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Journal articles on the topic 'Variantes H1'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Izzo, Annalisa, Kinga Kamieniarz, and Robert Schneider. "The histone H1 family: specific members, specific functions?" Biological Chemistry 389, no. 4 (2008): 333–43. http://dx.doi.org/10.1515/bc.2008.037.

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AbstractThe linker histone H1 binds to the DNA entering and exiting the nucleosomal core particle and has an important role in establishing and maintaining higher order chromatin structures. H1 forms a complex family of related proteins with distinct species, tissue and developmental specificity. In higher eukaryotes all H1 variants have the same general structure, consisting of a central conserved globular domain and less conserved N-terminal and C-terminal tails. These tails are moderately conserved among species, but differ among variants, suggesting a specific function for each H1 variant.

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2

Schulze, E., S. Nagel, K. Gavenis, and U. Grossbach. "Structurally divergent histone H1 variants in chromosomes containing highly condensed interphase chromatin." Journal of Cell Biology 127, no. 6 (1994): 1789–98. http://dx.doi.org/10.1083/jcb.127.6.1789.

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Condensed and late-replicating interphase chromatin in the Dipertan insect Chironomus contains a divergent type of histone H1 with an inserted KAP-KAP repeat that is conserved in single H1 variants of Caenorhabditis elegans and Volvox carteri. H1 peptides comprising the insertion interact specifically with DNA. The Chironomid Glyptotendipes exhibits a corresponding correlation between the presence of condensed chromosome sections and the appearance of a divergent H1 subtype. The centromere regions and other sections of Glyptotendipes barbipes chromosomes are inaccessible to immunodecoration by

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3

Palyga, Jan, and James M. Neelin. "Isolation and preliminary characterization of histone H1.b allelic variants from quail erythrocytes." Genome 41, no. 5 (1998): 709–19. http://dx.doi.org/10.1139/g98-070.

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Our goal was to purify and characterize the allelic variants H1b1 and H1b2 of histone H1.b, one of the seven subtypes of this linker histone extracted from Japanese quail erythrocyte nuclei. These variants are revealed phenotypically as band H1.3 or part of band H1.4 by polyacrylamide gel electrophoresis (PAGE) in sodium dodecyl sulfate (SDS). All H1 subtypes together were separated from H5 by gel-permeation chromatography through Bio-Gel P-150. H1 was then fractionated on a column of the cation-exchange resin Amberlite CG-50 by using a shallow guanidine hydrochloride gradient, which enriched

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Cramer, Thomas J., Ranjeet K. Sinha, and John H. Griffin. "Reduction Of Histone H1 Cytotoxicity By Activated Protein C and Its Exosite Variants." Blood 122, no. 21 (2013): 2334. http://dx.doi.org/10.1182/blood.v122.21.2334.2334.

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Abstract In vivo and in vitro data in murine and baboon sepsis models have shown pathogenic effects of extracellular histones H3 and H4 in the circulation. The plasma serine protease, activated protein C (APC), is protective in these models by proteolysis of histones H3 and H4, and APC remarkably reduces mortality in these models. Histones H3 and H4 are also pathogenic in lung, liver, and kidney injury models. The function of extracellular histone H1, the linker histone between nucleosomes, has not been well investigated. Here we test the hypothesis that H1 can exert cytotoxic activity on lung

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5

Lindner, H., W. Helliger, and B. Puschendorf. "Separation of rat tissue histone H1 subtypes by reverse-phase h.p.l.c. Identification and assignment to a standard H1 nomenclature." Biochemical Journal 269, no. 2 (1990): 359–63. http://dx.doi.org/10.1042/bj2690359.

