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Artículos de revistas sobre el tema "Proteins maturation"

Autor: Grafiati

Publicado: 10 de marzo de 2023

Última modificación: 31 de julio de 2025

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1

Hellen, Christopher U. T., and Eckard Wimmer. "Maturation of poliovirus capsid proteins." Virology 187, no. 2 (1992): 391–97. http://dx.doi.org/10.1016/0042-6822(92)90440-z.

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2

Sumi, Mamta P., and Arnab Ghosh. "Hsp90 in Human Diseases: Molecular Mechanisms to Therapeutic Approaches." Cells 11, no. 6 (2022): 976. http://dx.doi.org/10.3390/cells11060976.

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The maturation of hemeprotein dictates that they incorporate heme and become active, but knowledge of this essential cellular process remains incomplete. Studies on chaperon Hsp90 has revealed that it drives functional heme maturation of inducible nitric oxide synthase (iNOS), soluble guanylate cyclase (sGC) hemoglobin (Hb) and myoglobin (Mb) along with other proteins including GAPDH, while globin heme maturations also need an active sGC. In all these cases, Hsp90 interacts with the heme-free or apo-protein and then drives the heme maturation by an ATP dependent process before dissociating fro

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3

Garoff, Henrik, Roger Hewson, and Dirk-Jan E. Opstelten. "Virus Maturation by Budding." Microbiology and Molecular Biology Reviews 62, no. 4 (1998): 1171–90. http://dx.doi.org/10.1128/mmbr.62.4.1171-1190.1998.

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SUMMARY Enveloped viruses mature by budding at cellular membranes. It has been generally thought that this process is driven by interactions between the viral transmembrane proteins and the internal virion components (core, capsid, or nucleocapsid). This model was particularly applicable to alphaviruses, which require both spike proteins and a nucleocapsid for budding. However, genetic studies have clearly shown that the retrovirus core protein, i.e., the Gag protein, is able to form enveloped particles by itself. Also, budding of negative-strand RNA viruses (rhabdoviruses, orthomyxoviruses, a

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4

Remington, S. James. "Fluorescent proteins: maturation, photochemistry and photophysics." Current Opinion in Structural Biology 16, no. 6 (2006): 714–21. http://dx.doi.org/10.1016/j.sbi.2006.10.001.

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5

Matthews, Glenn. "Introduction: Proteolytic maturation of secretory proteins." Seminars in Cell & Developmental Biology 9, no. 1 (1998): 1–2. http://dx.doi.org/10.1006/scdb.1997.0193.

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6

Gross, I. "Regulation of fetal lung maturation." American Journal of Physiology-Lung Cellular and Molecular Physiology 259, no. 6 (1990): L337—L344. http://dx.doi.org/10.1152/ajplung.1990.259.6.l337.

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The recent identification of the genes for the surfactant proteins has greatly facilitated the study of the regulation of fetal lung alveolar epithelial cell development at the molecular level. In general, expression of the genes for the surfactant proteins is enhanced by the same hormones that stimulate phospholipid synthesis. There are, however, some notable differences that indicate that the genes for the different components of surfactant are independently regulated. Species differences in the response of the surfactant proteins to hormones such as glucocorticoids and adenosine 3',5'-cycli

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7

Roland, Mélanie, Jonathan Przybyla-Toscano, Florence Vignols, et al. "The plastidial Arabidopsis thaliana NFU1 protein binds and delivers [4Fe-4S] clusters to specific client proteins." Journal of Biological Chemistry 295, no. 6 (2020): 1727–42. http://dx.doi.org/10.1074/jbc.ra119.011034.

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Proteins incorporating iron–sulfur (Fe-S) co-factors are required for a plethora of metabolic processes. Their maturation depends on three Fe-S cluster assembly machineries in plants, located in the cytosol, mitochondria, and chloroplasts. After de novo formation on scaffold proteins, transfer proteins load Fe-S clusters onto client proteins. Among the plastidial representatives of these transfer proteins, NFU2 and NFU3 are required for the maturation of the [4Fe-4S] clusters present in photosystem I subunits, acting upstream of the high-chlorophyll fluorescence 101 (HCF101) protein. NFU2 is a

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8

Watanabe, Satoshi, Daisuke Sasaki, Taiga Tominaga, and Kunio Miki. "Structural basis of [NiFe] hydrogenase maturation by Hyp proteins." Biological Chemistry 393, no. 10 (2012): 1089–100. http://dx.doi.org/10.1515/hsz-2012-0197.

