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Journal articles on the topic 'Zinc Histidine'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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1

Petrarca, Patrizia, Serena Ammendola, Paolo Pasquali, and Andrea Battistoni. "The Zur-Regulated ZinT Protein Is an Auxiliary Component of the High-Affinity ZnuABC Zinc Transporter That Facilitates Metal Recruitment during Severe Zinc Shortage." Journal of Bacteriology 192, no. 6 (2010): 1553–64. http://dx.doi.org/10.1128/jb.01310-09.

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ABSTRACT The pathways ensuring the efficient uptake of zinc are crucial for the ability of bacteria to multiply in the infected host. To better understand bacterial responses to zinc deficiency, we have investigated the role of the periplasmic protein ZinT in Salmonella enterica serovar Typhimurium. We have found that zinT expression is regulated by Zur and parallels that of ZnuA, the periplasmic component of the zinc transporter ZnuABC. Despite the fact that ZinT contributes to Salmonella growth in media containing little zinc, disruption of zinT does not significantly affect virulence in mic

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2

Jiang, Qian, Andrew M. Peterson, Yuyang Chu, Xiaolan Yao, Xiang-ming Zha, and Xiang-Ping Chu. "Histidine Residues Are Responsible for Bidirectional Effects of Zinc on Acid-Sensing Ion Channel 1a/3 Heteromeric Channels." Biomolecules 10, no. 9 (2020): 1264. http://dx.doi.org/10.3390/biom10091264.

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Acid-sensing ion channel (ASIC) subunits 1a and 3 are highly expressed in central and peripheral sensory neurons, respectively. Endogenous biomolecule zinc plays a critical role in physiological and pathophysiological conditions. Here, we found that currents recorded from heterologously expressed ASIC1a/3 channels using the whole-cell patch-clamp technique were regulated by zinc with dual effects. Co-application of zinc dose-dependently potentiated both peak amplitude and the sustained component of heteromeric ASIC1a/3 currents; pretreatment with zinc between 3 to 100 µM exerted the same poten

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3

Fujiwara, Tamaki, Shin Aoki, Hitoshi Komatsuzawa, et al. "Mutation Analysis of the Histidine Residues in the Glycylglycine Endopeptidase ALE-1." Journal of Bacteriology 187, no. 2 (2005): 480–87. http://dx.doi.org/10.1128/jb.187.2.480-487.2005.

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ABSTRACT A novel staphylolytic enzyme, ALE-1, is a glycylglycine endopeptidase produced by Staphylococcus capitis EPK1. ALE-1 possesses seven histidines. Chemical modification studies using diethylpyrocarbonate and iodoacetic acid suggested that a histidine or tyrosine residue(s) in the molecule is important for the organism's staphylolytic activity. All of the histidine residues, one tyrosine, and one aspartic acid residue in the N-terminally truncated ALE-1 (ΔN-term ALE-1) were systematically altered by site-directed mutagenesis, and the enzyme activities and metal contents of the variants w

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Zhu, Rongfeng, Yanqun Song, Haiping Liu, et al. "Allosteric histidine switch for regulation of intracellular zinc(II) fluctuation." Proceedings of the National Academy of Sciences 114, no. 52 (2017): 13661–66. http://dx.doi.org/10.1073/pnas.1708563115.

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Metalloregulators allosterically control transcriptional activity through metal binding-induced reorganization of ligand residues and/or hydrogen bonding networks, while the coordination atoms on the same ligand residues remain seldom changed. Here we show that the MarR-type zinc transcriptional regulator ZitR switches one of its histidine nitrogen atoms for zinc coordination during the allosteric control of DNA binding. The Zn(II)-coordination nitrogen on histidine 42 within ZitR’s high-affinity zinc site (site 1) switches from Nε2 to Nδ1 upon Zn(II) binding to its low-affinity zinc site (sit

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5

Zhang, Tuo, Eziz Kuliyev, Dexin Sui, and Jian Hu. "The histidine-rich loop in the extracellular domain of ZIP4 binds zinc and plays a role in zinc transport." Biochemical Journal 476, no. 12 (2019): 1791–803. http://dx.doi.org/10.1042/bcj20190108.