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H1 histones from rat liver and rat testis were separated by reverse-phase h.p.l.c. Within 40 min six subfractions (H1(0), H1b, H1a, H1d, H1e + H1c and H1c) and seven subfractions (H1(0), H1b, H1a, H1d, H1e + H1c, H1c and H1t) respectively were isolated by using a linear acetonitrile gradient. Each individual H1 subtype was identified either by comparing the H1 variants (contained in both tissues but in different quantities) or by SDS/PAGE and acetic acid/urea/PAGE. Moreover, all H1 variants were characterized by amino acid analyses. The amino acid compositions of rat histone subfractions H1(0)

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6

Medvedev, Zhores A., and Margarita N. Medvedeva. "Age-related changes of the H1 and H1° histone variants in murine tissues." Experimental Gerontology 25, no. 2 (1990): 189–200. http://dx.doi.org/10.1016/0531-5565(90)90050-c.

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7

Kowalski, Andrzej, and Sebastian Knaga. "Evidence on the stability of histone H1.a polymorphic variants during selection in quail." Archives Animal Breeding 60, no. 2 (2017): 145–51. http://dx.doi.org/10.5194/aab-60-145-2017.

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Abstract. The goal of this work was to check whether selection for quantitative traits may cause a change in the histone H1 allelic complement and whether it can therefore be considered a modulator of histone H1-dependent chromatin functioning. For this purpose, a fluctuation of histone H1.a polymorphic variants was analyzed among a non-selected (control) quail line and the line selected for a high cholesterol content in the egg yolk. The histone H1.a was found to be polymorphic due to its differential migration rate in the AU-PAGE (acetic acid–urea polyacrylamide gel electrophoresis). Based o

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8

Kowalski, Andrzej, and Jan Pałyga. "Polymorphic linker histone H1 variants in breeding and conservative duck populations." Annals of Animal Science 14, no. 1 (2014): 33–42. http://dx.doi.org/10.2478/aoas-2013-0061.

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Abstract A purpose of this study was to evaluate genetic diversity in duck populations based on polymorphic variants (H1.a, H1.b and H1.z) of linker histone H1. The study was performed using conservative brown-feathered Khaki Campbell (Kh1) and Orpington (Or) populations and white-feathered Pekin (P77) duck breeding line. While no significant distortion between both brown-feathered duck populations was noted (P>0.05), the allele frequencies at histone H1 polymorphic loci were found to differ significantly between brown-feathered and white-feathered duck flocks (P<0.001). While the allele

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Ślusarczyk, Joanna, Andrzej Wierzbicki, Marcin Przewłoka, Teresa Tykarska, Andrzej Jerzmanowski, and Mieczysław Kuraś. "Influence of change in the proportion of H1 histone variants on microsporogenesis and development of male gametophyte in transgenic plants of tobacco (Nicotiana tabacum L.)." Acta Societatis Botanicorum Poloniae 72, no. 1 (2011): 25–35. http://dx.doi.org/10.5586/asbp.2003.004.

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As continuation of investigations in to the mechanism of the role of the H1 histone, which is a crucial protein component chromosomes of all eukaryotes, transgenic tobacco plants with different levels of the H1 histone variants were examined. Tobacco has six sequential variants of the H1 histone: two major ones (H1A and H1B), constituting ca. 90% of all H1, and four minor ones (H1C, H1D, H1E and H1F), occurring in very small quantities. The following groups of plants were examined: K - control group with a full set of histone variants; -AB -with the A and B variants removed; -ABCD - with the A

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10

Gornicka-Michalska, Ewa, Jan Palyga, Andrzej Kowalski, and Katarzyna Cywa-Benko. "Sequence variants of chicken linker histone H1.a." FEBS Journal 273, no. 6 (2006): 1240–50. http://dx.doi.org/10.1111/j.1742-4658.2006.05147.x.

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11

Uno, Tomohide, Toshiaki Uchikawa, Teruo Iwasaki, and Yasuo Aizono. "Molecular Characteristics of Porcine Thymus Histone H1 Variants." Bioscience, Biotechnology, and Biochemistry 59, no. 3 (1995): 420–24. http://dx.doi.org/10.1271/bbb.59.420.