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Abstract [NiFe] hydrogenases catalyze reversible hydrogen production/consumption. The active site of [NiFe] hydrogenases contains a complex NiFe(CN)2CO center, and the biosynthesis/maturation of these enzymes is a complex and dynamic process, primarily involving six Hyp proteins (HypABCDEF). HypA and HypB are involved in the Ni insertion, whereas the other four Hyp proteins (HypCDEF) are required for the biosynthesis, assembly and insertion of the Fe(CN)2CO group. Over the last decades, a large number of functional and structural studies on maturation proteins have been performed, revealing de

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9

Davis, Brandi N., Aaron C. Hilyard, Giorgio Lagna, and Akiko Hata. "SMAD proteins control DROSHA-mediated microRNA maturation." Nature 454, no. 7200 (2008): 56–61. http://dx.doi.org/10.1038/nature07086.

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10

PAGES, Jean Marie, and Claude LAZDUNSKI. "Maturation of Exported Proteins in Escherichia coli." European Journal of Biochemistry 124, no. 3 (2005): 561–66. http://dx.doi.org/10.1111/j.1432-1033.1982.tb06630.x.

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11

Long, Courtney L., William L. Berry, Ying Zhao, Xiao-Hong Sun, and Mary Beth Humphrey. "E proteins regulate osteoclast maturation and survival." Journal of Bone and Mineral Research 27, no. 12 (2012): 2476–89. http://dx.doi.org/10.1002/jbmr.1707.

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12

Gegenfurtner, Katrin, Florian Flenkenthaler, Thomas Fröhlich, Eckhard Wolf, and Georg J. Arnold. "The impact of transcription inhibition during in vitro maturation on the proteome of bovine oocytes†." Biology of Reproduction 103, no. 5 (2020): 1000–1011. http://dx.doi.org/10.1093/biolre/ioaa149.

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Abstract Proper oocyte maturation is a prerequisite for successful reproduction and requires the resumption of meiosis to the metaphase II stage (MII). In bovine oocytes, nuclear maturation has been shown to occur in in vitro maturing cumulus-enclosed oocytes (COCs) in the absence of transcription, but their developmental capacity is reduced compared to transcriptionally competent COCs. To assess the impact of transcription during in vitro maturation of bovine COCs on the quantitative oocyte proteome, a holistic nano-LC–MS/MS analysis of germinal vesicle oocytes and MII oocytes matured with or

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13

Abaturov, A. E., and V. L. Babуch. "MiRNA biogenesis. Part 1. Maturation of pre-miRNA. Maturation of canonical miRNAs." CHILD`S HEALTH 16, no. 2 (2021): 200–207. http://dx.doi.org/10.22141/2224-0551.16.2.2021.229886.

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The scientific review presents the biogenesis of miRNAs. To write the article, information was searched using databases Scopus, Web of Science, MedLine, PubMed, Google Scholar, EMBASE, Global Health, The Cochrane Library, CyberLeninka. The article presents a brief description of the RNA sequence encoding miRNAs. It is emphasized that microRNAs, depending on the location of the sequence encoding them in the genome, are divided into two major groups: canonical and non-canonical miRNAs. It has been found that a single locus of a sequence encoding a miRNA can generate a series of non-coding matur

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14

ENSRUD, KATHY M., and DAVID W. HAMILTON. "Use of Neonatal Tolerization and Chemical Immunosuppression for the Production of Monoclonal Antibodies to Maturation‐Specific Sperm Surface Molecules." Journal of Andrology 12, no. 5 (1991): 305–14. http://dx.doi.org/10.1002/j.1939-4640.1991.tb01606.x.

