Relevant bibliographies by topics / Glycine-rich proteins

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  2. Dissertations / Theses
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  4. Conference papers

Academic literature on the topic 'Glycine-rich proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 10 February 2022

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Journal articles on the topic "Glycine-rich proteins"

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Mousavi, Amir, and Yasuo Hotta. "Glycine-Rich Proteins: A Class of Novel Proteins." Applied Biochemistry and Biotechnology 120, no. 3 (2005): 169–74. http://dx.doi.org/10.1385/abab:120:3:169.

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Flores Fusaro, Adriana, and Gilberto Sachetto-Martins. "Blooming Time for plant Glycine-Rich Proteins." Plant Signaling & Behavior 2, no. 5 (2007): 386–87. http://dx.doi.org/10.4161/psb.2.5.4262.

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Graham, L. A. "Glycine-Rich Antifreeze Proteins from Snow Fleas." Science 310, no. 5747 (2005): 461. http://dx.doi.org/10.1126/science.1115145.

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Cr�tin, Claude, and Pere Puigdom�nech. "Glycine-rich RNA-binding proteins from Sorghum vulgare." Plant Molecular Biology 15, no. 5 (1990): 783–85. http://dx.doi.org/10.1007/bf00016128.

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Mangeon, Amanda, Ricardo Magrani Junqueira, and Gilberto Sachetto-Martins. "Functional diversity of the plant glycine-rich proteins superfamily." Plant Signaling & Behavior 5, no. 2 (2010): 99–104. http://dx.doi.org/10.4161/psb.5.2.10336.

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Sachetto-Martins, Gilberto, Luciana O. Franco, and Dulce E. de Oliveira. "Plant glycine-rich proteins: a family or just proteins with a common motif?" Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1492, no. 1 (2000): 1–14. http://dx.doi.org/10.1016/s0167-4781(00)00064-6.

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de Oliveira, Dulce E., Jef Seurinck, Dirk Inze, Marc Van Montagu, and Johan Botterman. "Differential Expression of Five Arabidopsis Genes Encoding Glycine-Rich Proteins." Plant Cell 2, no. 5 (1990): 427. http://dx.doi.org/10.2307/3869092.

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de Oliveira, D. E., J. Seurinck, D. Inzé, M. Van Montagu, and J. Botterman. "Differential expression of five Arabidopsis genes encoding glycine-rich proteins." Plant Cell 2, no. 5 (1990): 427–36. http://dx.doi.org/10.1105/tpc.2.5.427.

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de Oliveira, D. E., L. O. Franco, C. Simoens, et al. "Inflorescence-specific genes from Arabidopsis thaliana encoding glycine-rich proteins." Plant Journal 3, no. 4 (1993): 495–507. http://dx.doi.org/10.1046/j.1365-313x.1993.03040495.x.

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Ringli, C., B. Keller, and U. Ryser. "Glycine-rich proteins as structural components of plant cell walls." Cellular and Molecular Life Sciences 58, no. 10 (2001): 1430–41. http://dx.doi.org/10.1007/pl00000786.

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Dissertations / Theses on the topic "Glycine-rich proteins"

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Poersch, Liane Balvedi. "Identificação e caracterização de genes codificantes de proteínas ricas em glicina ligantes de RNA em soja (Glycine max (L.) Merril)." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2011. http://hdl.handle.net/10183/37419.

