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Relevant bibliographies by topics / Proteine non histone

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Academic literature on the topic 'Proteine non histone'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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Journal articles on the topic "Proteine non histone"

1

Traub, Peter, Georg Perides, Siegfried Kühn, and Annemarie Scherbarth. "Interaction in vitro of Non-Epithelial Intermediate Filament Proteins with Histones." Zeitschrift für Naturforschung C 42, no. 1-2 (February 1, 1987): 47–63. http://dx.doi.org/10.1515/znc-1987-1-209.

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Abstract Non-epithelial intermediate filament (IF) subunit proteins show a high and specific affinity for core histones at physiological ionic strength. When IF proteins are titrated with a mixture of core histones and linker histone H1, in general the latter is totally excluded from com plexation and in the adducts formed the moderately-arginine-rich histones H2A and H2B are progressively replaced by the very-arginine-rich histones H3 and H4. At histone saturation, 2 molecules of nonneuronal IF protein bind 1 histone HI molecule or 8 core histone m olecules, whereas due to its glutamic acid rich, C terminal extensions one dimer of thp 68 kD npnrofilament nrotein associates with 3 molecules of histone H1 or 24 molecules of core histones. The salt stability of the insoluble association products is dependent on the amount and arginine content of the constituent histone species. Rem oval of the non-α-helical N- and C-terminal polypeptides from IF proteins by partial chymotryptic digestion does not affect their histone-binding characteristics. Since core histones are only partially inactivated by limited tryptic digestion, they also appear to react through their a-helix-rich central domains; the limit peptide derived from histone H1 is com pletely inactive at physiological ionic strength. Affinity chromatography of rod domains of IF proteins on core histone-Sepharose 4B and of histones and their limit peptides on vim entin-Sepharose 4B has shown that the interactions involving fractions of histones H3 and H4 are extrem ely resistant to salt and can be dissociated only with arginine or salt under denaturing conditions. In general, the experim ental results revealed close parallels between the association of histones with IF proteins and their interaction with DNA.

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Al-Hamashi, Ayad A., Krystal Diaz, and Rong Huang. "Non-Histone Arginine Methylation by Protein Arginine Methyltransferases." Current Protein & Peptide Science 21, no. 7 (September 23, 2020): 699–712. http://dx.doi.org/10.2174/1389203721666200507091952.

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Protein arginine methyltransferase (PRMT) enzymes play a crucial role in RNA splicing, DNA damage repair, cell signaling, and differentiation. Arginine methylation is a prominent posttransitional modification of histones and various non-histone proteins that can either activate or repress gene expression. The aberrant expression of PRMTs has been linked to multiple abnormalities, notably cancer. Herein, we review a number of non-histone protein substrates for all nine members of human PRMTs and how PRMT-mediated non-histone arginine methylation modulates various diseases. Additionally, we highlight the most recent clinical studies for several PRMT inhibitors.

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Kumar, Amish, and Gitanjali Yadav. "Shared ancestry of core-histone subunits and non-histone plant proteins containing the Histone Fold Motif (HFM)." Journal of Bioinformatics and Computational Biology 19, no. 02 (April 2021): 2140001. http://dx.doi.org/10.1142/s0219720021400011.

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The three helical Histone Fold Motif (HFM) of core histone proteins provides an evolutionarily favored site for the protein–DNA interface. Despite significant variation in sequence, the HFM retains a distinctive structural fold that has diversified into several non-histone protein families. In this work, we explore the ancestry of non-histone HFM containing families in the plant kingdom. A sequence search algorithm was developed using iterative profile Hidden Markov Models to identify remote homologs of core-histone proteins. The resulting hits were functionally annotated, classified into families, and subjected to comprehensive phylogenetic analyses via Maximum likelihood and Bayesian methods. We have identified 4390 HFM containing proteins in the plant kingdom that are not histones, mostly existing as diverse transcription factor families, distributed widely within and across taxonomic groups. Patterns of homology suggest that core histone subunit H2A has evolved into newer families like NF-YC and DRAP1, whereas the H2B subunit of core histones shares a common ancestry with NF-YB and DR1 class of TFs. Core histone subunits H3 and H4 were found to have evolved into DPE and TAF proteins, respectively. Taken together these results provide insights into diversification events during the evolution of the HFM, including sub-functionalization and neo-functionalization of the HFM.

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Gong, Ping, Yuetong Wang, and Yongkui Jing. "Apoptosis Induction byHistone Deacetylase Inhibitors in Cancer Cells: Role of Ku70." International Journal of Molecular Sciences 20, no. 7 (March 30, 2019): 1601. http://dx.doi.org/10.3390/ijms20071601.

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Histone deacetylases (HDACs) are a group of enzymes that regulate gene transcription by controlling deacetylation of histones and non-histone proteins. Overexpression of HDACs is found in some types of tumors and predicts poor prognosis. Five HDAC inhibitors are approved for the treatment of cutaneous T-cell lymphoma, peripheral T-cell lymphoma, and multiple myeloma. Treatment with HDAC inhibitors regulates gene expression with increased acetylated histones with unconfirmed connection with therapy. Apoptosis is a key mechanism by which HDAC inhibitors selectively kill cancer cells, probably due to acetylation of non-histone proteins. Ku70 is a protein that repairs DNA breaks and stabilizes anti-apoptotic protein c-FLIP and proapoptotic protein Bax, which is regulated by acetylation. HDAC inhibitors induce Ku70 acetylation with repressed c-FLIP and activated Bax in cancer cells. Current studies indicate that Ku70 is a potential target of HDAC inhibitors and plays an important role during the induction of apoptosis.