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12

Pérez-Montero, Salvador, Albert Carbonell, and Fernando Azorín. "Germline-specific H1 variants: the “sexy” linker histones." Chromosoma 125, no. 1 (2015): 1–13. http://dx.doi.org/10.1007/s00412-015-0517-x.

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13

González-Romero, Rodrigo, Juan Ausió, Josefina Méndez, and José M. Eirín-López. "Histone genes of the razor clam Solen marginatus unveil new aspects of linker histone evolution in protostomes." Genome 52, no. 7 (2009): 597–607. http://dx.doi.org/10.1139/g09-034.

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The association of DNA with histones results in a nucleoprotein complex called chromatin that consists of repetitive nucleosomal subunits. Nucleosomes are joined together in the chromatin fiber by short stretches of linker DNA that interact with a wide diversity of linker H1 histones involved in chromatin compaction and dynamics. Although the long-term evolution of the H1 family has been the subject of different studies during the last 5 years, the lack of molecular data on replication-independent (RI) H1 variants from protostomes has been hampering attempts to complete the evolutionary pictur

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14

Noberini, Roberta, Cristina Morales Torres, Evelyn Oliva Savoia, et al. "Label-Free Mass Spectrometry-Based Quantification of Linker Histone H1 Variants in Clinical Samples." International Journal of Molecular Sciences 21, no. 19 (2020): 7330. http://dx.doi.org/10.3390/ijms21197330.

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Epigenetic aberrations have been recognized as important contributors to cancer onset and development, and increasing evidence suggests that linker histone H1 variants may serve as biomarkers useful for patient stratification, as well as play an important role as drivers in cancer. Although traditionally histone H1 levels have been studied using antibody-based methods and RNA expression, these approaches suffer from limitations. Mass spectrometry (MS)-based proteomics represents the ideal tool to accurately quantify relative changes in protein abundance within complex samples. In this study, w

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15

Okuwaki, Mitsuru, Mayumi Abe, Miharu Hisaoka, and Kyosuke Nagata. "Regulation of Cellular Dynamics and Chromosomal Binding Site Preference of Linker Histones H1.0 and H1.X." Molecular and Cellular Biology 36, no. 21 (2016): 2681–96. http://dx.doi.org/10.1128/mcb.00200-16.

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Linker histones play important roles in the genomic organization of mammalian cells. Of the linker histone variants, H1.X shows the most dynamic behavior in the nucleus. Recent research has suggested that the linker histone variants H1.X and H1.0 have different chromosomal binding site preferences. However, it remains unclear how the dynamics and binding site preferences of linker histones are determined. Here, we biochemically demonstrated that the DNA/nucleosome and histone chaperone binding activities of H1.X are significantly lower than those of other linker histones. This explains why H1.

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16

Starkova, T. Yu, T. O. Artamonova, V. V. Ermakova, E. V. Chikhirzhina, M. A. Khodorkovskii, and A. N. Tomilin. "The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells." Acta Naturae 11, no. 2 (2019): 82–91. http://dx.doi.org/10.32607/20758251-2019-11-2-82-91.

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Linker histone H1 is one of the main chromatin proteins which plays an important role in organizing eukaryotic DNA into a compact structure. There is data indicating that cell type-specific post-translational modifications of H1 modulate chromatin activity. Here, we compared histone H1 variants from NIH/3T3, mouse embryonic fibroblasts (MEFs), and mouse embryonic stem (ES) cells using matrix-assisted laser desorption/ ionization Fourier transform ion cyclotron resonance mass spectrometry (MALDI-FT-ICR-MS). We found significant differences in the nature and positions of the post-translational m

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17

Malanga, Maria, Luigia Atorino, Filomena Tramontano, Benedetta Farina, and Piera Quesada. "Poly(ADP-ribose) binding properties of histone H1 variants." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1399, no. 2-3 (1998): 154–60. http://dx.doi.org/10.1016/s0167-4781(98)00110-9.