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ABSTRACT: Mammalian sperm acquire functional maturity as they move from the caput to the cauda epididymidis. Changes occur in the protein/glycoprotein composition of the sperm plasma membrane during this time, and may be essential to the maturation process. The production of monoclonal antibody (Mab) probes to the maturation‐specific molecules has been difficult since new proteins comprise a minor portion of total membrane proteins. This report describes a protocol for enhancing the production of Mabs to maturation specific molecules. By injecting neonatal mice with caput epididymal sperm plas

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15

Yen, Benjamin C., and Christopher F. Basler. "Effects of Filovirus Interferon Antagonists on Responses of Human Monocyte-Derived Dendritic Cells to RNA Virus Infection." Journal of Virology 90, no. 10 (2016): 5108–18. http://dx.doi.org/10.1128/jvi.00191-16.

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ABSTRACTDendritic cells (DCs) are major targets of filovirus infectionin vivo. Previous studies have shown that the filoviruses Ebola virus (EBOV) and Marburg virus (MARV) suppress DC maturationin vitro. Both viruses also encode innate immune evasion functions. The EBOV VP35 (eVP35) and the MARV VP35 (mVP35) proteins each can block RIG-I-like receptor signaling and alpha/beta interferon (IFN-α/β) production. The EBOV VP24 (eVP24) and MARV VP40 (mVP40) proteins each inhibit the production of IFN-stimulated genes (ISGs) by blocking Jak-STAT signaling; however, this occurs by different mechanisms

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16

Lu, Rebecca, and David G. Drubin. "Selection and stabilization of endocytic sites by Ede1, a yeast functional homologue of human Eps15." Molecular Biology of the Cell 28, no. 5 (2017): 567–75. http://dx.doi.org/10.1091/mbc.e16-06-0391.

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During clathrin-mediated endocytosis (CME), endocytic-site maturation can be divided into two stages corresponding to the arrival of the early and late proteins at the plasma membrane. The early proteins are required to capture cargo and position the late machinery, which includes proteins involved in actin assembly and membrane scission. However, the mechanism by which early-arriving proteins select and stabilize endocytic sites is not known. Ede1, one of the earliest proteins recruited to endocytic sites, facilitates site initiation and stabilization. Deletion of EDE1 results in fewer CME in

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17

Yang, Huijun, Weijing Liu, Shen Song, et al. "Proteogenomics Integrating Reveal a Complex Network, Alternative Splicing, Hub Genes Regulating Heart Maturation." Genes 13, no. 2 (2022): 250. http://dx.doi.org/10.3390/genes13020250.

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Heart maturation is an essentially biological process for neonatal heart transition to adult heart, thus illustrating the mechanism of heart maturation may be helpful to explore postnatal heart development and cardiac cardiomyopathy. This study combined proteomic analysis based on isobaric tags for relative and absolute quantitation (iTRAQ) and transcriptome analysis based on RNA sequencing to detect the proteins and genes associated with heart maturation in mice. The proteogenomics integrating analysis identified 254 genes/proteins as commonly differentially expressed between neonatal and adu

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18

Frank-Vaillant, Marie, Catherine Jessus, René Ozon, James L. Maller, and Olivier Haccard. "Two Distinct Mechanisms Control the Accumulation of Cyclin B1 and Mos inXenopusOocytes in Response to Progesterone." Molecular Biology of the Cell 10, no. 10 (1999): 3279–88. http://dx.doi.org/10.1091/mbc.10.10.3279.

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Progesterone-induced meiotic maturation of Xenopusoocytes requires the synthesis of new proteins, such as Mos and cyclin B. Synthesis of Mos is thought to be necessary and sufficient for meiotic maturation; however, it has recently been proposed that newly synthesized proteins binding to p34cdc2could be involved in a signaling pathway that triggers the activation of maturation-promoting factor. We focused our attention on cyclin B proteins because they are synthesized in response to progesterone, they bind to p34cdc2, and their microinjection into resting oocytes induces meiotic maturation. We

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19

Stevens-Hernandez, Christian J., and Lesley J. Bruce. "Reticulocyte Maturation." Membranes 12, no. 3 (2022): 311. http://dx.doi.org/10.3390/membranes12030311.