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Xu, Qiutao, Qian Liu, Zhengting Chen, Yaping Yue, Yuan Liu, Yu Zhao, and Dao-Xiu Zhou. "Histone deacetylases control lysine acetylation of ribosomal proteins in rice." Nucleic Acids Research 49, no. 8 (April 9, 2021): 4613–28. http://dx.doi.org/10.1093/nar/gkab244.

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Abstract Lysine acetylation (Kac) is well known to occur in histones for chromatin function and epigenetic regulation. In addition to histones, Kac is also detected in a large number of proteins with diverse biological functions. However, Kac function and regulatory mechanism for most proteins are unclear. In this work, we studied mutation effects of rice genes encoding cytoplasm-localized histone deacetylases (HDAC) on protein acetylome and found that the HDAC protein HDA714 was a major deacetylase of the rice non-histone proteins including many ribosomal proteins (r-proteins) and translation factors that were extensively acetylated. HDA714 loss-of-function mutations increased Kac levels but reduced abundance of r-proteins. In vitro and in vivo experiments showed that HDA714 interacted with r-proteins and reduced their Kac. Substitutions of lysine by arginine (depleting Kac) in several r-proteins enhance, while mutations of lysine to glutamine (mimicking Kac) decrease their stability in transient expression system. Ribo-seq analysis revealed that the hda714 mutations resulted in increased ribosome stalling frequency. Collectively, the results uncover Kac as a functional posttranslational modification of r-proteins which is controlled by histone deacetylases, extending the role of Kac in gene expression to protein translational regulation.

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Bertos, Nicholas R., Audrey H. Wang, and Xiang-Jiao Yang. "Class II histone deacetylases: Structure, function, and regulation." Biochemistry and Cell Biology 79, no. 3 (June 1, 2001): 243–52. http://dx.doi.org/10.1139/o01-032.

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Acetylation of histones, as well as non-histone proteins, plays important roles in regulating various cellular processes. Dynamic control of protein acetylation levels in vivo occurs through the opposing actions of histone acetyltransferases and histone deacetylases (HDACs). In the past few years, distinct classes of HDACs have been identified in mammalian cells. Class I members, such as HDAC1, HDAC2, HDAC3, and HDAC8, are well-known enzymatic transcriptional corepressors homologous to yeast Rpd3. Class II members, including HDAC4, HDAC5, HDAC6, HDAC7, and HDAC9, possess domains similar to the deacetylase domain of yeast Hda1. HDAC4, HDAC5, and HDAC7 function as transcriptional corepressors that interact with the MEF2 transcription factors and the N-CoR, BCoR, and CtBP corepressors. Intriguingly, HDAC4, HDAC5, and probably HDAC7 are regulated through subcellular compartmentalization controlled by site-specific phosphorylation and binding of 14-3-3 proteins; the regulation of these HDACs is thus directly linked to cellular signaling networks. Both HDAC6 and HDAC9 possess unique structural modules, so they may have special biological functions. Comprehension of the structure, function, and regulation of class II deacetylases is important for elucidating how acetylation regulates functions of histones and other proteins in vivo.Key words: histone acetylation, protein acetylation, histone deacetylase, 14-3-3 proteins.

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Li, Hong-Tao, Ting Gong, Zhen Zhou, Yu-Ting Liu, Xiongwen Cao, Yongning He, Charlie Degui Chen, and Jin-Qiu Zhou. "Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro." Biochemical Journal 467, no. 3 (April 17, 2015): 507–15. http://dx.doi.org/10.1042/bj20141437.

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Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate protein arginine residues. PRMTs’ substrates include histones and a variety of non-histone proteins. Previous studies have shown that yeast Hmt1 is a type I PRMT and methylates histone H4 arginine 3 and several mRNA-binding proteins. Hmt1 forms dimers or oligomers, but how dimerization or oligomerization affects its activity remains largely unknown. We now report that Hmt1 can methylate histone H3 arginine 2 (H3R2) in vitro. The dimerization but not hexamerization is essential for Hmt1’s activity. Interestingly, the methyltransferase activity of Hmt1 on histone H3R2 requires reciprocal contributions from two Hmt1 molecules. Our results suggest an intermolecular trans-complementary mechanism by which Hmt1 dimer methylates its substrates.

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Yu, Yucong, Hong Wen, and Xiaobing Shi. "Histone mimics: more tales to read." Biochemical Journal 478, no. 14 (July 23, 2021): 2789–91. http://dx.doi.org/10.1042/bcj20210357.

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Post-translational modifications (PTMs) on histone proteins are known as epigenetic marks that demarcate the status of chromatin. These modifications are ‘read' by specific reader proteins, which in turn recruit additional factors to modulate chromatin accessibility and the activity of the underlying DNA. Accumulating evidence suggests that these modifications are not restricted solely to histones, many non-histone proteins may function in a similar way through mimicking the histones. In this commentary, we briefly discuss a systematic study of the discovery of histone H3 N-terminal mimicry proteins (H3TMs), and their implications in chromatin regulation and drug discoveries.

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WONDRAK, Georg T., Daniel CERVANTES-LAUREAN, Elaine L. JACOBSON, and Myron K. JACOBSON. "Histone carbonylation in vivo and in vitro." Biochemical Journal 351, no. 3 (October 24, 2000): 769–77. http://dx.doi.org/10.1042/bj3510769.