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Abstract The Zrt-/Irt-like protein (ZIP) family mediates zinc influx from extracellular space or intracellular vesicles/organelles, playing a central role in systemic and cellular zinc homeostasis. Out of the 14 family members encoded in human genome, ZIP4 is exclusively responsible for zinc uptake from dietary food and dysfunctional mutations of ZIP4 cause a life-threatening genetic disorder, Acrodermatitis Enteropathica (AE). About half of the missense AE-causing mutations occur within the large N-terminal extracellular domain (ECD), and our previous study has shown that ZIP4–ECD is crucial

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6

Davie, R. J., J. D. Phillips, and N. J. Birch. "The effect of zinc-histidine ratios on zinc intestinal absorption." Journal of Inorganic Biochemistry 43, no. 2-3 (1991): 686. http://dx.doi.org/10.1016/0162-0134(91)84653-q.

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7

Dyja, Renata, Barbara Dolińska, and Florian Ryszka. "Release of selected amino acids from zinc carriers." Acta Pharmaceutica 66, no. 2 (2016): 269–77. http://dx.doi.org/10.1515/acph-2016-0024.

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Abstract The paper deals with the results of an investigation of the release of selected amino acids (histidine, tryptophan, tyrosine) from model suspensions prepared by co-precipitation with zinc chloride. It has been proven that the influence of the Zn(II)/amino acid molar ratio on dissolution profiles of the tested amino acids and dissolution half-life (t1/2) of histidine or tryptophan is significant. The amount of amino acid in the dispersed phase (supporting dose) is a determinant of the amino acid release profile. There is a minimal supporting dose (30.0 μmol of histidine or 17.4 μmol of

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8

Lee, Myungwoon, Tuo Wang, Olga V. Makhlynets, et al. "Zinc-binding structure of a catalytic amyloid from solid-state NMR." Proceedings of the National Academy of Sciences 114, no. 24 (2017): 6191–96. http://dx.doi.org/10.1073/pnas.1706179114.

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Throughout biology, amyloids are key structures in both functional proteins and the end product of pathologic protein misfolding. Amyloids might also represent an early precursor in the evolution of life because of their small molecular size and their ability to self-purify and catalyze chemical reactions. They also provide attractive backbones for advanced materials. When β-strands of an amyloid are arranged parallel and in register, side chains from the same position of each chain align, facilitating metal chelation when the residues are good ligands such as histidine. High-resolution struct

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9

Erk, Inge, Jean-Claude Huet, Mariela Duarte, et al. "A Zinc Ion Controls Assembly and Stability of the Major Capsid Protein of Rotavirus." Journal of Virology 77, no. 6 (2003): 3595–601. http://dx.doi.org/10.1128/jvi.77.6.3595-3601.2003.

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ABSTRACT The recent determination of the crystal structure of VP6, the major capsid protein of rotavirus, revealed a trimer containing a central zinc ion coordinated by histidine 153 from each of the three subunits. The role of the zinc ion in the functions of VP6 was investigated by site-directed mutagenesis. The mutation of histidine 153 into a serine (H153S and H153S/S339H) did not prevent the formation of VP6 trimers. At pH <7.0, about the pK of histidine, wild-type and mutated VP6 proteins display similar properties, giving rise to identical tubular and spherical assemblies. However, a

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10

Glover, Chris N., and Christer Hogstrand. "Amino acid modulation of in vivo intestinal zinc absorption in freshwater rainbow trout." Journal of Experimental Biology 205, no. 1 (2002): 151–58. http://dx.doi.org/10.1242/jeb.205.1.151.

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SUMMARY The composition of the intestinal lumen is likely to have considerable influence upon the absorption, and consequently the nutrition and/or toxicity, of ingested zinc in aquatic environments, where zinc is both a nutrient and a toxicant of importance. The effects of amino acids upon intestinal zinc uptake in freshwater rainbow trout (Oncorhynchus mykiss) were studied using an in vivo perfusion technique. The presence of histidine, cysteine and taurine had distinct modifying actions upon quantitative and qualitative zinc absorption, compared to perfusion of zinc alone. Alterations in zi

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11

Wang, Xiaogang, Huiwen Zhang, Mingkai Xu, et al. "Biological characterization of the zinc site coordinating histidine residues of staphylococcal enterotoxin C2." Microbiology 155, no. 3 (2009): 680–86. http://dx.doi.org/10.1099/mic.0.025254-0.