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Changes to the membrane proteins and rearrangement of the cytoskeleton must occur for a reticulocyte to mature into a red blood cell (RBC). Different mechanisms of reticulocyte maturation have been proposed to reduce the size and volume of the reticulocyte plasma membrane and to eliminate residual organelles. Lysosomal protein degradation, exosome release, autophagy and the extrusion of large autophagic–endocytic hybrid vesicles have been shown to contribute to reticulocyte maturation. These processes may occur simultaneously or perhaps sequentially. Reticulocyte maturation is incompletely und

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20

Sadeghi, Hamid M., Giulio Innamorati, and Mariel Birnbaumer. "Maturation of Receptor Proteins in Eukaryotic Expression Systems." Journal of Receptors and Signal Transduction 17, no. 1-3 (1997): 433–45. http://dx.doi.org/10.3109/10799899709036619.

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21

UCHIDA, Takeshi. "Structure and Function of Cytochrome c Maturation Proteins." Seibutsu Butsuri 47, no. 2 (2007): 112–17. http://dx.doi.org/10.2142/biophys.47.112.

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22

Spangler, S. A., та C. C. Hoogenraad. "Liprin-α proteins: scaffold molecules for synapse maturation". Biochemical Society Transactions 35, № 5 (2007): 1278–82. http://dx.doi.org/10.1042/bst0351278.

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Synapses are specialized communication junctions between neurons whose plasticity provides the structural and functional basis for information processing and storage in the brain. Recent biochemical, genetic and imaging studies in diverse model systems are beginning to reveal the molecular mechanisms by which synaptic vesicles, ion channels, receptors and other synaptic components assemble to make a functional synapse. Recent evidence has shown that the formation and function of synapses are critically regulated by the liprin-α family of scaffolding proteins. The liprin-αs have been implicated

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23

Kramer, Günter, Ayala Shiber, and Bernd Bukau. "Mechanisms of Cotranslational Maturation of Newly Synthesized Proteins." Annual Review of Biochemistry 88, no. 1 (2019): 337–64. http://dx.doi.org/10.1146/annurev-biochem-013118-111717.

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The timely production of functional proteins is of critical importance for the biological activity of cells. To reach the functional state, newly synthesized polypeptides have to become enzymatically processed, folded, and assembled into oligomeric complexes and, for noncytosolic proteins, translocated across membranes. Key activities of these processes occur cotranslationally, assisted by a network of machineries that transiently engage nascent polypeptides at distinct phases of translation. The sequence of events is tuned by intrinsic features of the nascent polypeptides and timely associati

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24

Blackman, Sheila A., Scott H. Wettlaufer, Ralph L. Obendorf, and A. Carl Leopold. "Maturation Proteins Associated with Desiccation Tolerance in Soybean." Plant Physiology 96, no. 3 (1991): 868–74. http://dx.doi.org/10.1104/pp.96.3.868.

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25

Netz, Daili J. A., Judita Mascarenhas, Oliver Stehling, Antonio J. Pierik, and Roland Lill. "Maturation of cytosolic and nuclear iron–sulfur proteins." Trends in Cell Biology 24, no. 5 (2014): 303–12. http://dx.doi.org/10.1016/j.tcb.2013.11.005.

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26

Rawe, V. Y., A. J. Espanñol, F. Nodar, and S. Brugo Olmedo. "Mammalian Oocyte Maturation and Microtubule-Associated Proteins Dynamics." Fertility and Sterility 84 (September 2005): S143. http://dx.doi.org/10.1016/j.fertnstert.2005.07.349.

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27

Kirchhoff, C., C. Osterhoff, I. Pera, and S. Schröter. "Function of human epididymal proteins in sperm maturation." Andrologia 30, no. 4-5 (2009): 225–32. http://dx.doi.org/10.1111/j.1439-0272.1998.tb01164.x.

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28

Sipos, Katalin, Heike Lange, Zsuzsanna Fekete, Pascaline Ullmann, Roland Lill, and Gyula Kispal. "Maturation of Cytosolic Iron-Sulfur Proteins Requires Glutathione." Journal of Biological Chemistry 277, no. 30 (2002): 26944–49. http://dx.doi.org/10.1074/jbc.m200677200.