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Non-enzymic damage to nuclear proteins has potentially severe consequences for the maintenance of genomic integrity. Introduction of carbonyl groups into histones in vivo and in vitro was assessed by Western blot immunoassay and reductive incorporation of tritium from radiolabelled NaBH4 (sodium borohydride). Histone H1 extracted from bovine thymus, liver and spleen was found to contain significantly elevated amounts of protein-bound carbonyl groups as compared with core histones. The carbonyl content of nuclear proteins of rat pheochromocytoma cells (PC12 cells) was not greatly increased following oxidative stress induced by H2O2, but was significantly increased following alkylating stress induced by N-methyl-N´-nitro-N-nitrosoguanidine or by combined oxidative and alkylating stress. Free ADP-ribose, a reducing sugar generated in the nucleus in proportion to DNA strand breaks, was shown to be a potent histone H1 carbonylating agent in isolated PC12 cell nuclei. Studies of the mechanism of histone H1 modification by ADP-ribose indicate that carbonylation involves formation of a stable acyclic ketoamine. Our results demonstrate preferential histone H1 carbonylation in vivo, with potentially important consequences for chromatin structure and function.

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Demyanenko, Svetlana, and Svetlana Sharifulina. "The Role of Post-Translational Acetylation and Deacetylation of Signaling Proteins and Transcription Factors after Cerebral Ischemia: Facts and Hypotheses." International Journal of Molecular Sciences 22, no. 15 (July 26, 2021): 7947. http://dx.doi.org/10.3390/ijms22157947.

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Histone deacetylase (HDAC) and histone acetyltransferase (HAT) regulate transcription and the most important functions of cells by acetylating/deacetylating histones and non-histone proteins. These proteins are involved in cell survival and death, replication, DNA repair, the cell cycle, and cell responses to stress and aging. HDAC/HAT balance in cells affects gene expression and cell signaling. There are very few studies on the effects of stroke on non-histone protein acetylation/deacetylation in brain cells. HDAC inhibitors have been shown to be effective in protecting the brain from ischemic damage. However, the role of different HDAC isoforms in the survival and death of brain cells after stroke is still controversial. HAT/HDAC activity depends on the acetylation site and the acetylation/deacetylation of the main proteins (c-Myc, E2F1, p53, ERK1/2, Akt) considered in this review, that are involved in the regulation of cell fate decisions. Our review aims to analyze the possible role of the acetylation/deacetylation of transcription factors and signaling proteins involved in the regulation of survival and death in cerebral ischemia.

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Dissertations / Theses on the topic "Proteine non histone"

1

Bonne-Andrea, Catherine. "Contribution à l'étude des propriétés et du rôle biologique de la protéine non-histone HMG1." Paris 6, 1986. http://www.theses.fr/1986PA066451.

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Durand, Jean-Pierre. "Contribution a l'etude du groupe des proteines nucleaires de faible mobilite electrophoretique (lmg)." Nantes, 1988. http://www.theses.fr/1988NANT2010.

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Smith, Marissa B. "Using gain of function genetics to explore the role of non-histone chromosomal protein D1 in Drosophila melanogaster." Morgantown, W. Va. : [West Virginia University Libraries], 2007. https://eidr.wvu.edu/etd/documentdata.eTD?documentid=5533.

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Thesis (M.S.)--West Virginia University, 2007.
Title from document title page. Document formatted into pages; contains vii, 124 p. : ill. (some col.). Includes abstract. Includes bibliographical references (p. 116-124).

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4

Simpson, Andrew. "Non-histone protein HMG-2A and chromatin structure." Thesis, University of Cambridge, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.359813.

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Yuan, Zhigang. "Functional characterization of roles of histone deacetylases in the regulation of DNA damage response." [Tampa, Fla.] : University of South Florida, 2007. http://purl.fcla.edu/usf/dc/et/SFE0002175.

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6

Collins, Kimberly A. "Characterization of the budding yeast centromeric histone H3 variant, Cse4 /." Thesis, Connect to this title online; UW restricted, 2006. http://hdl.handle.net/1773/5011.

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7

Novak, Ivana. "Molecular architecture of meiotic chromosomes /." Stockholm, 2006. http://diss.kib.ki.se/2006/91-7140-959-9/.

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Bonne-Andrea, Catherine. "Contribution à l'étude des propriétés et du rôle biologique de la protéine non-histone HMG1." Grenoble 2 : ANRT, 1986. http://catalogue.bnf.fr/ark:/12148/cb37596144d.

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9

SALA-ROVIRA, MONTSERRAT. "Caracterisation et clonage des proteines nucleaires basiques non-histones chez le dinoflagelle crypthecodinium cohnii." Paris 6, 1991. http://www.theses.fr/1991PA066321.

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Les protistes dinoflagelles (pyrrhophytes) representent la seule classe d'eucaryotes dont la chromatine est depourvue d'histones et de nucleosomes. Les proteines nucleaires basiques ont ete caracterisees et leurs proprietes dna-binding demontrees in vivo et in vitro chez l'espece crythecodinium cohnii. La famille des proteines hcc de 14kda qui represente environ 30% de proteines basiques a ete plus particulierement analysee. La fabrication et la purification d'un anticorps polyclonal dirige contre hcca permis d'isoler des clones de cdna codant pour cette proteine a partir d'une banque d'expression. L'analyse de leur sequence nucleotidique a revele deux variants presentent une homologie de 77%. Les proteines hcc ont ete immunolocalises sur coupes, en microscopie optique et electronique. Elles sont detectees preferentiellement a la peripherique des chromosomes et dans la nucleole. Cette localisation dans des regions activement transcrites suggere que les proteines basiques hcc, dont la fonction n'est pas encore connue, pourraient intervenir dans les premiers stades de l'expression genetique ou dans l'organisation de la chromatine active

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Böhm, Stefanie. "Non-protein-coding RNA : Transcription and regulation of ribosomal RNA." Doctoral thesis, Stockholms universitet, Institutionen för molekylär biovetenskap, Wenner-Grens institut, 2014. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-102718.