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The bacterial toxin staphylococcal enterotoxin C2 (SEC2) can cause staphylococcal toxic shock syndrome and food poisoning. Although the previously determined crystal structure of SEC2 revealed that some histidine residues (His47, His118 and His122) contribute to the binding of zinc ions, little is known about their biological roles in SEC2. This prompted us to investigate the role of the zinc site coordinating histidine residues in the biological activities of SEC2. The mutants with substitutions at positions 118 and 122 all retained T-cell stimulatory activity, whereas the histidine mutants a

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12

Chappell, Richard L., Haohua Qian, Jane Zakevicius, and Harris Ripps. "Histidine Suppresses Zinc Modulation of Connexin Hemichannels." Biological Bulletin 207, no. 3 (2004): 188–90. http://dx.doi.org/10.2307/1543206.

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13

Sreevalsa, V. G., P. P. Jeeju, M. Sajimol Augustine, K. M. Anilkumar, and S. Jayalekshmi. "L-Histidine-modified biocompatible zinc oxide nanocrystals." Journal of Experimental Nanoscience 8, no. 7-8 (2012): 937–46. http://dx.doi.org/10.1080/17458080.2011.624553.

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14

Thalacker-Mercer, Anna E., and Mary E. Gheller. "Benefits and Adverse Effects of Histidine Supplementation." Journal of Nutrition 150, Supplement_1 (2020): 2588S—2592S. http://dx.doi.org/10.1093/jn/nxaa229.

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ABSTRACT Histidine is a nutritionally essential amino acid with many recognized benefits to human health, while circulating concentrations of histidine decline in pathologic conditions [e.g., chronic obstructive pulmonary disease (COPD) and chronic kidney disease (CKD)]. The purpose of this review is to examine the existing literature regarding the benefits of histidine intake, the adverse effects of excess histidine, and the upper tolerance level for histidine. Supplementation with doses of 4.0–4.5 g histidine/d and increased dietary histidine intake are associated with decreased BMI, adiposi

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15

Deters, A., E. Schnetz, M. Schmidt, and A. Hensel. "Effects of Zinc Histidine and Zinc Sulfate on Natural Human Keratinocytes." Complementary Medicine Research 10, no. 1 (2003): 19–25. http://dx.doi.org/10.1159/000069903.

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16

Sobczak, Amélie I. S., Samantha J. Pitt, and Alan J. Stewart. "Influence of zinc on glycosaminoglycan neutralisation during coagulation." Metallomics 10, no. 9 (2018): 1180–90. http://dx.doi.org/10.1039/c8mt00159f.

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17

Fu, Chieh-Lin, and McDonald K. Horn. "Histidine-rich glycoprotein plus zinc to neutralize heparin." Journal of Laboratory and Clinical Medicine 139, no. 4 (2002): 211–17. http://dx.doi.org/10.1067/mlc.2002.121854.

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18

Förster, Martin, and Heinrich Vahrenkamp. "Zinc Complexes of Histidine-Containing Di- and Tripeptides." Chemische Berichte 128, no. 6 (1995): 541–50. http://dx.doi.org/10.1002/cber.19951280603.

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19

Bottari, E., and M. R. Festa. "Histidine and Ornithine as Ligands Towards Zinc(II)." Journal of Coordination Chemistry 22, no. 3 (1990): 237–48. http://dx.doi.org/10.1080/00958979009408220.

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20

Merryman, Paula, Ann Cullinane, and McDonald Horne. "Histidine-Proline-Rich Glycoprotein Binding to Platelets Mediated by Transition Metals." Thrombosis and Haemostasis 85, no. 05 (2001): 890–95. http://dx.doi.org/10.1055/s-0037-1615764.

