development and Progression." In Cancer Genome and Tumor Microenvironment, 93–115. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-0711-0_5.

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Chua, Hon Nian, Guimei Liu, and Limsoon Wong. "Protein Function Prediction Using Protein–Protein Interaction Networks." In Protein Function Prediction for Omics Era, 243–70. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-0881-5_13.

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Debrunner, Peter G. "Mössbauer Spectroscopy of Iron Proteins." In EMR of Paramagnetic Molecules, 59–101. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2892-0_2.

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Brancaccio, Mara, Emila Turco, and Emilio Hirsch. "Tissue-Specific KO of ECM Proteins." In Methods in Molecular Biology, 15–50. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-413-1_2.

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Cuff, Alison, Oliver Redfern, Benoit Dessailly, and Christine Orengo. "Exploiting Protein Structures to Predict Protein Functions." In Protein Function Prediction for Omics Era, 107–23. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-0881-5_6.

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Thomas, David D., E. Michael Ostap, Christopher L. Berger, Scott M. Lewis, Piotr G. Fajer, and James E. Mahaney. "Transient EPR of Spin-Labeled Proteins." In EMR of Paramagnetic Molecules, 323–51. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2892-0_8.

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Andiappan, Muthumanickkam, and Subramanian Sundaramoorthy. "Studies on Indian Eri Silk Electrospun Fibroin Scaffold for Biomedical Applications." In Biomedical Applications of Natural Proteins, 51–64. New Delhi: Springer India, 2015. http://dx.doi.org/10.1007/978-81-322-2491-4_4.

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Conference papers on the topic "ERM PROTEINS"

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de Andrade, Juliana B., and Fernando A. Soares. "Abstract 338: Immunohistochemical expression of CD44/ERM complex proteins in penile carcinoma." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-338.

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Santiago, Caio R. N., Luciano A. Digiampietri, and Leandro M. Moreira. "GTACG: Um arcabouço computacional focado em genômica comparativa de bactérias de um mesmo ramo evolutivo." In Anais Estendidos do Simpósio Brasileiro de Computação Aplicada à Saúde. Sociedade Brasileira de Computação (SBC), 2020. http://dx.doi.org/10.5753/sbcas.2020.11553.

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Neste trabalho é apresentado o GTACG: um arcabouço computacional para genômica comparativa com foco em uma usabilidade facilitada e destinada a pesquisas para identificação de características genéticas únicas em subgrupos de genomas de bactérias que possuem um determinado fenótipo em comum. Os resultados foram validados com dois estudos de caso envolvendo um conjunto com 161 genomas da família Xanthomonadaceae, no qual foram encontradas 19 famílias proteicas ortólogas exclusivas aos genomas associados a plantas e 45 genomas de Streptococcus pyogenes, no qual foram encontrados 15 famílias de proteínas ortólogas que servem como marcadores filogenéticos para a proteína emm.
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Dias, André, Mateus Boiani, and Rafael Parpinelli. "Aplicação de Evolução Diferencial em GPU Para o Problema de Predição de Estrutura de Proteínas com Modelo 3D AB Off-Lattice." In XXI Simpósio em Sistemas Computacionais de Alto Desempenho. Sociedade Brasileira de Computação, 2020. http://dx.doi.org/10.5753/wscad.2020.14080.

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A função que uma proteína exerce está diretamente relacionada com a sua estrutura tridimensional. Porém, para a maior parte das proteínas atualmente sequenciadas ainda não se conhece sua forma estrutural nativa. Este artigo propõe a utilização do algoritmo de Evolução Diferencial (DE) desenvolvido na plataforma NVIDIA CUDA aplicado ao modelo 3D AB Off-Lattice para Predição de Estrutura de Proteínas. Uma estratégia de nichos e crowding foi implementada no algoritmo DE combinada com técnicas de autoajuste de parâmetros, rotinas para reinicialização da população, dois níveis de otimização e busca local. Quatro proteínas reais foram utilizadas para experimentação e os resultados obtidos se mostram competitivos com o estado-da-arte. A utilização de paralelismo massivo através da GPU ressalta a aplicabilidade desses recursos a esta classe de problemas atingindo acelerações de 708.78x para a maior cadeia proteica.
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Dong, Jinrui, Wupeng Liao, Hong Yong Peh, Tze Khee Chan, W. S. Daniel Tan, Li Li, and W. S. Fred Wong. "Ribosomal protein S3 gene silencing protects against experimental allergic asthma." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa562.