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A soja constitui uma das culturas mais importantes mundialmente, tanto social quanto economicamente. Consequentemente, informações moleculares sobre processos de desenvolvimento, bem como conhecimento detalhado das interações entre condições estressoras e a resposta da planta a fatores ambientais são necessários. A identificação e caracterização de genes que respondem a condições ambientais específicas constituem um passo inicial no entendimento dos processos adaptativos. Proteínas ricas em glicina (GRPs) são polipeptídeos contendo um grande número do aminoácido glicina em sua estrutura primária. Os genes codificantes de GRPs são regulados ao longo do desenvolvimento e regulados por auxina, ABA, frio, ferimentos, luz, ritmo circadiano, salinidade, seca, patógenos e encharcamento. Entretanto, há pouca informação sobre GRPs de plantas e seus papéis no desenvolvimento e resposta a estresses. As GRPs podem ser divididas em quatro classes (I, II, III, IV) de acordo com sua estrutura primária e presença de domínios característicos. A classe IV é composta por proteínas ligantes de RNA. Domínios adicionais permitem dividir a classe IV de GRPs em quatro subclasses (IVa, IVb, IVc, IVd). A subclasse IVc é representada por proteínas contendo um cold-schock domain (CSD) e dedos de zinco CCHC tipo retrovirais. O objetivo do presente estudo foi: (i) identificar e caracterizar os genes codificantes de classe IV de GRPs, (ii) verificar a padrão de expressão dos genes codificantes da subclasse IVc de GRPs e (iii) produzir plantas de soja transgênicas expressando o gene AtGRP2, o qual foi mostrado estar envolvido na floração e desenvolvimento da semente em Arabidopsis, e também poderia desempenhar um papel na aclimatação ao frio. Um total de 47 genes codificantes da classe IV de GRPs foi identificado no genoma da soja: 19 da subclasse IVa, sete da IVb, seis da IVc e 15 da IVd. Análises in silico indicaram uma expressão preferencial de todos os genes codificantes da subclasse IVc em tecidos em desenvolvimento. Análises de RT-qPCR revelaram que plantas jovens e maduras exibem uma expressão mais alta em folhas do que em outros órgãos, com exceção dos genes GRP2L_4/5 que tiveram expressão mais alta em sementes. GRP2L_4/5 e GRP2L_2 foram induzidos em resposta a baixas temperaturas. Sob estresse com ABA a expressão de todos os genes foi reprimida em folhas e/ou raízes, com exceção do gene GRP2L_2 que foi induzido em raízes. Em resposta a infecção com Phakopsora pachyrhizi, a expressão de GRP2L_2 e GRP2L_3 foi mais alta e precoce no genótipo suscetível quando comparada com o resistente, enquanto que a resposta de GRP2L_4/5 e GRP2L_6 foi mais tardia no genótipo resistente. Ainda, embriões somáticos secundários das cultivares Bragg, IAS-5 e BRSMG 68 Vencedora de soja foram usados para introduzir o gene AtGRP2 no genoma da soja por bombardeamento e sistema bombardeamento/Agrobacterium. Seis eventos de transformação independentes foram confirmados por PCR. No presente momento as plantas estão em desenvolvimento em frascos de vidro. No presente estudo a classe IV de GRPs em soja foi identificada e caracterizada. Este é o primeiro passo para elucidar o papel destas proteínas em plantas.
Molecular information on plant developmental process, as well as detailed knowledge of the interaction between stress conditions and plant response to environmental factors are essential for understanding the adaptive response. Glycine-Rich Proteins (GRP) have the amino acid glycine well represented in their primary structure. The genes encoding GRPs are developmentally regulated and induced by auxin, ABA, cold, wound, light, circadian rhythm, salinity, drought, pathogens, and flooding. However, there is scarce information about plant GRPs and its role on development and stress response. The GRPs can be divided into four classes (I, II, II and IV) according to their primary structure and the presence of characteristic domains. Class IV is composed by RNA-binding proteins. Additional domains permit to split class IV GRPs into four subclasses (IVa, IVb, IVc and IVd). Subclass IVc is represented by proteins containing a Cold-Shock Domain (CSD) and retroviral-like CCHC zinc fingers. The goal of the present study was: (i) to identify and characterize the genes encoding class IV GRPs, (ii) to verify the relative expression of genes encoding subclass IVc GRPs and (iii) to produce transgenic soybean plants expressing the AtGRP2 gene, which was shown to be involved in Arabidopsis flower and seed development, and can also play a role in cold acclimation. A total of 47 genes encoding class IV GRPs were found in the soybean genome: 19 from IVa, seven from IVb, six from IVc and 15 from IVd subclasses. In silico analyses indicated a preferential expression of all genes encoding subclass IVc GRPs in tissues under development. RT-qPCR analyses revealed that both young and mature plants exhibit relative higher expression of subclass IVc GRPs in leaves than in other organs, with exception of GRP2L_4/5 genes that have higher expression in seeds. The GRP2L_4/5 and GRP2L_2 were up-regulated in response to low temperatures. Under ABA stress the expression of all genes was down-regulated in leaves and roots, with exception of GRP2L_2 gene that was up-regulated in roots. In response to Phakopsora pachyrhizi infection, GRP2L_2 and GRP2L_3 expression was higher and earlier in the susceptible genotype when compared with that of the resistant one, while GRP2L_4/5 and GRP2_6 respond later in the resistant genotype. Furthermore, secondary somatic embryos of Bragg, IAS-5 and BRSMG 68 Vencedora soybean cultivars were used to introduce the AtGRP2 gene into the soybean genome by particle bombardment and bombardment/Agrobacterium system. Six independent Bragg transformation events were confirmed by PCR. In the present moment the plants are under development in glass flasks. In the present study the soybean class IV GRPs were identified and characterized. This is the first step to elucidate the role of these proteins in plants.
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Tao, Titus. "Functional characterization of ZmGRP5, a glycine-rich protein specifically expressed in the cell wall of maize silk tissue." Thesis, University of Ottawa (Canada), 2004. http://hdl.handle.net/10393/26780.