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SummaryHistidine-proline-rich glycoprotein (HPRG) binds zinc, which in turn promotes HPRG binding to lymphocytes and monocytes. We examined the possibility that zinc and other transition metals also promote HPRG binding to platelets. Only non-specific, unsaturable association of HPRG with resting or activated platelets was observed in the absence of transition metals. However, nickel, cobalt, copper, cadmium, and zinc greatly increased HPRG association with the cells. In the presence of zinc, specific, saturable binding of HPRG to platelets was demonstrated. The cell binding capacity for HPRG

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21

Schölmerich, J., A. Freudemann, E. Köttgen, et al. "Bioavailability of zinc from zinc-histidine complexes. I. Comparison with zinc sulfate in healthy men." American Journal of Clinical Nutrition 45, no. 6 (1987): 1480–86. http://dx.doi.org/10.1093/ajcn/45.6.1480.

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22

Cragnell, Carolina, Lasse Staby, Samuel Lenton, Birthe Kragelund, and Marie Skepö. "Dynamical Oligomerisation of Histidine Rich Intrinsically Disordered Proteins Is Regulated through Zinc-Histidine Interactions." Biomolecules 9, no. 5 (2019): 168. http://dx.doi.org/10.3390/biom9050168.

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Intrinsically disordered proteins (IDPs) can form functional oligomers and in some cases, insoluble disease related aggregates. It is therefore vital to understand processes and mechanisms that control pathway distribution. Divalent cations including Zn2+ can initiate IDP oligomerisation through the interaction with histidine residues but the mechanisms of doing so are far from understood. Here we apply a multi-disciplinary approach using small angle X-ray scattering, nuclear magnetic resonance spectroscopy, calorimetry and computations to show that that saliva protein Histatin 5 forms highly

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23

Kawahara, Masahiro, Yutaka Sadakane, Hironari Koyama, Keiko Konoha, and Susumu Ohkawara. "d-Histidine and l-histidine attenuate zinc-induced neuronal death in GT1-7 cells." Metallomics 5, no. 5 (2013): 453. http://dx.doi.org/10.1039/c3mt20264j.

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24

Christianson, David W., and Richard S. Alexander. "Carboxylate-histidine-zinc interactions in protein structure and function." Journal of the American Chemical Society 111, no. 16 (1989): 6412–19. http://dx.doi.org/10.1021/ja00198a065.

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25

Gao, Sheng-Li, San-Ping Chen, Rong-Zu Hu, and Qi-Zhen Shi. "Thermokinetics of the Formation Reaction of Zinc Histidine Complex." Chinese Journal of Chemistry 20, no. 1 (2010): 14–17. http://dx.doi.org/10.1002/cjoc.20020200104.

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26

Takeda, Atsushi, Mai Suzuki, Shoji Okada, and Naoto Oku. "Influence of Histidine on Zinc Transport into Rat Brain." JOURNAL OF HEALTH SCIENCE 46, no. 3 (2000): 209–13. http://dx.doi.org/10.1248/jhs.46.209.

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27

Xu, Pin, John Price, Alan Wise, and Peter J. Aggett. "Interaction of inositol phosphates with calcium, zinc, and histidine." Journal of Inorganic Biochemistry 47, no. 2 (1992): 119–30. http://dx.doi.org/10.1016/0162-0134(92)84048-r.

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28

Aiken, Simon P., Niall M. Horn, and Norman R. Saunders. "Effects of histidine on tissue zinc distribution in rats." BioMetals 5, no. 4 (1992): 235–43. http://dx.doi.org/10.1007/bf01061224.

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29

Siepi, Marialuisa, Rosario Oliva, Filomena Battista, et al. "Molecular Dissection of dH3w, A Fluorescent Peptidyl Sensor for Zinc and Mercury." Sensors 20, no. 3 (2020): 598. http://dx.doi.org/10.3390/s20030598.

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Previously, we reported that fluorescent peptide dansyl-HPHGHW-NH2 (dH3w), designed on the repeats of the human histidine-rich glycoprotein, shows a turn-on response to Zn(II) and a complex response to Hg(II) characterized by a turn-off phase at low Hg(II) concentrations and a turn-on phase at high concentrations. As Hg(II) easily displaces Zn(II), dH3w is a useful probe for the environmental monitoring of Hg(II). In order to investigate the molecular basis of the metal selectivity and fluorescence response, we characterized three variants, dH3w(H1A), dH3w(H3A), and dH3w(H5A), in which each of

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Radko, Sergey P., Svetlana A. Khmeleva, Dmitry N. Kaluzhny та ін. "The English (H6R) Mutation of the Alzheimer’s Disease Amyloid-β Peptide Modulates Its Zinc-Induced Aggregation". Biomolecules 10, № 6 (2020): 961. http://dx.doi.org/10.3390/biom10060961.