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Wang, Yunjie, and Katherine Yanhang Zhang. "The Biomechanical Properties of Arterial Elastin With Glucose Effect." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14200.

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Elastin, as one of the major extracellular matrix (ECM) components, is essential to accommodate physiological deformation and provide elastic support for blood vessels. Elastin is a long-lived ECM protein and it can suffer from cumulative effects of exposure to chemical damage, which can greatly compromise its biomechanical properties. The mechanical properties of elastin are related to its microstructure and the chemical environment. Glucose is an important carbohydrate in human body. The effect of glucose on the mechanical properties of blood vessels is especially magnified in diabetic patients [1]. Glucose can directly condense with amino groups of proteins by nonenzymatic glycation, which is one of the main mechanisms of aging [2].
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Lee, Hae-Jeong, Marvi A. Matos, Lisa Pakstis, Marcus T. Cicerone, and Joy P. Dunkers. "Quantitation of Laminin Adsorbed Onto Polydimethylsiloxane Surfaces Using Various Treatment Protocols." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192785.

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There is considerable interest in how cells respond to mechanical stimuli, from the ligands used to transmit the stimulus to the signaling pathways initiated and the proteins expressed upon phenotype change [1]. Previous work focused on the evaluation of the quality of the extracellular matrix (ECM) coating and cell proliferation [2]. Our focus is the characterization of a flexible polymeric substrate, treated with ECM, used to induce tensile strain on cells. In this work, we expand our physical characterization of the protein modified polydimethylsiloxane (PDMS) surface by quantifying the coverage of laminin on PDMS, plasma-treated PDMS, and PDMS treated with plasma and aminopropyltrimethoxysilane (APTMS) (Silane_70 protocol) using X-ray reflectivity.
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Sewell-Loftin, M. K., and W. David Merryman. "The Role of SRC in Strain- and Ligand- Dependent Phenotypic Modulation of Mouse Embryonic Fibroblasts." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53604.

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Connective tissue fibrosis represents a significant portion of mortality and morbidity in our society. These diseases include many illnesses such as heart valve disease, atherosclerosis, macular degeneration, and cirrhosis, meaning that millions of lives are affected by these conditions each year. Fibrotic tissues form when quiescent fibroblasts activate becoming myofibroblasts, the phenotype of active tissue construction and fibrosis. During this process, the cells produce smooth muscle α-actin (αSMA), a contractile element considered to be the hallmark of cellular activation [1]. Following the production of αSMA, there is an increase in the synthesis of extracellular matrix (ECM) proteins, most notably type I collagen; this increase in ECM proteins causes the stiffening of the tissue characteristic of fibrotic disease. In non-disease states (such as wound healing or tissue development), the myofibroblasts will either deactivate, becoming fibroblasts again, or apoptose before tissue fibrosis occurs. However, when myofibroblasts persist, increased ECM protein deposition causes increased tissue stiffness and activates neighboring cells, causing the fibrosis to propagate. Currently there are no therapies to prevent or reverse fibrosis. Therefore a more thorough understanding of the dynamic mechanical environment and signaling pathways involved in the activation of fibroblasts is required to develop potential treatments.
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Loskutoff, D. J., J. Mimuro, and C. Hekman. "PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644763.