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29

Deretic, V., Laura E. Via, Rutilio A. Fratti, and Dusanka Deretic. "Mycobacterial phagosome maturation, rab proteins, and intracellular trafficking." Electrophoresis 18, no. 14 (1997): 2542–47. http://dx.doi.org/10.1002/elps.1150181409.

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30

Dacheux, Jean-Louis, Jean Luc Gatti, and Françoise Dacheux. "Contribution of epididymal secretory proteins for spermatozoa maturation." Microscopy Research and Technique 61, no. 1 (2003): 7–17. http://dx.doi.org/10.1002/jemt.10312.

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31

Nim, Yap Shing, and Kam-Bo Wong. "The Maturation Pathway of Nickel Urease." Inorganics 7, no. 7 (2019): 85. http://dx.doi.org/10.3390/inorganics7070085.

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Maturation of urease involves post-translational insertion of nickel ions to form an active site with a carbamylated lysine ligand and is assisted by urease accessory proteins UreD, UreE, UreF and UreG. Here, we review our current understandings on how these urease accessory proteins facilitate the urease maturation. The urease maturation pathway involves the transfer of Ni2+ from UreE → UreG → UreF/UreD → urease. To avoid the release of the toxic metal to the cytoplasm, Ni2+ is transferred from one urease accessory protein to another through specific protein–protein interactions. One central

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32

Smirnov, Alexandre. "Research Progress in RNA-Binding Proteins." International Journal of Molecular Sciences 24, no. 1 (2022): 58. http://dx.doi.org/10.3390/ijms24010058.

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RNA-binding proteins are everywhere and accompany RNA molecules at every stage of their molecular life, from “birth” (transcription) through “growing up” (maturation), “active life” (molecular function) until “death” (turnover) [...]

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33

Bhojwani, M., M. Marx, F. Melo-Sterza, W. Kanitz, C. Leiding, and W. Tomek. "307CHARACTERIZATION OF PROTEIN PHOSPHORYLATIONS IN THE COURSE OF MEIOTIC MATURATION OF BOVINE OOCYTES." Reproduction, Fertility and Development 16, no. 2 (2004): 273. http://dx.doi.org/10.1071/rdv16n1ab307.

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The importance of protein phosphorylations during meiotic maturation (transition from prophase I to metaphase II) of oocytes is documented by the fact that the inhibition of the M-phase kinases, cdc2k or MAPK, arrests the oocytes in the GV stage. A detailed knowledge of the targets of these kinases during this stage of development is still missing. Therefore, we have analyzed the proteome of bovine oocytes by high resolution 2D-gel electrophoresis to detect differences in the expression and phosphorylation state of proteins in the course of in vitro maturation (IVM). Bovine oocytes were mature

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34

Desjardins, M., N. N. Nzala, R. Corsini, and C. Rondeau. "Maturation of phagosomes is accompanied by changes in their fusion properties and size-selective acquisition of solute materials from endosomes." Journal of Cell Science 110, no. 18 (1997): 2303–14. http://dx.doi.org/10.1242/jcs.110.18.2303.

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Maturation of phagosomes is characterized by changes in their polypeptides, phosphorylated proteins and phospholipid composition. Kinetic analyses have shown that a variety of proteins associate and dissociate from latex-containing phagosomes at precise intervals during phagolysosome biogenesis. In an attempt to link these temporal biochemical modifications to functional changes, we have examined the in vivo fusion properties of aging endosomes and phagosomes. Using an in vivo fusion assay at the electron microscope, we measured the rate of exchange of bovine serum albumin-gold (5 and 16 nm pa

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35

Hausen, Peter, Ya Hui Wang, Christine Dreyer, Reimer Stick, Ursula Müller, and Metta Riebesell. "Distribution of nuclear proteins during maturation of the Xenopus oocyte." Development 89, Supplement (1985): 17–34. http://dx.doi.org/10.1242/dev.89.supplement.17.