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18

Kowalski, Andrzej, and Jan Pałyga. "Modulation of chromatin function through linker histone H1 variants." Biology of the Cell 108, no. 12 (2016): 339–56. http://dx.doi.org/10.1111/boc.201600007.

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19

Helliger, W., H. Lindner, O. Grübl-Knosp, and B. Puschendorf. "Alteration in proportions of histone H1 variants during the differentiation of murine erythroleukaemic cells." Biochemical Journal 288, no. 3 (1992): 747–51. http://dx.doi.org/10.1042/bj2880747.

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We have investigated the changes in the relative amounts of histone H1 zero and all five H1 variants during the differentiation in vitro of Friend erythroleukaemic cells. Three different agents were used as inducers of differentiation: dimethyl sulphoxide, hexamethylenebisacetamide and sodium butyrate. By applying a combination of reverse-phase h.p.l.c. and one-dimensional gel electrophoresis we observed that, during differentiation in vitro, (1) the relative amount of each subtype changes upon induction and that (2) dimethyl sulphoxide and hexamethylenebisacetamide produce a similar histone H

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20

Zheng, Yupeng, Sam John, James J. Pesavento, et al. "Histone H1 phosphorylation is associated with transcription by RNA polymerases I and II." Journal of Cell Biology 189, no. 3 (2010): 407–15. http://dx.doi.org/10.1083/jcb.201001148.

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Histone H1 phosphorylation affects chromatin condensation and function, but little is known about how specific phosphorylations impact the function of H1 variants in higher eukaryotes. In this study, we show that specific sites in H1.2 and H1.4 of human cells are phosphorylated only during mitosis or during both mitosis and interphase. Antisera generated to individual H1.2/H1.4 interphase phosphorylations reveal that they are distributed throughout nuclei and enriched in nucleoli. Moreover, interphase phosphorylated H1.4 is enriched at active 45S preribosomal RNA gene promoters and is rapidly

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21

WRIGHT, Jonathan M., Paul A. WIERSMA, and Gordon H. DIXON. "Use of protein blotting to study the DNA-binding properties of histone H1 and H1 variants." European Journal of Biochemistry 168, no. 2 (1987): 281–85. http://dx.doi.org/10.1111/j.1432-1033.1987.tb13418.x.

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22

D'ERME, Maria, Giuseppe ZARDO, Anna REALE, and Paola CAIAFA. "Co-operative interactions of oligonucleosomal DNA with the H1e histone variant and its poly(ADP-ribosyl)ated isoform." Biochemical Journal 316, no. 2 (1996): 475–80. http://dx.doi.org/10.1042/bj3160475.

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H1 histone somatic variants from L929 mouse fibroblasts were purified by reverse-phase HPLC. We analysed the ability of each H1 histone variant to allow the H1–H1 interactions that are essential for the formation of the higher levels of chromatin structure, and we investigated the role played by the poly(ADP-ribosyl)ation process. Cross-linking analysis showed that H1e is the only somatic variant which, when bound to DNA, is able to produce H1–H1 polymers; the size of polymers was decreased when H1e was enriched in its poly(ADP-ribosyl)ated isoform. Measurement of the methyl-accepting ability

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23

Wang, Binbin, Jinting Yan, Rui Mi, et al. "Forkhead box H1 (FOXH1) sequence variants in ventricular septal defect." International Journal of Cardiology 145, no. 1 (2010): 83–85. http://dx.doi.org/10.1016/j.ijcard.2009.05.030.

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24

Ristiniemi, Jukka, and Jouko Oikarinen. "Homology of histone H1 variants with adenine nucleotide-binding proteins." Biochemical and Biophysical Research Communications 153, no. 2 (1988): 783–91. http://dx.doi.org/10.1016/s0006-291x(88)81164-1.

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25

Starkova, T. Yu, A. M. Polyanichko, T. O. Artamonova, et al. "Post-translational modifications of linker histone H1 variants in mammals." Physical Biology 14, no. 1 (2017): 016005. http://dx.doi.org/10.1088/1478-3975/aa551a.