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Plasminogen activation provides an important source of localized proteolytic activity not only during fibrinolysis, but also during ovulation, cell migration, epithelial cell differentiation, tumor invasion and a variety of other physiological processes. Precise regulation of plasminogen activator (PA) activity thus constitutes a critical feature of many biological processes. This control is achieved in large part through the action of specific PA inhibitors (PAIs). Although 4 distinct PAIs have been detected,1the endothelial cellTderived inhibitor (PAI-1) is the only one that efficiently inhibits both urokinase (Kd=2.3×10−13M; Kassoc =1.6×108 M−1s−1) and single-chaintissue-type PA (tPA; Kd=1.3×lO−15 M Kd=3.9×lO7M−1s−1). It also inhibits trypsin (Kassoc=6.8×106M−1 s−1 ) ancl Plasmin (Kassoc=7.6×l05 M−1 s5 Analysis of the effect of PAI-1 on the rate of plasminogen activation revealed a competitive type of inhibition when urokinase was employed but a linear mixed type of inhibition when single chain tPA was employed. These results suggest that the interaction of PAI-1 with tPA, in contrast to its interaction with urokinase, may involve 2 sites on the tPA molecule.PAI-1 has been purified from medium conditioned by cultured bovine aortic endothelial cells and partially characterized. It is a major biosynthetic product of these cells, accounting for as much as 12% of the total protein released by the cells in 24 h. It has an M of 50,000, an isoelectric point of 4.5-5.0, and is immunologically and biochemically related to the rapidly acting inhibitor present in human platelets and in the plasma of some patients at risk to develop thrombotic problems. Although it is relatively stable to conditions which inactivate most protease inhibitors (acid pH, SDS), it is extremely sensitive to oxidants. The molecular cloning of the PAI-1 gene revealed that the mature human protein is 379 amino acids long, contains an NH2-terminal valine, lacks cysteines and has a methionine at the Pi position of it's reactive center. The conversion of this methionine to methionine sulfoxide may be responsible for the rapid inactivation of PAI-1 by oxidants. Human PAI-1 has extensive (30%) homology with α1-antitrypsin and antithrombin III and is thus a member of the serine proteinase inhibitor (serpin) family; a group of related molecules that control the major protease cascades of the blood. The PAI-1 gene is approximately 12.2 kilobase pairs in length and is organized into nine exons and eight introns.The production of PAI-1 by endothelial cells is stimulated by endotoxin, interleukin-1, tumor necrosis factor, and transforming growth factor β(TGFβ). The cells are extremely sensitive to TGFβwith maximal effects (100-fold stimulation) observed with 1-2 ng/ml. These changes were relatively specific for PAI-1, and could be detected at both the protein and the RNA level. Interestingly, TGFgalso stimulated the amount of PAI-1 present in the extracellular matrix (ECM) of BAEs. PAI-1 was one of the primary ECM components of these cells, constituting 10-20% of the ECM proteins detected after SDS-PAGE.One of the most unusual properties of PAI-1 is that it exists in blood and in various cellular samples in both an active and an inactive (latent) form, the ratio depending on the source. The latent form can be converted into the active one by treatment with denaturants like SDS or guanidine-HCl. Although the majority of the cell-associated PAI-1 is active, it rapidly decays (t1/2=3 h) into the latent form once it is released from the cells. In contrast, the half-life of ECM associated PAI-1 was greater than 24 h. These data suggest that PAI-1 is produced by BAEs in an active form, and is then either released into the medium where it is rapidly inactivated, or released into the subendothelium where it binds to ECM. The specific binding of PAI-1 to ECM protects it from this inactivation.
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Cheng, Jeffrey K., Victoria Le, Robert P. Mecham, and Jessica E. Wagenseil. "Mechanics and Modeling of Postnatal Arterial Development in Wild-Type and Elastin-Insufficient Mice." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53140.