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The internal structure of the Xenopus oocyte is reorganized during the hormone-induced egg maturation. A cytological survey of the intracellular movements and changes is described. The behaviour of the nuclear lamina protein and of three nucleoplasmic proteins during these processes was studied by immunocytology. The proteins are finally deposited in the egg in different patterns brought about by their differential behaviour during the process of maturation.

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36

Wright, J. T., and W. T. Butler. "Alteration of Enamel Proteins in Hypomaturation Amelogenesis Imperfecta." Journal of Dental Research 68, no. 9 (1989): 1328–30. http://dx.doi.org/10.1177/00220345890680090801.

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Amelogenesis imperfecta (AI) is a diverse group of disorders that affects primarily the enamel of teeth through a number of developmental processes. The purpose of this study was to characterize the enamel proteins in normal enamel and in hypomaturation AI enamel. Impacted teeth, which were at similar stages of development, were obtained for analysis from an individual with Al and from normal healthy controls. Evaluation of the amino acid profile and quantity of organic material collected showed that there was an excess of enamel protein material that had an amelogenin-like amino acid profile

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37

Gillam, Shirley. "Molecular biology of rubella virus structural proteins." Biochemistry and Cell Biology 72, no. 9-10 (1994): 349–56. http://dx.doi.org/10.1139/o94-048.

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Rubella virus is a small, enveloped, positive-stranded RNA virus in the Togaviridae family and bears similarities to the prototype alphaviruses in terms of its genome organization and strategy for viral gene expression. Despite being an important human pathogen, the cell biology of rubella virus remains poorly characterized. This review focuses on the molecular biology of rubella virus structural proteins, with emphasis on the proteolytic processing and maturation of virus structural proteins, the glycosylation requirement for intracellular transport and function of glycoproteins, and the loca

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38

Wang, Xiangyu, Xiaofei Guo, Xiaoyun He, et al. "Proteomic Analysis Identifies Distinct Protein Patterns for High Ovulation in FecB Mutant Small Tail Han Sheep Granulosa Cells." Animals 14, no. 1 (2023): 11. http://dx.doi.org/10.3390/ani14010011.

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The Booroola fecundity (FecB) mutation in the bone morphogenetic protein receptor type 1B (BMPR1B) gene increases ovulation in sheep. However, its effect on follicular maturation is not fully understood. Therefore, we collected granulosa cells (GCs) at a critical stage of follicle maturation from nine wild-type (WW), nine heterozygous FecB mutant (WB), and nine homozygous FecB mutant (BB) Small Tail Han sheep. The GCs of three ewes were selected at random from each genotype and consolidated into a single group, yielding a total of nine groups (three groups per genotype) for proteomic analysis.

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Johnstone, RM, and K. Teng. "Membrane Remodelling During Reticulocyte Maturation." Physiology 4, no. 1 (1989): 37–42. http://dx.doi.org/10.1152/physiologyonline.1989.4.1.37.

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During maturation, reticulocytes lose many membrane functions, including the transferrin receptor. Immunocytochemical studies reveal that after endocytosis the transferrin receptor (and many other membrane proteins) is packaged into multivesicular bodies. The vesicular contents are externalized by exocytosis. The specificity of such membrane processing underlies the changing properties of the cells' surfaces.

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40

Stehling, Oliver, Daili J. A. Netz, Brigitte Niggemeyer, et al. "Human Nbp35 Is Essential for both Cytosolic Iron-Sulfur Protein Assembly and Iron Homeostasis." Molecular and Cellular Biology 28, no. 17 (2008): 5517–28. http://dx.doi.org/10.1128/mcb.00545-08.

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ABSTRACT The maturation of cytosolic iron-sulfur (Fe/S) proteins in mammalian cells requires components of the mitochondrial iron-sulfur cluster assembly and export machineries. Little is known about the cytosolic components that may facilitate the assembly process. Here, we identified the cytosolic soluble P-loop NTPase termed huNbp35 (also known as Nubp1) as an Fe/S protein, and we defined its role in the maturation of Fe/S proteins in HeLa cells. Depletion of huNbp35 by RNA interference decreased cell growth considerably, indicating its essential function. The deficiency in huNbp35 was asso

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41

Chirivino, Dafne, Laurence Del Maestro, Etienne Formstecher, et al. "The ERM proteins interact with the HOPS complex to regulate the maturation of endosomes." Molecular Biology of the Cell 22, no. 3 (2011): 375–85. http://dx.doi.org/10.1091/mbc.e10-09-0796.