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26

Falco, J. R. P., and M. L. S. Mello. "Critical electrolyte concentration of spermatozoal chromatin containing histone H1 variants." Genetics and Molecular Biology 22, no. 2 (1999): 197–200. http://dx.doi.org/10.1590/s1415-47571999000200010.

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The critical electrolyte concentrations (CEC) of sperm chromatin from animal species known or suspected to contain histone H1 variants were compared by examining the affinity of their DNA-protein complexes for toluidine blue in the presence of Mg2+. Bullfrog, sea urchin, bee and bumblebee spermatozoa were studied. The CEC for Rana catesbeiana and two sea urchin species were similar to that of histone H5-containing chromatin from chicken erythrocytes, thus confirming the biochemical and structural similarities of these DNA-protein complexes. The CEC for bees and the bumblebee, Bombus atratus, s

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27

Pyo, Sang-Hyun, Jae-Heung Lee, Yeune Hee Lee, Jong-Won Yoon, and Jin-Hyun Kim. "Purification and characterization of histone H1 variants from human placenta." Biotechnology and Bioprocess Engineering 13, no. 6 (2008): 772–77. http://dx.doi.org/10.1007/s12257-008-0186-1.

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28

Mandl, B., W. F. Brandt, G. Superti-Furga, P. G. Graninger, M. L. Birnstiel, and M. Busslinger. "The five cleavage-stage (CS) histones of the sea urchin are encoded by a maternally expressed family of replacement histone genes: functional equivalence of the CS H1 and frog H1M (B4) proteins." Molecular and Cellular Biology 17, no. 3 (1997): 1189–200. http://dx.doi.org/10.1128/mcb.17.3.1189.

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The cleavage-stage (CS) histones of the sea urchin are known to be maternally expressed in the egg, have been implicated in chromatin remodeling of the male pronucleus following fertilization, and are the only histone variants present in embryonic chromatin up to the four-cell stage. With the help of partial peptide sequence information, we have isolated and identified CS H1, H2A, H2B, H3, and H4 cDNAs from egg poly(A)+ mRNA of the sea urchin Psammechinus miliaris. All five CS proteins correspond to replacement histone variants which are encoded by replication-independent genes containing intr

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29

Lu, Z. H., D. B. Sittman, D. T. Brown, R. Munshi, and G. H. Leno. "Histone H1 modulates DNA replication through multiple pathways in Xenopus egg extract." Journal of Cell Science 110, no. 21 (1997): 2745–58. http://dx.doi.org/10.1242/jcs.110.21.2745.

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We investigated the effects of histone H1s on DNA replication using Xenopus egg extract. Mouse variants H1c and H10 were assembled onto Xenopus sperm chromatin by the extract during the remodeling that accompanies nuclear decondensation. The association of H1 with chromatin was rapid and concentration dependent. H1-associated chromatin displayed a typical nucleosomal repeat pattern indicating that linker histones are properly positioned along the DNA. The presence of H1 on sperm chromatin reduced both the rate and extent of DNA replication in egg extract. This reduction in rate is due, in part

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30

Terme, Jean-Michel, Borja Sesé, Lluis Millán-Ariño, et al. "Histone H1 Variants Are Differentially Expressed and Incorporated into Chromatin during Differentiation and Reprogramming to Pluripotency." Journal of Biological Chemistry 286, no. 41 (2011): 35347–57. http://dx.doi.org/10.1074/jbc.m111.281923.