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Cell growth and proliferation are processes in the cell that must be tightly regulated. Transcription of ribosomal RNA and ribosomal biogenesis are directly linked to cell growth and proliferation, since the ribosomal RNA encodes for the majority of transcription in a cell and ribosomal biogenesis influences directly the number of proteins that are synthesized. In the work presented in this thesis, we have investigated the ribosomal RNA genes, namely the ribosomal DNA genes and the 5S rRNA genes, and their transcriptional regulation. One protein complex that is involved in RNA polymerase I and III transcription is the chromatin remodelling complex B‑WICH (WSTF, SNF2h, NM1). RNA polymerase I transcribes the rDNA gene, while RNA polymerase III transcribes the 5S rRNA gene, among others. In Study I we determined the mechanism by which B‑WICH is involved in regulating RNA polymerase I transcription. B‑WICH is associated with the rDNA gene and was able to create a more open chromatin structure, thereby facilitating the binding of HATs and the subsequent histone acetylation. This resulted in a more active transcription of the ribosomal DNA gene. In Study II we wanted to specify the role of NM1 in RNA polymerase I transcription. We found that NM1 is not capable of remodelling chromatin in the same way as B‑WICH, but we demonstrated also that NM1 is needed for active RNA polymerase I transcription and is able to attract the HAT PCAF. In Study III we investigated the intergenic part of the ribosomal DNA gene. We detected non-coding RNAs transcribed from the intergenic region that are transcribed by different RNA polymerases and that are regulated differently in different stress situations. Furthermore, these ncRNAs are distributed at different locations in the cell, suggesting that they have different functions. In Study IV we showed the involvement of B‑WICH in RNA Pol III transcription and, as we previously had shown in Study I, that B‑WICH is able to create a more open chromatin structure, in this case by acting as a licensing factor for c-Myc and the Myc/Max/Mxd network. Taken together, we have revealed the mechanism by which the B‑WICH complex is able to regulate RNA Pol I and Pol III transcription and we have determined the role of NM1 in the B‑WICH complex. We conclude that B‑WICH is an important factor in the regulation of cell growth and proliferation. Furthermore, we found that the intergenic spacer of the rDNA gene is actively transcribed, producing ncRNAs. Different cellular locations suggest that the ncRNAs have different functions.

At the time of the doctoral defence the following papers were unpublished and had a status as follows: Paper 2: Manuscript; Paper 3: Manuscript

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Books on the topic "Proteine non histone"

1

Chen, Hsiao Ying. Molecular studies of a non-histone chromatin protein B2. Ottawa: National Library of Canada, 1990.

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2

Ciavolella, Paul Edward. The purification and characterization of a developmentally regulated myocardial non-histone nuclear protein and the isolation of a cDNA clone of unknown function which is developmentally expressed. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1991.

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3

Davide, Viterbo, ed. Un rabbino tunisino nei ghetti del Regno di Sardegna 1818-1830: Gli ebrei non lo gradiscono ma la corte lo protegge. Firenze: Giuntina, 2006.

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4

Isaac, Bekhor, Mirell Carol J, and Liew C. C, eds. Progress in nonhistone protein research. Boca Raton, Fla: CRC Press, 1985.

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5

Lehn, Donald Andrew. The non-histone chromosomal protein HMG-I(Y) and its interactions with nucleic acids. 1989.

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6

Emery, Alan E. H., and Marcia L. H. Emery. The history of muscular dystrophy: a unique story. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199591473.003.0001.

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Chapter 1 discusses the history of Duchenne muscular dystrophy, a serious condition and the second most common genetic disorder in many countries. Its cause was unknown until relatively recently and there has been no effective treatment. However, the responsible gene and its protein product have now been identified and gene therapy is under serious consideration.

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Lucchesi, John C. Epigenetics, Nuclear Organization & Gene Function. Oxford University Press, 2019. http://dx.doi.org/10.1093/oso/9780198831204.001.0001.

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Epigenetics is the study of heritable changes in gene function that do not involve changes in the DNA sequence. Epigenetic changes, consisting principally of DNA methylation, histone modifications and non-coding RNAs, maintain and modulate the initial impact of regulatory factors that recognize and associate with particular genomic sequences. This book’s primary goal is to establish a framework that can be used to understand the basis of epigenetic regulation and to appreciate both its derivation from genetics and its interdependence with genetic mechanisms. A further aim is to highlight the role played by the three-dimensional organization of the genetic material itself (the complex of DNA, histones and non-histone proteins referred to as chromatin) and its distribution within a functionally compartmentalized nucleus. Dysfunctions at any level of genetic regulation have the potential to result in an increased susceptibility to disease or actually give rise to overt pathologies. As illustrated in this book, research is continuously uncovering the role of epigenetics in a variety of human disorders, providing new avenues for therapeutic interventions and advances in regenerative medicine.

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Egreteau, Pierre-Yves, and Jean-Michel Boles. Assessing nutritional status in the ICU. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199600830.003.0204.

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Decreased nutrient intake, increased body requirements, and/or altered nutrient utilization are frequently combined in critically-ill patients. The initial nutritional status and the extent of the disease-related catabolism are the main risk factors for nutrition- related complications. Many complications are related to protein energy malnutrition, which is frequent in the ICU setting. Assessing nutritional status pursues several different goals. Nutritional assessment is required for patients presenting with clinical evidence of malnutrition, with chronic diseases, with acute conditions accompanied by a high catabolic rate, and elderly patients. Recording the patient’s history, nutrient intake, and physical examination, and subjective global assessment allows classification of nutritional status. All the traditional markers of malnutrition, anthropometric measurements and plasma proteins, lose their specificity in the sick adult as each may be affected by a number of non-nutritional factors. Muscle function evaluated by hand-grip strength in cooperative patients and serum albumin provide an objective risk assessment. Several nutritional indices have been validated in specific groups of patients to identify patients at risk of nutritionally-mediated complications and, therefore, the need for nutritional support. A strong suspicion remains the best way of uncovering potentially harmful nutritional deficiencies.