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The coordination of zinc ions by histidine residues of amyloid-beta peptide (Aβ) plays a critical role in the zinc-induced Aβ aggregation implicated in Alzheimer’s disease (AD) pathogenesis. The histidine to arginine substitution at position 6 of the Aβ sequence (H6R, English mutation) leads to an early onset of AD. Herein, we studied the effects of zinc ions on the aggregation of the Aβ42 peptide and its isoform carrying the H6R mutation (H6R-Aβ42) by circular dichroism spectroscopy, dynamic light scattering, turbidimetric and sedimentation methods, and bis-ANS and thioflavin T fluorescence a

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31

Eijkelkamp, Bart A., Victoria G. Pederick, Charles D. Plumptre, et al. "The First Histidine Triad Motif of PhtD Is Critical for Zinc Homeostasis inStreptococcus pneumoniae." Infection and Immunity 84, no. 2 (2015): 407–15. http://dx.doi.org/10.1128/iai.01082-15.

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Streptococcus pneumoniaeis the world's foremost human pathogen. Acquisition of the first row transition metal ion zinc is essential for pneumococcal colonization and disease. Zinc is acquired via the ATP-binding cassette transporter AdcCB and two zinc-binding proteins, AdcA and AdcAII. We have previously shown that AdcAII is reliant upon the polyhistidine triad (Pht) proteins to aid in zinc recruitment. Pht proteins generally contain five histidine (His) triad motifs that are believed to facilitate zinc binding and therefore play a significant role in pneumococcal metal ion homeostasis. Howeve

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32

Abendrot, Michał, Elżbieta Płuciennik, Aleksandra Felczak, et al. "Zinc(II) Complexes of Amino Acids as New Active Ingredients for Anti-Acne Dermatological Preparations." International Journal of Molecular Sciences 22, no. 4 (2021): 1641. http://dx.doi.org/10.3390/ijms22041641.

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Zinc compounds have a number of beneficial properties for the skin, including antimicrobial, sebostatic and demulcent activities. The aim of the study was to develop new anti-acne preparations containing zinc–amino acid complexes as active ingredients. Firstly, the cytotoxicity of the zinc complexes was evaluated against human skin fibroblasts (1BR.3.N cell line) and human epidermal keratinocyte cell lines, and their antimicrobial activity was determined against Cutibacterium acnes. Then, zinc complexes of glycine and histidine were selected to create original gel formulations. The stability (

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33

Bernstein, Bradley E., Ross C. Hoffman, Suzanne Horvath, Jon R. Herriott, and Rachel E. Klevit. "Structure of a Histidine-X4-Histidine Zinc Finger Domain: Insights into ADR1-UAS1 Protein-DNA Recognition." Biochemistry 33, no. 15 (1994): 4460–70. http://dx.doi.org/10.1021/bi00181a005.

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34

Besold, Angelique N., Deborah L. Amick, and Sarah L. J. Michel. "A role for hydrogen bonding in DNA recognition by the non-classical CCHHC type zinc finger, NZF-1." Mol. BioSyst. 10, no. 7 (2014): 1753–56. http://dx.doi.org/10.1039/c4mb00246f.

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35

Yoon, Bo-Young, Yong-Hak Kim, Nahee Kim, et al. "Structure of the periplasmic copper-binding protein CueP fromSalmonella entericaserovar Typhimurium." Acta Crystallographica Section D Biological Crystallography 69, no. 10 (2013): 1867–75. http://dx.doi.org/10.1107/s090744491301531x.