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Large arteries in vertebrates serve as elastic reservoirs that store a portion of the blood volume with systole and discharge it during diastole. This function is made possible by the combination of extracellular matrix (ECM) proteins deposited by the smooth muscle cells (SMCs) in the arterial wall. Elastin and collagen expression in mice is first detectable around embryonic day 14 and peaks around postnatal day (P) 14, returning to baseline levels by P30. During this time, pressure and cardiac output increase significantly before leveling off ∼P30 [1]. Hence, the protein amounts and consequent mechanical properties of the arterial wall change simultaneously with the applied hemodynamic loads in a complicated and unknown feedback loop.
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Espinosa, Gabriela, Lisa Bennett, William Gardner, and Jessica Wagenseil. "The Effects of Extracellular Matrix Protein Insufficiency and Treatment on the Stiffness of Arterial Smooth Muscle Cells." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14131.

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Increased arterial stiffness is directly correlated with hypertension and cardiovascular disease. Stiffness of the conducting arteries is largely determined by the extracellular matrix (ECM) proteins in the wall, such as collagen and elastin, produced by the smooth muscle cells (SMCs) found in the medial layer. Elastin is deposited as soluble tropoelastin and is later crosslinked into elastin fibers. Newborn mice lacking the elastin protein ( Eln−/−) have increased arterial wall stiffness and SMCs with altered proliferation, migration and morphology [1]. Vessel elasticity is also mediated by other ECM proteins, such as fibulin-4. Elastic tissue, such as lung, skin, and arteries, from fibulin-4 deficient ( Fbln4−/−) mice show no decrease in elastin content, but have reduced elasticity due to disrupted elastin fibers [2]. Arteries from both elastin and fibulin-4 deficient mice have been previously studied, but the mechanical properties of their SMCs have not been investigated. Recent experiments comparing arterial SMCs from old and young animals suggest that mechanical properties of the SMCs themselves may contribute to changes in wall stiffness [3]. Hence, we investigated the stiffness of isolated arterial SMCs from elastin and fibulin-4 deficient mice using atomic force microscopy (AFM). In addition, we studied the effects of two elastin treatments on the mechanical properties of SMCs from Eln+/+ and Eln−/− mice. Differences between the treatments may elucidate the importance of soluble versus crosslinked elastin on single cell stiffness.
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Reports on the topic "ERM PROTEINS"

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Herman, Eliot D., Gad Galili, and Alan Bennett. Recognition and Disposal of Misfolded Seed Proteins. United States Department of Agriculture, August 1994. http://dx.doi.org/10.32747/1994.7568791.bard.

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This project was directed at determining mechanisms involved in storage of intrinsic and foreign storage proteins in seeds. Seeds constitute the majority of direct and indirect food. Understanding how seeds store proteins is important to design approaches to improve the quality of seed proteins through biotechnology. In the Israeli part of this project we have conducted investigations to elucidate the mechanisms involved in assembling wheat storage proteins into ER-derived protein bodies. The results obtained have shown how domains of storage protein molecules are critical in the assembly of protein bodies. In the US side of this project the fate of foreign and engineered proteins expressed in seeds has been investigated. Engineering seed proteins offers the prospect of improving the quality of crops. Many foreign proteins are unstable when expressed in transgenic seeds. The results obtained have demonstrated that sequestering foreign proteins in the ER or ER-derived protein bodies stabilizes the proteins permitting their accumulation. The collaboration conducted in this project has advanced the understanding how protein bodies are assembled and the potential to use the ER and protein bodies to store engineered proteins that can enhance the composition of seeds.
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Galili, Gad, and Alan Bennett. Role of Molecular Chaperone in Wheat Storage Protein Assembly. United States Department of Agriculture, April 1995. http://dx.doi.org/10.32747/1995.7604926.bard.