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Puntis, John. Food allergy. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198759928.003.0019.

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Food allergy is an immune response to food that can be classified as immunoglobulin (Ig)-E and non-IgE mediated. Milk, egg, peanut, tree nuts, and fish are among the most prevalent causes of food allergy. Mild reactions can include itchy rash, watering eyes, and nasal congestion while a severe reaction results in anaphylaxis. A detailed clinical history is essential when making a diagnosis, and skin prick testing and quantitative measurement of food-specific IgE antibodies can be helpful. Cow milk protein allergy causes a plethora of symptoms and frequently resolves spontaneously over the first 2 years of life; diagnosis is based mainly on clinical history. Food challenges have a pivotal role in the diagnosis of food allergy. Introduction of ‘allergic’ foods at 3–6 months alongside continuing breastfeeding may prevent allergy.

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Machado, Pedro M. Inclusion body myositis. Edited by Hector Chinoy and Robert Cooper. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198754121.003.0011.

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Sporadic inclusion body myositis (IBM) is an acquired muscle disorder associated with ageing, for which there is no effective treatment. It is characterized by a typical early clinical phenotype with (often asymmetric) weakness of the knee extensors and finger flexors, potential involvement of pharyngeal and upper-oesophageal muscles (which may contribute to malnutrition and aspiration), and progressive and slow deterioration, which may lead to severe disability and loss of quality of life. Muscle biopsy shows chronic myopathic features, lymphocytic infiltration with invasion of non-necrotic fibres, rimmed vacuoles, mitochondrial changes, and pathological accumulation of proteins in the muscle tissue. It remains uncertain whether IBM is primarily an immune-mediated inflammatory myopathy or a degenerative myopathy with an associated inflammatory component. This chapter will describe the clinical features, natural history, investigations, current pathogenic concepts, outcome measures, and therapeutic approaches in IBM. Despite recent clues, in many respects IBM remains an unsolved mystery.

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Book chapters on the topic "Proteine non histone"

1

Gupta, G. S. "Nuclear Skeleton Proteins: Non-Histones." In Proteomics of Spermatogenesis, 111–36. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/0-387-27655-6_6.

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2

Batta, Kiran, Chandrima Das, Shrikanth Gadad, Jayasha Shandilya, and Tapas K. Kundu. "Reversible Acetylation Of Non Histone Proteins." In Subcellular Biochemistry, 193–214. Dordrecht: Springer Netherlands, 2007. http://dx.doi.org/10.1007/1-4020-5466-1_9.

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Elgin, Sarah C. R., and William E. Stumph. "Chemistry of the Non-Histone Chromosomal Proteins." In Novartis Foundation Symposia, 113–30. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/9780470720103.ch8.

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Paul, J., and R. S. Gilmour. "The Regulatory Role of Non-Histone Proteins in RNA Synthesis." In Novartis Foundation Symposia, 181–98. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/9780470720103.ch11.

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Sanchez-Pina, M. A., H. Kieft, J. H. N. Schel, P. S. Testillano, and M. C. Risueño. "Localization of Non-Histone Nuclear Proteins by Immunocytochemistry in Somatic Embryos and Pollen Grains." In Nuclear Structure and Function, 253–58. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4613-0667-2_54.

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Kopple, Joel D., and Jerrilynn D. Burrowes. "History of Dietary Protein Treatment for Non-dialyzed Chronic Kidney Disease Patients." In Nutrition in Kidney Disease, 19–38. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-44858-5_2.

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Panagiotidis, Christos A., and Dimitrios A. Kyriakidis. "Purification of a non-histone protein with properties of antizyme to ornithine decarboxylase from germinated barley seeds." In Polyamines in Plants, 45–53. Dordrecht: Springer Netherlands, 1985. http://dx.doi.org/10.1007/978-94-009-5171-6_4.

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Allfrey, Vincent G., Akira Inoue, Jonathan Karn, Edward M. Johnson, Robert A. Good, and John W. Hadden. "Sequence-Specific Binding of DNA by Non-Histone Proteins and Their Migration from Cytoplasm to Nucleus During Gene Activation." In Novartis Foundation Symposia, 199–228. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/9780470720103.ch12.

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"Non-histone Proteins." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 1356–57. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_11501.

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Dirk, Lynnette M. A., Raymond C. Trievel, and Robert L. Houtz. "7 Non-histone protein lysine methyltransferases: Structure and catalytic roles." In Protein Methyltransferases, 179–228. Elsevier, 2006. http://dx.doi.org/10.1016/s1874-6047(06)80009-0.

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Conference papers on the topic "Proteine non histone"

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Schleuning, W. D. "THE BIOCHEMISTRY AND CELL BIOLOGY OF SINGLE CHAIN UROKINASE TYPE PLASMINOGEN ACTIVATOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642956.