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Silk tissue is a specialized reproductive tissue of the maize plant, equivalent to the stigma and style portion of the female inflorescence. The moist and nutrient rich properties of maize silk tissue that facilitate pollen reception and the support of pollen tube growth also make maize silk a preferred site of infection by fungal pathogens such as Fusarium graminearum. The cDNA clone zmgrp5 was isolated in a previous study to identify silk tissue-specific genes. ZmGRP5, the encoded protein, was predicted to be a cell wall glycine-rich protein (GRP) and was experimentally characterized in this study. Using polyclonal antiserum, immunoblot analysis confirmed the silk tissue specificity of the protein. Additionally, subcellular fractionation studies confirmed ZmGRP5 localization in the cell wall fraction, and not in any other subcellular fractions. Interaction of ZmGRP5 with the cell wall matrix was observed to be disrupted by the addition of the reducing agent beta-ME. The reversible nature of disulfide bond formation and disruption under different redox conditions suggest that ZmGRP5 could potentially be important in the regulation of cell wall structural properties such as elasticity and rigidity in accordance with environmental and developmental changes. The variable immobilization of ZmGRP5 to the cell wall matrix could also serve as a potential mechanism of activation or inactivation of any non-structural functions. The identification of potential post-translational modifications such as phosphorylation and glycosylation, which are rarely observed in other cell wall GRPs, suggest that the functional significance of these modifications in ZmGRP5 is worthy of further study.
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Yeh, Yuh-Ying. "The regulation of Atg1 protein kinase activity is important to the autophagy process in Saccharomyces cerevisiae." The Ohio State University, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=osu1290439442.

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Stracovsky, Lynne, and 石凌. "Functional Study of Two Glycine Rich Proteins under Abiotic Stress and during Development in Arabidopsis." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/62m4p4.

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碩士
國立臺灣大學
植物科學研究所
106
Although glycine rich proteins (GRPs) in plants were isolated nearly 30 years ago, much remains unknown about their function. Previously studied GRPs have been found to have diverse localization and functions, as well as diverse quasi-repetitive glycine repeats. Arabidopsis glycine rich proteins AtGRP11 and AtGRP12 are characterized by 6.5% and 26.5% glycine content, respectively. We have functionally characterized these two proteins to better understand their roles. The results indicated that AtGRP11 and AtGRP12 are localized to the cell wall, and AtGRP11 is also localized to the nucleus. Tissue expression analysis revealed that AtGRP11 is expressed in the vascular tissue at various developmental stages of vegetative plant growth. AtGRP11-knockdown and AtGRP12-knockout mutant plants show shorter and longer root lengths, respectively, as compared to wild-type plants. Both AtGRP11 and AtGRP12 are induced by 37℃ heat, and AtGRP11 is also induced by 0℃ cold and salinity stresses. Moreover, analysis of germination rates and cotyledon greening in mutants indicate that AtGRP11 and AtGRP12 participate in abscisic acid (ABA) and salinity stress responses. Lastly, AtGRP12 was found to play a role in basal thermotolerance. This study shows that AtGRP11 and AtGRP12 are cell wall proteins that are induced by various abiotic stresses, and which possibly serve structural functions.
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Monaghan, Erin Kelly Sathe Shridhar K. "Enzyme linked immunosorbent assay (ELISA) for detection of sulfur-rich protein (SRP) in Soybeans (Glycine Max L.) and certain other edible plant seeds." 2003. http://etd.lib.fsu.edu/theses/available/etd-08282003-181925.

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Thesis (M.S.)--Florida State University, 2003.
Advisor: Dr. Shridhar K. Sather, Florida State University, College of Human Sciences, Dept. of Nutriton, Food and Excercise Sciences. Title and description from dissertation home page (viewed 5/4/04). Includes bibliographical references.
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Lin, Chia-Hua, and 林家華. "Characterization and functional studies of a plant class II glycine-rich protein LsGRP1 in plant defense." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/53815589109654474742.