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In the degradative pathway, the progression of cargos through endosomal compartments involves a series of fusion and maturation events. The HOPS (homotypic fusion and protein sorting) complex is part of the machinery that promotes the progression from early to late endosomes and lysosomes by regulating the exchange of small GTPases. We report that an interaction between subunits of the HOPS complex and the ERM (ezrin, radixin, moesin) proteins is required for the delivery of EGF receptor (EGFR) to lysosomes. Inhibiting either ERM proteins or the HOPS complex leads to the accumulation of the EG

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42

Johnstone, R. M. "Maturation of reticulocytes: formation of exosomes as a mechanism for shedding membrane proteins." Biochemistry and Cell Biology 70, no. 3-4 (1992): 179–90. http://dx.doi.org/10.1139/o92-028.

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The transferrin receptor is a member of a group of reticulocyte surface proteins that disappear from the membranes of reticulocytes as the cells mature to the erythrocyte stage. The selective loss of membrane proteins appears to be preceded by the formation of multivesicular bodies (MVBs). At the reticulocyte stage, many species of mammalian red cells including man, and one nucleated avian species (chicken), contain these intracellular structures in both natural and induced anemias. Also characteristic of blood containing reticulocytes is the presence of circulating vesicles (exosomes), which

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43

Hube, Michaela, Melanie Blokesch, and August Böck. "Network of Hydrogenase Maturation in Escherichia coli: Role of Accessory Proteins HypA and HybF." Journal of Bacteriology 184, no. 14 (2002): 3879–85. http://dx.doi.org/10.1128/jb.184.14.3879-3885.2002.

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ABSTRACT We have studied the roles of the auxiliary protein HypA and of its homolog HybF in hydrogenase maturation. A mutation in hypA leads to the nearly complete blockade of maturation solely of hydrogenase 3 whereas a lesion in hybF drastically but not totally reduces maturation and activity of isoenzymes 1 and 2. The residual level of matured enzymes in the hybF mutant was shown to be due to the function of HypA; HybF, conversely, was responsible for a minimal residual activity of hydrogenase 3 in the mutant hypA strain. Accordingly, a hypA ΔhybF double mutant was completely blocked in the

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Jeyaretnam, Benjamin, Hazel Y. Wetzstein, and Sharad C. Phatak. "DEVELOPMENTAL REGULATION OF PROTEINS IN ZYGOTICAND SOMATIC EMBRYOS OF PECAN." HortScience 28, no. 5 (1993): 499a—499. http://dx.doi.org/10.21273/hortsci.28.5.499a.

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Soluble and insoluble proteins from pecan (Carya illinoensis) zygotic and somatic embryos were resolved on one dimensional SDS-PAGE to study the changes in expression patterns of proteins. Soluble proteins were extracted using 0.1M NaCl and 50 mM Tris-HCl buffer while insoluble proteins were recovered by treating the pellet with SDS in Tris-HCl buffer. Several new insoluble proteins appeared during early maturation (26-47 days post anthesis, DPA) of zygotic embryos. The insoluble protein profile from early somatic embryos resembled that of cotyledon expansion stage zygotic embryos. About 12 gr

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Ge, Peng, and Z. Hong Zhou. "Chaperone fusion proteins aid entropy-driven maturation of class II viral fusion proteins." Trends in Microbiology 22, no. 2 (2014): 100–106. http://dx.doi.org/10.1016/j.tim.2013.11.006.

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Auhim, Husam Sabah, Bella L. Grigorenko, Tessa K. Harris, et al. "Stalling chromophore synthesis of the fluorescent protein Venus reveals the molecular basis of the final oxidation step." Chemical Science 12, no. 22 (2021): 7735–45. http://dx.doi.org/10.1039/d0sc06693a.