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Urokinase was discovered in the late nineteenth century, as an enzymatic principle in urine, that initiates the dissolution of blood clots. The basis of this phenomenon was recognized more than fifty years ago as the activation of plasminogen, the precursor of a tryptic protease, then known as profibrinolysin. Despite this long history, detailed data on the biochemistry of plasminogen activation have only become available recently. Urokinase (now designated urokinase-type plasminogen activator : u-PA) is synthesized and secreted as a single chain polypeptide (Mr-: 53,000) by many cell types. Single chain u-PA (scu-PA) is with equal justification called prourokinase (pro-u-PA), notwithstanding its low catalytic activity for synthetic peptide substrates and plasminogen, as most proenzymes of proteases display a certain degree of activity. The structure of pro-u-PA has been elucidated by protein and cDNA sequencing. It consists of three domains, exhibiting characteristic homology to other proteins: a serine protease domain, homologous to trypsin, chymotrypsin and elastase; a kringle domain, likewise found in prothrombin, plasminogen, tissue-type plasminogen activator (t-PA) and Factor XII; and an epidermal growth factor (EGF)-like domain, found in many other proteins, including certain clotting factors. Pro-u-PA is activated by the cleavage of its LYS158-Ile159 h1 bY either plasmin or kallikrein. This cleavage leads to a high increase of Kcat values with respect to both plasminogen and synthetic peptide substrates, but apparently to a reduction of its affinity to plasminogen. Thrartoin inactivates pro-u-PA irreversibly by the cleavage of the Arg156-Phe157 bond. U-PA but not pro-u-PA rapidly forms ccnplexes with plasminogen activator inhibitors (PAI)-l and PAI-2: second order rate constants Kass are respectively > 107 and 0.9xl06 (M-11sec-1). Unknown enzymes process pro-u-PA and u-PA to low molecular weight (LMW) pro-u-PA and LMW u-PA (Mr: 33,000) by cutting off a fragment consisting of the kr ingle and the EGF—like region. Pro—u—PA mediated plasminogen activation is fibrin dependent in vivo, and to a certain degree in vitro. Hie biochemical basis of this fibrin specificity is at present uncertain, although there are reports indicating that it may require polyvalent cations. Through its EGF-like region HMW pro-u-PA and HMW u-PA are capable of binding to specific membrane protein receptors which are found on many cells. Thus, u-PA activity may be restricted to the cell surface. According to a recent report, binding of u—PA to the receptor may also mediate signal transduction in auto- or paracrine growth control. In cells permissive for the respective pathways, pro-u-PA gene transcription is stimulated by mechanisms of signal transduction, that include the cAMP, the tyrosine specific kinase and the protein kinase C dependent pathways. Glucocorticoid hormones downregulate pro-u-PA gene transcription in cells where the gene is canstitutively expressed. Although different cells vary greatly in their response to agents that stimulate urokinase biosynthesis, growth factors and other mitogens are in many cases effective inducers. Significantly elevated levels of u-PA are also found in many malignant tissues. These findings and many others suggest that plasminogen activation by u-PA provides localized extracellular matrix degradation which is required for invasive growth, cell migration and other forms of tissue remodelling. Fibrin represents in this view only a variant of an extracellular matrix, which is provided through the clotting system in the case of an emergency.

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2

Briët, E., L. Engesser, E. J. P. Brommer, A. W. Broekmans, and R. M. Bertina. "THROMBOPHILIA:ITS CAUSES AND A ROUGH ESTIMATE OF ITS PREVALENCE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642945.

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Idiopathic venous thrombosis and embolism have gained widespread interest since the discovery that, deficiencies of antithrombin III, protein C, and protein S are associated with familial venous thrombophilia. The purpose of our study was to obtain an estimate of the prevalence of this syndrome and to establish the etiology in as many cases as possible.We collaborated with specialists from 37 Dutch hospitals, covering about 10% of the Dutch population. A history as well as blood samples were obtained from 113 unrelated cases with familial thrombophilia and from 90 isolated cases. Assuming that each proband in a family with thrombophilia has an average of four affected relatives, a rough estimate of the prevalence of familial thrombophilia in The Netherlands is 40 cases per 100.000. The prevalence of non-familial thrombophilia is probably lower.In 35 out of the 113 familial cases we established a diagnosis of hereditary antithrombin III deficiency (n=5), protein C deficiency (type I: n=9; type II: n=4), protein S deficiency (n=15) and dysfibrinogenemia (n=2). In 36 cases we found no abnormality at all and in the remaining 42 cases abnormalities were found in one or more of the following: heparin cofactor II, factor V, factor VII, factor VIII, von Willebrand factor, plasminogen, tissue plasminogen activator, plasminogen activator inhibitor, alpha 2 antiplasmin and histidine rich glycoprotein. In most of these cases, however, the hereditary nature of the abnormalities could not be demonstrated and the causal relationships remain to be established.In the 90 isolated cases, we diagnosed hereditary deficiencies of anti thrombin III, protein C and protein S each in one case and a lupus anticoagulant in two cases. In 54 cases no abnormality was found and in the remaining 31 cases various abnormalities were found in one or more of the proteins mentioned above.We conclude that the syndrome of thrombophilia is not rare but its true prevalence needs to be established by more rigorous means. An etiological diagnosis can be made with confidence in only one third of the familial cases and in less than 10 percent of the isolated cases.

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Qiu, Yusheng, Jie Zhu, Joseph Footitt, Patrick Mallia, Sebastian L. Johnston, and Peter K. Jeffery. "Bronchial Mucosal Histone Deacetylase 2 (HDAC2) Protein Expression In Non-Smokers, Smokers And Smokers With COPD: A Biopsy Study." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a1355.

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Rabiet, M. J., B. C. Furie, and B. Furie. "MOLECULAR DEFECT IN PROTHROMBIN MADRID: SUBSTITUTION OF ARGININE 273 BY CYSTEINE PRECLUDES ACTIVATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643936.