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There are seven linker histone variants in human somatic cells (H1.0 to H1.5 and H1X), and their prevalence varies as a function of cell type and differentiation stage, suggesting that the different variants may have distinct roles. We have revisited this notion by using new methodologies to study pluripotency and differentiation, including the in vitro differentiation of human embryonic stem (ES) and teratocarcinoma cells and the reprogramming of keratinocytes to induced pluripotent stem cells. Our results show that pluripotent cells (PCs) have decreased levels of H1.0 and increased levels of

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31

Finsterbusch, Tim, Anne Wolbert, Ingrid Deitemeier, et al. "Measles viruses of genotype H1 evade recognition by vaccine-induced neutralizing antibodies targeting the linear haemagglutinin noose epitope." Journal of General Virology 90, no. 11 (2009): 2739–45. http://dx.doi.org/10.1099/vir.0.013524-0.

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The linear haemagglutinin noose epitope (HNE; aa 379–410) is a protective B-cell epitope and considered to be highly conserved in both the vaccine and the wild-type measles virus (MeV) haemagglutinin (H) proteins. Vaccine virus-derived monoclonal antibodies (mAbs) BH6 and BH216, which target the HNE, neutralized MeVs of genotypes B3, C2, D4, D5, D6, D7 and D8, and the vaccine strain Edmonston Zagreb. In the case of genotype H1, only strain Berlin.DEU/44.01 was neutralized by these mAbs, whereas strains Shenyang.CHN/22.99 and Sofia.BGR/19.05 were not. The H gene sequences of these two strains s

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32

Talasz, Heribert, Wilfried Helliger, Bernd Puschendorf, and Herbert Lindner. "In Vivo Phosphorylation of Histone H1 Variants during the Cell Cycle†." Biochemistry 35, no. 6 (1996): 1761–67. http://dx.doi.org/10.1021/bi951914e.

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33

AZORIN, Fernando, Elisabeth ROCHA, Luis CORNUDELLA, and Juan A. SUBIRANA. "Anomalous nuclease digestion of Holothuria, sperm chromatin containing histone H1 variants." European Journal of Biochemistry 148, no. 3 (1985): 529–32. http://dx.doi.org/10.1111/j.1432-1033.1985.tb08871.x.

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Lindner, Herbert, Wilfried Helliger, Arnold Dirschlmayer, et al. "Separation of phosphorylated histone H1 variants by high-performance capillary electrophoresis." Journal of Chromatography A 608, no. 1-2 (1992): 211–16. http://dx.doi.org/10.1016/0021-9673(92)87126-s.

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35

Brandt, Wolf F., and Claus von Holt. "Variants of wheat histone H1 with N- and C-terminal extensions." FEBS Letters 194, no. 2 (1986): 282–86. http://dx.doi.org/10.1016/0014-5793(86)80101-6.

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Saha, Ankita, Christopher H. Seward, Lisa Stubbs, and Craig A. Mizzen. "Site-Specific Phosphorylation of Histone H1.4 Is Associated with Transcription Activation." International Journal of Molecular Sciences 21, no. 22 (2020): 8861. http://dx.doi.org/10.3390/ijms21228861.

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Core histone variants, such as H2A.X and H3.3, serve specialized roles in chromatin processes that depend on the genomic distributions and amino acid sequence differences of the variant proteins. Modifications of these variants alter interactions with other chromatin components and thus the protein’s functions. These inferences add to the growing arsenal of evidence against the older generic view of those linker histones as redundant repressors. Furthermore, certain modifications of specific H1 variants can confer distinct roles. On the one hand, it has been reported that the phosphorylation o

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Santoro, R., M. D'Erme, S. Mastrantonio, et al. "Binding of histone H1e-c variants to CpG-rich DNA correlates with the inhibitory effect on enzymic DNA methylation." Biochemical Journal 305, no. 3 (1995): 739–44. http://dx.doi.org/10.1042/bj3050739.