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Fluorescent proteins (FPs) have revolutionised the life sciences, but the chromophore maturation mechanism is still not fully understood. Here we photochemically trap maturation at a crucial stage and structurally characterise the intermediate.

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Berger, Nathalie, Florence Vignols, Jonathan Przybyla-Toscano, et al. "Identification of client iron–sulfur proteins of the chloroplastic NFU2 transfer protein in Arabidopsis thaliana." Journal of Experimental Botany 71, no. 14 (2020): 4171–87. http://dx.doi.org/10.1093/jxb/eraa166.

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Abstract Iron–sulfur (Fe-S) proteins have critical functions in plastids, notably participating in photosynthetic electron transfer, sulfur and nitrogen assimilation, chlorophyll metabolism, and vitamin or amino acid biosynthesis. Their maturation relies on the so-called SUF (sulfur mobilization) assembly machinery. Fe-S clusters are synthesized de novo on a scaffold protein complex and then delivered to client proteins via several transfer proteins. However, the maturation pathways of most client proteins and their specificities for transfer proteins are mostly unknown. In order to decipher t

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King, Paul W., Matthew C. Posewitz, Maria L. Ghirardi, and Michael Seibert. "Functional Studies of [FeFe] Hydrogenase Maturation in an Escherichia coli Biosynthetic System." Journal of Bacteriology 188, no. 6 (2006): 2163–72. http://dx.doi.org/10.1128/jb.188.6.2163-2172.2006.

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ABSTRACT Maturation of [FeFe] hydrogenases requires the biosynthesis and insertion of the catalytic iron-sulfur cluster, the H cluster. Two radical S-adenosylmethionine (SAM) proteins proposed to function in H cluster biosynthesis, HydEF and HydG, were recently identified in the hydEF-1 mutant of the green alga Chlamydomonas reinhardtii (M. C. Posewitz, P. W. King, S. L. Smolinski, L. Zhang, M. Seibert, and M. L. Ghirardi, J. Biol. Chem. 279:25711-25720, 2004). Previous efforts to study [FeFe] hydrogenase maturation in Escherichia coli by coexpression of C. reinhardtii HydEF and HydG and the H

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Xu, Z., and M. B. Hille. "Cell-free translation systems prepared from starfish oocytes faithfully reflect in vivo activity; mRNA and initiation factors stimulate supernatants from immature oocytes." Cell Regulation 1, no. 13 (1990): 1057–67. http://dx.doi.org/10.1091/mbc.1.13.1057.

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Meiotic maturation stimulates a change in the translation of stored mRNAs: mRNAs encoding proteins needed for growth of oocytes are translated before meiotic maturation, whereas those encoding proteins required for cleavage are translated after meiotic maturation. Studies of translational regulation during meiotic maturation have been limited by the lack of translationally active cell-free supernatants. Starfish oocytes are ideal for preparing cell-free translation systems because experimental application of the hormone 1-methyladenine induces their maturation, synchronizing meiosis. We have p

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Gerber, Jana, Karina Neumann, Corinna Prohl, Ulrich Mühlenhoff, and Roland Lill. "The Yeast Scaffold Proteins Isu1p and Isu2p Are Required inside Mitochondria for Maturation of Cytosolic Fe/S Proteins." Molecular and Cellular Biology 24, no. 11 (2004): 4848–57. http://dx.doi.org/10.1128/mcb.24.11.4848-4857.2004.

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ABSTRACT Iron-sulfur (Fe/S) proteins are located in mitochondria, cytosol, and nucleus. Mitochondrial Fe/S proteins are matured by the iron-sulfur cluster (ISC) assembly machinery. Little is known about the formation of Fe/S proteins in the cytosol and nucleus. A function of mitochondria in cytosolic Fe/S protein maturation has been noted, but small amounts of some ISC components have been detected outside mitochondria. Here, we studied the highly conserved yeast proteins Isu1p and Isu2p, which provide a scaffold for Fe/S cluster synthesis. We asked whether the Isu proteins are needed for bios

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