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Prothrombin Madrid, a mutant prothrombin, was detected in a patient with a excessive bleeding history. The defect was characterized by a low coagulant activity contrasting with a normal level of prothrombin antigen in plasma. Activation of the purified protein was impaired by the absence of one of the two factor Xa catalyzed cleavages, generating meizothrombin which expressed a thrombin-like activity but was inactive on fibrinogen (Guillin et al., Ann. N.Y. Acad. Sci. 370:414, 1981). Prothrombin and prothrombin Madrid were isolated directly from plasma, with high yield, by immunoaffinity chromatography using conformation specific antibodies immobilized on Sepharose. After reduction and alkylation, purified proteins were hydrolyzed by trypsin. Resulting peptides were separated by reverse phase HPLC. Comparison of the two peptide maps showed that the prothrombin Madrid digest contained an additional peptide, identified by automated Edman degradation as residues 269 to 287 in prothrombin with the substitution of cysteine for arginine at position 273. Peptide 274—287, present in the prothrombin digest, was missing in the prothrombin Madrid digest. The mutation, precluding cleavage by factor Xa and normal generation of thrombin, is identical to the one described for prothrombin Barcelona. The two patients families are not related, raising the possibility that the gene coding for the cysteine 273 mutation in prothrombin is more common than anticipated. Of the seven mutants of vitamin E-dependant blood clotting proteins structurally characterized to date, three are functionally defective due to the presence of the propeptide on the mature amino-ternfinus (factor IX Cambridge, Oxford 3 and San Dimas) and three are due to an alteration that precludes zymogen activation (faotor TX Chapel Hill, prothrombin Barcelona and Madrid). This sample remains too small to anticipate the different classes of point mutations seen in the human population but functional abnormalities of protein processing, metal and lipid binding, zymogen activation, substrate recognition and enzyme catalysis will likely be important phenotypes. However genetic defects may be limited to a discrete group of point mutations that have significant functional implication for the proteins

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5

Petruccelli, Luca A., Filippa Pettersson, Daphne Dupere‐Richer, Kim L. Rice, Jonathan D. Licht, and Wilson H. Miller. "Abstract A189: Expression of fusion proteins in acute myeloid leukemia cells increases sensitivity to histone deacetylase inhibitors." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-a189.

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Panzer, S., I. Pabinger, R. Dudczak, E. Schulz, E. Wurz, K. Lechner, and K. Lechner. "PROTEIN S AND ANTICARDIOLIPIN ANTIBODIES IN PATIENTS WITH LUPUS ANTICOAGULANT WITH OR WITHOUT THROMBOSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644236.

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Arterial and venous thrombosis frequently occur in patients with lupus anticoagulant. We investigated in patients with lupus anticoagulant the possible association between protein S:Ag deficiency and/or anticardiolipin antibodies and a history of thrombosis. In 27 patients (8 with and 19 without a history of thromboembolic disease) free protein S:Ag was determined with immunoelectrophoresis in PEG 8000 precipitated plasma. Anticardiolipin antibodies were measured in 22 patients (10 with thromboembolism) by means of a solid phase radioimmunoassay.Free plasma protein S:Ag was normal or elevated in 25 patients and slightly decreased (protein S:Ag 67%) in 2 patients without thromboembolism. 2-dimensional electrophoresis revealed a normal distribution of the free and of the complexed form of protein S:Ag. Anticardiolipin antibodies were found in 6 out of 10 patients with a history of thrombosis (5 of 7 with venous thrombosis, 1 of 1 with cerebral infarction , none of 2 with combined venous and arterial thromboembolism) and in 4 out of 12 patients without a history of thrombosis.We conclude 1. the thrombophilic state in patients with lupus anticoagulant cannot be explained by a reduction of protein S:Ag, and 2. there seems to be no correlation between the presence or absence of anticardiolipin antibodies and the development of thromboembolic disease.

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Malm, J., M. Laurell, I. M. Nilsson, and B. Dahlbäck. "PROTEIN C, PROTEIN S AND THE FIBRINOLYTIC SYSTEM IN PATIENTS WITH A HISTORY OF THROMBOSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643643.

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Consecutive patients with a history of thrombo-embolic disease (n = 241, 109 males, 132 females, mean age 46 y), referred to the Coagulation Laboratory during an 18 month period, were analysed for defects in their coagulation and fibrinolytic systems. The diagnosis of thrombosis had been verified with phlebography and that of pulmonary embolus with scintigraphy or angiography. Retinal venous thrombosis was found in 15 of the patients. In 15 cases the thrombotic episodes occurred postoperatively, in 15 during pregnancy, in 12 during the postpartum period and in 20 during use of oral contraceptives. In the remaining cases no clinical riskfactors were identified.The concentration of protein C zymogen was measured with an immunoradiometric assay. Functional protein C was determined with a clotting inhibition assay. Protein C deficiency was found in 8 cases. Two of these had a functional protein C deficiency with normal zymogen levels. The concentration of total, as well as free (not in complex with C4b-binding protein), protein S was determined with a radioimmunoassay. Two cases of protein S deficiency were detected. Three patients with antithrombin III deficiency and two with plasminogen deficiency were found.The fibrinolytic activity after venous occlusion was analysed in 216 patients. Decreased levels were found in 32 %. The concentration of tissue plasminogen activator inhibitor (PAI) was measured in 110 patients and found to be increased in 65 % of the cases. In 99 patients both the fibrinolytic activity and the PAI concentration were measured. A combination of decreased fibrinolytic activity and increased levels of PAI was found in 44 cases. The concentration of tissue plasminogen activator antigen was decreased in 22 % of 105 cases analysed.Thus, in this material of patients with thrombo-embolic disease, abnormalities were found in 47 %. Defects in the fibrinolytic system were the most common findings. Protein C or protein S deficiency was diagnosed in less than 5 % of the cases.