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博士
國立臺灣大學
植物病理與微生物學研究所
102
Salicylic acid- and Botrytis elliptica-inducible defense-related LsGRP1 gene in lily presumably encodes a plant class II glycine-rich protein (GRP). In this study, the results of western blot detection and tandem mass spectrometer analysis revealed that three LsGRP1 variants of 14, 16 and 23 kDa expressed in the leaves of lily specifically, and the expression of 14 and 16 kDa LsGRP1 remained a similar level at different growth stages while the amount of 23 kDa LsGRP1 decreased at the senescence stage. As investigated by immunohistochemistry, LsGRP1 was found to accumulate in the epidermal and the phloem tissues of leaves. The subcellular localization assayed by EGFP imaging and protein extraction analysis revealed that 14 kDa LsGRP1 was located in the plasma membrane whereas 16 and 23 kDa LsGRP1 were weakly bound to the cell wall. Additionally, the accumulation of 14 kDa LsGRP1 and ubiquitin antibody-recognizable 23 kDa LsGRP1 was triggered by salicylic acid and B. elliptica, suggesting that 23 kDa LsGRP1 comes from mono-ubiquitinated 14 kDa LsGRP1 and is related to the occurrence of induced resistance in lily. This is a novel trait never reported for other plant class II GRPs. On the other hand, the failure in LsGRP1 expression using Escherichia coli system suggested the presence of antimicrobial activity in certain region of LsGRP1, and LsGRP1C corresponding to the cysteine-rich C-terminal region was considered an antimicrobial peptide according to its broad-spectrum and effective antimicrobial activity as assayed using chemically synthesized LsGRP1-derived peptides. Furthermore, the inhibition effect of LsGRP1C on fungal growth is possibly via alteration of the integrity of cell membrane and induction of programmed cell death-like phenomenon as revealed by SYTOX Green, H2DCFDA and DAPI staining assays. Moreover, immunofluorescence of LsGRP1C present at the outer layer of fungal cells was indicated and implied that plant cell surface-localized LsGRP1 might retard pathogen via the antimicrobial activity conferred by its C-terminal region. Thus, defense-related LsGRP1 playing an important role in the induced resistance of lily against B. elliptica was assumed; in addition, LsGRP1C derived from LsGRP1 is an antimicrobial peptide with a potential for practical use.
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Book chapters on the topic "Glycine-rich proteins"

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Jiménez-Bremont, Juan Francisco, Maria Azucena Ortega-Amaro, Itzell Eurídice Hernández-Sánchez, Alma Laura Rodriguez-Piña, and Israel Maruri-Lopez. "Plant Glycine-Rich Proteins and Abiotic Stress Tolerance." In Metabolic Adaptations in Plants During Abiotic Stress. CRC Press, 2018. http://dx.doi.org/10.1201/b22206-17.

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Inglis, Adam S., J. Morton Gillespie, Charles M. Roxburgh, Lois A. Whittaker, and Franca Casagranda. "Sequence of a Glycine-Rich Protein from Lizard Claw: Unusual Dilute Acid and Heptafluorobutyric Acid Cleavages." In Proteins. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1787-6_77.

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Olson, Mark O. J., Tamba S. Dumbar, S. V. V. Rao, and Michael O. Wallace. "Determination of the Location of NG, NG-Dimethylarginine in a Glycine-Rich Region of Nucleolar Protein C23." In Proteins. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1787-6_72.

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Dobritsa, S. V., C. M. Maillet, and B. C. Mullin. "Novel Nodule-Specific Glycine- and Histidine-Rich Proteins Expressed in the Zone of Infection of Actinorhizal Nodules may be Multimeric Metal-Binding Proteins." In Nitrogen Fixation: From Molecules to Crop Productivity. Springer Netherlands, 2000. http://dx.doi.org/10.1007/0-306-47615-0_258.

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Znój, Anna, Katarzyna Zientara-Rytter, Paweł Sęktas, Grzegorz Moniuszko, Agnieszka Sirko, and Anna Wawrzyńska. "A Glycine-Rich Protein Encoded by Sulfur-Deficiency Induced Gene Is Involved in the Regulation of Callose Level and Root Elongation." In Proceedings of the International Plant Sulfur Workshop. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-56526-2_21.

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Sivakumar, K. "Computational Analysis and Characterization of Marfan Syndrome Associated Human Proteins." In Biocomputation and Biomedical Informatics. IGI Global, 2010. http://dx.doi.org/10.4018/978-1-60566-768-3.ch009.