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Following sequestration into the ER, wheat gliadins assemble into complexes that initiate the formation of protein bodies. In the present work we have characterized the DNA sequence and regulation of expression of a plant BiP and also studied its interaction with wheat storage proteins as well as its role in the maturation of these storage proteins. In the Israeli lab, immunoprecipitation studies were made using anti BiP and anti storage proteins sera, both in wheat and in transgenic tobacco plants expressing a wheat gliadin storage proteins. In both cases, we could show that BiP interacts with the gliadin storage proteins. In addition, we could show that BiP also played an important role in the initial assembly of the gliadins. In the American lab, the complexity, structure and properties of tomato BiP was characterized at the molecular and biochemical levels. In addition, tomato BiP was also overexpressed in bacteria and the overexpressed protein was found to be active. The cooperative findings of the Israeli and American labs clearly improves our understanding of the structure and expression of a plant BiP as well as its role in the maturation of storage proteins in plants seeds. In addition, it will serve as a foundation for future studies of the mechanisms of BiP function in in vitro studies using purified storage proteins and purified recombinant active BiP.
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Epel, Bernard, and Roger Beachy. Mechanisms of intra- and intercellular targeting and movement of tobacco mosaic virus. United States Department of Agriculture, November 2005. http://dx.doi.org/10.32747/2005.7695874.bard.

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To cause disease, plant viruses must replicate and spread locally and systemically within the host. Cell-to-cell virus spread is mediated by virus-encoded movement proteins (MPs), which modify the structure and function of plasmodesmata (Pd), trans-wall co-axial membranous tunnels that interconnect the cytoplasm of neighboring cells. Tobacco mosaic virus (TMV) employ a single MP for cell- cell spread and for which CP is not required. The PIs, Beachy (USA) and Epel (Israel) and co-workers, developed new tools and approaches for study of the mechanism of spread of TMV that lead to a partial identification and molecular characterization of the cellular machinery involved in the trafficking process. Original research objectives: Based on our data and those of others, we proposed a working model of plant viral spread. Our model stated that MPᵀᴹⱽ, an integral ER membrane protein with its C-terminus exposed to the cytoplasm (Reichel and Beachy, 1998), alters the Pd SEL, causes the Pd cytoplasmic annulus to dilate (Wolf et al., 1989), allowing ER to glide through Pd and that this gliding is cytoskeleton mediated. The model claimed that in absence of MP, the ER in Pd (the desmotubule) is stationary, i.e. does not move through the Pd. Based on this model we designed a series of experiments to test the following questions: -Does MP potentiate ER movement through the Pd? - In the presence of MP, is there communication between adjacent cells via ER lumen? -Does MP potentiate the movement of cytoskeletal elements cell to cell? -Is MP required for cell-to-cell movement of ER membranes between cells in sink tissue? -Is the binding in situ of MP to RNA specific to vRNA sequences or is it nonspecific as measured in vitro? And if specific: -What sequences of RNA are involved in binding to MP? And finally, what host proteins are associated with MP during intracellular targeting to various subcellular targets and what if any post-translational modifications occur to MP, other than phosphorylation (Kawakami et al., 1999)? Major conclusions, solutions and achievements. A new quantitative tool was developed to measure the "coefficient of conductivity" of Pd to cytoplasmic soluble proteins. Employing this tool, we measured changes in Pd conductivity in epidermal cells of sink and source leaves of wild-type and transgenic Nicotiana benthamiana (N. benthamiana) plants expressing MPᵀᴹⱽ incubated both in dark and light and at 16 and 25 ᵒC (Liarzi and Epel, 2005 (appendix 1). To test our model we measured the effect of the presence of MP on cell-to-cell spread of a cytoplasmic fluorescent probe, of two ER intrinsic membrane protein-probes and two ER lumen protein-probes fused to GFP. The effect of a mutant virus that is incapable of cell-to-cell spread on the spread of these probes was also determined. Our data shows that MP reduces SEL for cytoplasmic molecules, dilates the desmotubule allowing cell-cell diffusion of proteins via the desmotubule lumen and reduces the rate of spread of the ER membrane probes. Replicase was shown to enhance cell-cell spread. The data are not in support of the proposed model and have led us to propose a new model for virus cell-cell spread: this model proposes that MP, an integral ER membrane protein, forms a MP:vRNAER complex and that this ER-membrane complex diffuses in the lipid milieu of the ER into the desmotubule (the ER within the Pd), and spreads cell to cell by simple diffusion in the ER/desmotubule membrane; the driving force for spread is the chemical potential gradient between an infected cell and contingent non-infected neighbors. Our data also suggests that the virus replicase has a function in altering the Pd conductivity. Transgenic plant lines that express the MP gene of the Cg tobamovirus fused to YFP under the control the ecdysone receptor and methoxyfenocide ligand were generated by the Beachy group and the expression pattern and the timing and targeting patterns were determined. A vector expressing this MPs was also developed for use by the Epel lab . The transgenic lines are being used to identify and isolate host genes that are required for cell-to-cell movement of TMV/tobamoviruses. This line is now being grown and to be employed in proteomic studies which will commence November 2005. T-DNA insertion mutagenesis is being developed to identify and isolate host genes required for cell-to-cell movement of TMV.
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Blaxter, Tamsin, and Tara Garnett. Primed for power: a short cultural history of protein. TABLE, November 2022. http://dx.doi.org/10.56661/ba271ef5.