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CueP was initially identified as a copper-resistance gene inSalmonella entericaserovar Typhimurium, which has evolved to survive in the phagosomes of macrophages. Recently, CueP was determined to be a periplasmic copper-binding protein and has been implicated in the transfer of copper ions to SodCII in the periplasm. In this study, the crystal structure of CueP has been determined, revealing a V-shaped dimeric structure. The conserved cysteine and histidine residues are clustered on the surface of one side of the C-terminal domain, suggesting that this cysteine- and histidine-rich region is re

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Carfi, Andrea, Emile Duée, Moreno Galleni, Jean-Marie Frère та Otto Dideberg. "1.85 Å Resolution Structure of the ZincII β-Lactamase from Bacillus cereus". Acta Crystallographica Section D Biological Crystallography 54, № 3 (1998): 313–23. http://dx.doi.org/10.1107/s0907444997010627.

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Class B \beta-lactamases are wide spectrum enzymes which require bivalent metal ions for activity. The structure of the class B zinc-ion-dependent β-lactamase from Bacillus cereus (BCII) has been refined at 1.85 Å resolution using data collected on cryocooled crystals (100 K). The enzyme from B. cereus has a molecular mass of 24 946 Da and is folded into a \beta-sandwich structure with helices on the external faces. The active site is located in a groove running between the two \beta-sheets [Carfi et al. (1995). EMBO J. 14, 4914–4921]. The 100 K high-resolution BCII structure shows one fully a

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Li, Ruiyi, Jun Chen, Xiaoyan Zhou, Zaijun Li, and Junkang Liu. "Fabrication of zinc–histidine-functionalized graphene quantum dot framework amphiphilic nanoparticles and application in the synthesis of polystyrene microspheres for adsorption of Cu2+ by Pickering emulsion polymerization." RSC Advances 6, no. 104 (2016): 102534–41. http://dx.doi.org/10.1039/c6ra23366j.

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We reported fabrication of zinc–histidine-functionalized graphene quantum dot framework amphiphilic nanoparticles and application in the synthesis of polystyrene microspheres for adsorption of Cu<sup>2+</sup> by Pickering emulsion polymerization.

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Rola, Anna, Robert Wieczorek, Henryk Kozłowski, Karolina Krzywoszyńska та Sławomir Potocki. "Sometimes less is more—the impact of the number of His residues on the stability of Zn(ii)–SmtB and BigR4 α-5 domain complexes". Dalton Transactions 50, № 35 (2021): 12118–29. http://dx.doi.org/10.1039/d1dt01690c.

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Gockel, P., R. Vogler, M. Gelinsky, A. Meißner, H. Albrich, and H. Vahrenkamp. "Zinc complexation of cyclic dipeptides containing cysteine and/or histidine." Inorganica Chimica Acta 323, no. 1-2 (2001): 16–22. http://dx.doi.org/10.1016/s0020-1693(01)00561-8.

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40

LOGUE, AISLING M., ROBERT J. DAVIE, and NICHOLAS J. BIRCH. "Factors affecting zinc-histidine kinetics in rat jejunal everted sacs." Biochemical Society Transactions 18, no. 5 (1990): 1006–7. http://dx.doi.org/10.1042/bst0181006.

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41

Kho, Richard, Liem Nguyen, Claudia L. Torres-Martínez, and Rajesh K. Mehra. "Zinc–Histidine as Nucleation Centers for Growth of ZnS Nanocrystals." Biochemical and Biophysical Research Communications 272, no. 1 (2000): 29–35. http://dx.doi.org/10.1006/bbrc.2000.2712.

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42

Murphy, John T., Janelle J. Bruinsma, Daniel L. Schneider, et al. "Histidine Protects Against Zinc and Nickel Toxicity in Caenorhabditis elegans." PLoS Genetics 7, no. 3 (2011): e1002013. http://dx.doi.org/10.1371/journal.pgen.1002013.

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43

Khodamoradi, K., A. H. Khoshgoftarmanesh, N. Dalir, M. Afyuni, and R. Schulin. "How do glycine and histidine in nutrient solution affect zinc uptake and root-to-shoot translocation by wheat and triticale?" Crop and Pasture Science 66, no. 11 (2015): 1105. http://dx.doi.org/10.1071/cp14227.