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Within the H1 histone family, only some fractions enriched in the H1e-c variants are effective in causing a marked inhibition, in vitro, of enzymic DNA methylation and, in gel retardation and Southwestern blot experiments, in binding double-stranded (ds) CpG-rich oligonucleotides. Both the 6-CpG ds-oligonucleotide and the DNA purified from chromatin fractions enriched in ‘CpG islands’ are good competitors for the binding of H1e-c to 6-meCpG ds-oligonucleotide. Because of their ability to bind any DNA sequence and to suppress the enzymic methylation in any sequence containing CpG dinucleotides,

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Yang, Chung-Ling, Cheng-Hung Lin, Wen-I. Luo, et al. "Mechanistic Study of the Stereoselective Hydroxylation of [2-2 H1 ,3-2 H1 ]Butanes Catalyzed by Cytochrome P450 BM3 Variants." Chemistry - A European Journal 23, no. 11 (2016): 2571–82. http://dx.doi.org/10.1002/chem.201603956.

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Cao, Kaixiang, Nathalie Lailler, Yunzhe Zhang, et al. "High-Resolution Mapping of H1 Linker Histone Variants in Embryonic Stem Cells." PLoS Genetics 9, no. 4 (2013): e1003417. http://dx.doi.org/10.1371/journal.pgen.1003417.

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Zheng, Xiao, Jiajun Li, Jie Sheng, et al. "Haplotypes of the Mutated SIRT2 Promoter Contributing to Transcription Factor Binding and Type 2 Diabetes Susceptibility." Genes 11, no. 5 (2020): 569. http://dx.doi.org/10.3390/genes11050569.

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Genetic variability is an important causative factor for susceptibility and pathogenesis of type 2 diabetes (T2D). Histone deacetylase, sirtuin 2 (SIRT2), plays regulatory roles in glucose metabolism and insulin sensitivity. However, whether the SIRT2 variants or haplotypes contribute to T2D risk remain to be elucidated. In this study, we first detected three novel polymorphisms (P-MU1, P-MU2, and P-MU3) in the promoter of SIRT2 in the Chinese population. All pairwise sets of the three loci were strongly in linkage disequilibrium. Next, we constructed the haplotype block structure, and found H

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Chen, Ling, Takeshi Azuma, Weiwei Yu, Xu Zheng, Liqun Luo, and Lieping Chen. "B7-H1 maintains the polyclonal T cell response by protecting dendritic cells from cytotoxic T lymphocyte destruction." Proceedings of the National Academy of Sciences 115, no. 12 (2018): 3126–31. http://dx.doi.org/10.1073/pnas.1722043115.

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Induced B7-H1 expression in the tumor microenvironment initiates adaptive resistance, which impairs immune functions and leads to tumor escape from immune destruction. Antibody blockade of the B7-H1/PD-1 interaction overcomes adaptive resistance, leading to regression of advanced human cancers and survival benefits in a significant fraction of patients. In addition to cancer cells, B7-H1 is expressed on dendritic cells (DCs), but its role in DC functions is less understood. DCs can present multiple antigens (Ags) to stimulate dominant or subdominant T cell responses. Here, we show that immuniz

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Zhao, Mingcai, Cindy Sutherland, David P. Wilson, Jingti Deng, Justin A. MacDonald та Michael P. Walsh. "Identification of the linker histone H1 as a protein kinase Cε-binding protein in vascular smooth muscle". Biochemistry and Cell Biology 82, № 5 (2004): 538–46. http://dx.doi.org/10.1139/o04-053.

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A variety of anchoring proteins target specific protein kinase C (PKC) isoenzymes to particular subcellular locations or multimeric signaling complexes, thereby achieving a high degree of substrate specificity by localizing the kinase in proximity to specific substrates. PKCε is widely expressed in smooth muscle tissues, but little is known about its targeting and substrate specificity. We have used a Far-Western (overlay) approach to identify PKCε-binding proteins in vascular smooth muscle of the rat aorta. Proteins of ~32 and 34 kDa in the Triton-insoluble fraction were found to bind PKCε in

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Kowalski, Andrzej. "Polymorphism of histone H1.c’ in the population of Muscovy duck (Cairina moschata L.): a link between histone H1.c’ allelic variants and ADP-ribosylation of histone H1 subtypes." European Zoological Journal 88, no. 1 (2021): 649–58. http://dx.doi.org/10.1080/24750263.2021.1912200.