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Hahn, Hwa-jeong, and Yong-sung juhnn. "Abstract LB-388: Regulation of histone deacethylase 8 expression by inhibitory GTP binding proteins in H1299 non-small-cell lung cancer cells." 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-lb-388.

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9

Imaoka, T., and T. Asaji. "FUNCTION OF PLATELET 47K PHOSPHOPROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644634.

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Secretion of platelet granule constituents is closely associated with the phosphorylation of a cytosol polypeptide that we called P47 of Mr 47,000 (Imaoka, T. and Haslam, R.J., J. Biol. Chem. 258, 11404, 1983), by protein kinase C. Since the identity and function remains to be known, we purified protein kinase C, unphosphorylated and phosphorylated P47 to homogeneity from human platelets. Then precise phosphorylation reaction of P47 in vitro and a biological function of P47 were studied. Protein kinase C catalysed the phosphorylation reaction of P47 protein, platelet myosin light chain, histone III-S with Km of 0.8±0.2, 4.2±0.5, 4.7±0.7μM, and Vmax of 0.312, 0.189, 0.874 nmole/min/mg, respectively. Some data previously obtained in this laboratory and others utilizing histone III-S as substrate are consistent with the synergistic effect by diacylglycerol (DG) in the presence of Ca++ , phosphatidylserine (PS). Using P47 as substrate, the enzyme required both Ca++ and PS, but not DG for activity. 125I labelled unphosphorylated P47 had an ability to bind with platelet membrane fraction in the presense of phosphatidylserine. Effect of diacylglycerol was inhibitory in this PS dependent P47 binding with membrane. Unphosphorylated P47 had a inhibitory activity in platelet actin polymerization. Molar ratio to inhibit actin polymerization was 1:8(P47:actin). These activities were Ca++ independent. Purified 32P-labelled P47 lost the binding ability with membrane, also the inhibitory activity in actin polymerization.Therefore, we propose the hypothesis that unphosphorylated P47 may loosely bind with the inside of plasma membrane of platelet and inhibit actin polymerization as a modulator, when stimulated, protein Kinase C rapidly phosphorylate P47 and induce the activation of cytoskeletal network and subsequently release reaction. On the other hand, whether DG in fact can act as a second messenger remain uncertain, (supported by MESC of Japan)

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Mannuccl, P. M., and A. Tripodl. "DIAGNOSTIC SCREENING OF CONGENITAL THROMBOTIC SYNDROMES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643717.

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The prevalence of inherited thrombotic syndromes in the general population (1 in 2,500/5,000) appears to be higher than that of inherited bleeding disorders. We have reviewed the problems of their diagnosis and propose a simple screening procedure. The most important candidates far. screening are patients with unexplained venous thromboembolism at ages ofless than 40 years, particularly when thrombotic episodes are recurrent.Screening must start from collectionof the clinical and family history of the propositus and from the exclusion of common acquired forms of thrombophilia. A negative family historydoes not exclude inherited thrombophilia, because the defects have oftena low penetrance and fresh mutationsmay have occurred in the propositi. The test chosen for laboratoryscreening of inherited thrombotic syndromes must be limited in number, easy todo and, more importantly, their results should be clinically relevent Which defects should be screened and what type of methodology should be used? The table is intended to answerthese questions by proposing a two-step screening procedure.The tests included in the .first step of the screening are aimed at evaluating Laboratory screening of inherited thrombotic syndromes the most frequent and well established causes of inherited thrombophilia, —-antithrombin III, protein C. protein S.plasminogen and fibrinogen.FIRST STEP Antithrombin III (heparin cofactorI chromogenic assay)Protein C (Francis' clotting assay)Protein S(electroimmunoassay of total proteinSantigen)Plasminogen (chromogenic assay)Fibrinogen (clotting assay)SECONSTEP(Tran's functional assay) Plasminogen activator (fibrin plate assay before and after venous stasisor DDAVP)Plasminogen activator inhibitor(chromogenic assay)The tests offirst choice that we propose (see table) are in general functional assaysdetecting both type I and type IIdeficiencies and are simple enough tobecarried out even in non specialized laboratories.For protein S, however,this goal has not been achieved yet and only type I protein S deficiencycan be currently identified with immunoassays measuring total protein S antigen. Since a number of laboratories may still not have the facilities to perform protein C functional assays, they are advised to set up at least an immunoassay, since type I deficiencies are much more frequent than type II deficiencies. The tests included in the second step of the screening are aimed at detectingthe less common or less well established causes of thrombophilia, and should be carried out when the clinical history suggests the existence of inherited thrombophilia and yet the first step has failed to reveal any laboratory abnormality. Defective plasminogen activation can be evaluated by measuring plasminogen activator activity with the simple fibrin plate assay carried out before and after stimuli such as venous occlusion and/or DDAVP infusion. The parallel measurement of plasminogen activator inhibitor allows to distinguish cases of detective plasminogen activation due to high inhibitor levels. The measurement of heparin cofactor II should also be included in this battery of second-step screening tests.Using this screening procedure in95 propositi with juvenile venous thromboembolism, we have identified 7 kindreds with antithrombin III deficiency (5 type I and 2 type II) (7.5%),7 kindreds with protein C deficiency (1 type II) (7.5%), 5 kindredswith protein S deficiency (5%), 1 withhypoplasminogenemia (1%) and 1 with dysfibrinogenemia Milano II (1). Theremaining undiagnosed cases might bedue to as yet unidentified deficiencies or abnormalities of other antithrombotic mechanisms such as,for instance, endothelial thrombomodulin or the fibrinolysis enhancing property of the protein C-protein S system.

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