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Novel computational procedures and methods have been used to analyze, characterize and to provide more detailed definition of some Marfan syndrome associated human Fibrillin 1 proteins retrieved from NCBI Entrez protein database. Primary structure analysis reveals that the Marfan syndrome associated proteins are rich in cysteine and glycine residues. Extinction Coefficients of Marfan syndrome associated proteins at 280nm is ranging from 1490 to 259165 M-1 cm-1. Expasy’s ProtParam classifies most of the Marfan syndrome associated human Fibrillin 1 proteins as unstable on the basis of Instability index (II>40) and few proteins (AAB25244.1, 1EMO_A, Q504W9) as stable (II
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Condit, Carol M., and Beat Keller. "The Glycine-Rich Cell Wall Proteins of Higher Plants." In Organization and Assembly of Plant and Animal Extracellular Matrix. Elsevier, 1990. http://dx.doi.org/10.1016/b978-0-12-044060-3.50009-1.

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"The Functions of Glycine-Rich Regions in TDP-43, FUS and Related RNA-Binding Proteins." In RNA Binding Proteins. CRC Press, 2012. http://dx.doi.org/10.1201/9781498713368-9.

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Rodriguez-Pascual, Fernando. "The Evolutionary Origin of Elastin: Is Fibrillin the Lost Ancestor?" In Extracellular Matrix - Developments and Therapeutics [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.95411.

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Elastin is the extracellular matrix protein providing large arteries, lung parenchyma and skin with the properties of extensibility and elastic recoil. Within these tissues, elastin is found as a polymer formed by tropoelastin monomers assembled and cross-linked. In addition to specific protein regions supporting the covalent cross-links, tropoelastin is featured by the presence of highly repetitive sequences rich in proline and glycine making up the so-called hydrophobic domains. These protein segments promote structural flexibility and disordered protein properties, a fundamental aspect to explain its elastomeric behavior. Unlike other matrix proteins such as collagens or laminins, elastin emerged relatively late in evolution, appearing at the divergence of jawed and jawless fishes, therefore present in all species from sharks to humans, but absent in lampreys and other lower chordates and invertebrates. In spite of an intense interrogation of the key aspects in the evolution of elastin, its origin remains still elusive and an ancestral protein that could give rise to a primordial elastin is not known. In this chapter, I review the main molecular features of tropoelastin and the available knowledge on its evolutionary history as well as establish hypotheses for its origin. Considering the remarkable similarities between the hydrophobic domains of the first recognizable elastin gene from the elasmobranch Callorhinchus milii with certain fibrillin regions from related fish species, I raise the possibility that fibrillins might have provided protein domains to an ancestral elastin that thereafter underwent significant evolutionary changes to give the elastin forms found today.
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Levitan, Irwin B., and Leonard K. Kaczmarek. "Neurotransmitters and Neurohormones." In The Neuron. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199773893.003.0010.

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A multitude of chemicals called neurotransmitters mediate intercellular communication in the nervous system. These include acetylcholine, the catecholamines, serotonin, glutamate, GABA, glycine, and a wide variety of neuropeptides. Although they exhibit great diversity in many of their properties, all are stored in vesicles in nerve terminals and are released to the extracellular space via a process requiring calcium ions. Their actions are terminated by reuptake into the presynaptic terminal or nearby glial cells by specific transporter proteins or by their destruction in the extracellular space. The role of neurotransmitters is to alter the properties—chemical, electrical, or both—of some target cell. With the arrival on the scene of the neuropeptides, it has become evident that signaling in the nervous system occurs through the use of rich and varied forms of chemical currency, and that some neurons use more than one type of currency simultaneously.
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Conference papers on the topic "Glycine-rich proteins"

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Myers, Corinne, Kristin Bergmann, Chang-Yu Sun, et al. "EXCEPTIONAL PRESERVATION OF GLYCINE-RICH PROTEINS AND SHELL ULTRASTRUCTURE IN PINNID BIVALVES." In GSA Annual Meeting in Seattle, Washington, USA - 2017. Geological Society of America, 2017. http://dx.doi.org/10.1130/abs/2017am-307099.

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Lin, Chia-Hua. "Evidence of LsGRP1, a class II glycine-rich protein of Lilium, involving in plant growth-defense tradeoffs." In ASPB PLANT BIOLOGY 2020. ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1049091.

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