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Bogdanova, V. S., S. M. Rozov, Y. A. Trusov, and V. A. Berdnikov. "Phenotypic effect of substitutions of short chromosomal segments containing different alleles of histone HI genes in garden pea (Pisum sativum L.)." Genetical Research 64, no. 1 (1994): 35–41. http://dx.doi.org/10.1017/s0016672300032523.

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SummaryA hypothesis has been tested that alterations in the molecule of histone H1 are capable of influencing quantitative traits of an organism. Two pairs of isogenic lines were constructed by selfing of plants kept heterozygous either for allelic variants of histone H1 subtype 1 (His1 gene) or for allelic combinations (haplotypes) of closely linked genes of H1 subtypes 3, 4, 5 and 6 (gene cluster His(2–6)). After 19 and 15 generations of selfing, respectively, expectation of the length of chromosome which remained heterozygous has comprised 2·6 cM near Hisl and 3·5 cM near His(2–6). The thir

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Schulze, E., L. Trieschmann, B. Schulze, et al. "Structural and functional differences between histone H1 sequence variants with differential intranuclear distribution." Proceedings of the National Academy of Sciences 90, no. 6 (1993): 2481–85. http://dx.doi.org/10.1073/pnas.90.6.2481.

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Atanasova, Rossitsa, and Stanka Koleva. "Electrophoretic and Immunochemical Characteristics of H1 Histone Variants in Peas (Pisum sativum L.)." Journal of Plant Physiology 133, no. 6 (1989): 664–70. http://dx.doi.org/10.1016/s0176-1617(89)80070-7.

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Wellman, Susan E. "Carboxyl-terminal peptides from histone H1 variants: DNA binding characteristics and solution conformation." Biopolymers 39, no. 4 (1998): 491–501. http://dx.doi.org/10.1002/(sici)1097-0282(199610)39:4<491::aid-bip2>3.0.co;2-s.

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Grossbach, Ulrich. "Selective distribution of histone H1 variants and high mobility group proteins in chromosomes." Seminars in Cell Biology 6, no. 4 (1995): 237–46. http://dx.doi.org/10.1006/scel.1995.0032.

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Nowak-Göttl, Ulrike, Hartmut Weiler, Irene Hernandez та ін. "Fibrinogen α and γ genes and factor VLeiden in children with thromboembolism: results from 2 family-based association studies". Blood 114, № 9 (2009): 1947–53. http://dx.doi.org/10.1182/blood-2009-04-218727.

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Previous case-control studies showed that genetic variation in the fibrinogen γ gene (FGG) increased the risk for deep vein thrombosis (VT) in adults. We investigated the association between the fibrinogen α (FGA) and FGG haplotypes, the factor VLeiden-mutation, and pediatric VT and thromboembolic stroke (TS) in 2 independent study samples. Association analysis revealed that the FGA-H1 and FGG-H2 haplotypes were significantly overtransmitted to VT patients (FGA-H1, P = .05; FGG: H2, P = .032). In contrast, the FGG-H3 haplotype was undertransmitted (P = .022). In an independent study sample, FG

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Kowalski, Andrzej. "A status of guinea fowl (Numida meleagris) and pheasant (Phasianus colchicus) population transferred from wildlife to the breeding assessed based on the histone H1.c’ polymorphic variation." Avian Biology Research 12, no. 4 (2019): 145–51. http://dx.doi.org/10.1177/1758155919860351.

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The genetic changes accompanying a relocation of population to the captivity are mostly adverse and usually associated with deterioration of its status. These alterations are greater in small populations in which a loss of genetic variation limits the capability to adaptation. In this work, a status of small-sized guinea fowl and pheasant population relocated to the breeding is presented. These populations were analyzed based on the polymorphism of histone H1.c’, the protein for the first time identified as a heterogeneous. Histone H1.c’ was resolved in the two-dimensional polyacrylamide gel i

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