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Protein has a singularly prominent place in discussions about food. It symbolises fitness, strength and masculinity, motherhood and care. It is the preferred macronutrient of affluence and education, the mark of a conscientious diet in wealthy countries and of wealth and success elsewhere. Through its association with livestock it stands for pastoral beauty and tradition. It is the high-tech food of science fiction, and in discussions of changing agricultural systems it is the pivotal nutrient around which good and bad futures revolve. There is no denying that we need protein and that engaging with how we produce and consume it is a crucial part of our response to the environmental crises. But discussions of these issues are affected by their cultural context—shaped by the power of protein. Given this, we argue that it is vital to map that cultural power and understand its origins. This paper explores the history of nutritional science and international development in the Global North with a focus on describing how protein gained its cultural meanings. Starting in the first half of the 19th century and running until the mid-1970s, it covers two previous periods when protein rose to singular prominence in food discourse: in the nutritional science of the late-19th century, and in international development in the post-war era. Many parallels emerge, both between these two eras and in comparison with the present day. We hope that this will help to illuminate where and why the symbolism and story of protein outpace the science—and so feed more nuanced dialogue about the future of food.
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Jeffrey J. Regan. Final technical brief / DOE grant DE-FG03-96 ER 62219. Computational study of electron tunneling in proteins. Office of Scientific and Technical Information (OSTI), March 1999. http://dx.doi.org/10.2172/761899.

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Sadigh, B. LDRD Final Report (08-ERD-037): Important Modes to Drive Protein MD Simulations to the Next Conformational Level. Office of Scientific and Technical Information (OSTI), April 2011. http://dx.doi.org/10.2172/1022884.

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Ramamoorthy, Sivapriya. Role of PY Motif Containing Protein, WBP-2 in ER, PR Signaling and Breast Tumorigenesis. Fort Belvoir, VA: Defense Technical Information Center, September 2009. http://dx.doi.org/10.21236/ada534171.

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Ramamoorthy, Sivapriya, and Zafar Nawaz. Role of PY Motif Containing Protein, WBP-2 in ER, PR Signaling and Breast Tumorigenesis. Fort Belvoir, VA: Defense Technical Information Center, March 2009. http://dx.doi.org/10.21236/ada510046.

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Litovchick, Larisa. Functional Characterization of the Protein Product of the Prostate Carcinoma Gene Fusion TMPRSS2:ERG Using the Proteomic and Microarray Analyses. Fort Belvoir, VA: Defense Technical Information Center, July 2009. http://dx.doi.org/10.21236/ada509751.

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Dhananjayan, Sarath C., and Zafar Nawaz. Role of the PY Motif Containing Protein, WBP-2 in ER, PR Signaling and Breast Tumorigenesis. Fort Belvoir, VA: Defense Technical Information Center, March 2008. http://dx.doi.org/10.21236/ada485774.

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