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Understanding how complexes with amino acids in soil solution affect plant zinc (Zn) uptake may aid in optimising plant Zn nutrition. We investigated the influence of histidine and glycine in nutrient solution on apoplastic and symplastic uptake and root-to-shoot translocation of Zn in a triticale (×Triticosecale cv. Elinor) and a bread wheat cultivar (Triticum aestivum cv. Back Cross Rushan). Six-week-old seedlings of the two cultivars were transferred to a nutrient solution containing 20 µm Zn, to which 50 µm histidine, 50 µm glycine or no amino acids were added. Control plants were transpla

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Gheller, Mary E., Francoise Vermeylen, Michal K. Handzlik, et al. "Tolerance to graded dosages of histidine supplementation in healthy human adults." American Journal of Clinical Nutrition 112, no. 5 (2020): 1358–67. http://dx.doi.org/10.1093/ajcn/nqaa210.

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ABSTRACT Background Histidine is an essential amino acid with health benefits that may warrant histidine supplementation; however, the clinical safety of histidine intake above the average dietary intake (1.52–5.20 g/d) needs to be vetted. Objectives We aimed to determine the tolerance to graded dosages of histidine in a healthy adult population. Methods Healthy adults aged 21–50 y completed graded dosages of histidine supplement (4, 8, and 12 g/d, Study 1) (n = 20 men and n = 20 women) and/or a 16-g/d dosage of histidine (Study 2, n = 21 men and n = 19 women); 27 participants (n = 12 men and

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45

Hake, Laura E., Raul Mendez, and Joel D. Richter. "Specificity of RNA Binding by CPEB: Requirement for RNA Recognition Motifs and a Novel Zinc Finger." Molecular and Cellular Biology 18, no. 2 (1998): 685–93. http://dx.doi.org/10.1128/mcb.18.2.685.

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ABSTRACT CPEB is an RNA binding protein that interacts with the maturation-type cytoplasmic polyadenylation element (CPE) (consensus UUUUUAU) to promote polyadenylation and translational activation of maternal mRNAs in Xenopus laevis. CPEB, which is conserved from mammals to invertebrates, is composed of three regions: an amino-terminal portion with no obvious functional motif, two RNA recognition motifs (RRMs), and a cysteine-histidine region that is reminiscent of a zinc finger. In this study, we investigated the physical properties of CPEB required for RNA binding. CPEB can interact with RN

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SCHILLING, Oliver, Andreas VOGEL, Brenda KOSTELECKY та ін. "Zinc- and iron-dependent cytosolic metallo-β-lactamase domain proteins exhibit similar zinc-binding affinities, independent of an atypical glutamate at the metal-binding site". Biochemical Journal 385, № 1 (2004): 145–53. http://dx.doi.org/10.1042/bj20040773.

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ZiPD (zinc phosphodiesterase; synonyms are ElaC, ecoZ, RNaseZ and 3′ tRNase) and the iron-dependent redox enzyme FlRd (flavorubredoxin) from Escherichia coli represent prototypical cases of proteins sharing the metallo-β-lactamase fold that require strict metal selectivity for catalytic activity, yet their metal selectivity has only been partially understood. In contrast with hydrolytic metallo-β-lactamase proteins, iron-dependent FlRd-like enzymes have an atypical glutamate ligand, which replaces one otherwise conserved histidine ligand. X-ray absorption spectroscopy revealed that the FlRd me

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Wapnir, R. A., and S. Y. Lee. "Dietary regulation of copper absorption and storage in rats: effects of sodium, zinc and histidine-zinc." Journal of the American College of Nutrition 12, no. 6 (1993): 714–19. http://dx.doi.org/10.1080/07315724.1993.10718364.

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Tanaka, Natsuki, Miki Kawachi, Takashi Fujiwara, and Masayoshi Maeshima. "Zinc-binding and structural properties of the histidine-rich loop ofArabidopsis thalianavacuolar membrane zinc transporter MTP1." FEBS Open Bio 3, no. 1 (2013): 218–24. http://dx.doi.org/10.1016/j.fob.2013.04.004.

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Chen, Lan, and Xianhui Bu. "Histidine-Controlled Two-Dimensional Assembly of Zinc Phosphite Four-Ring Units." Chemistry of Materials 18, no. 7 (2006): 1857–60. http://dx.doi.org/10.1021/cm052801c.

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Loomans, Henry J., Beth L. Hahn, Qi‐Qin Li, Suhas H. Phadnis, and Peter G. Sohnle. "Histidine‐Based Zinc‐Binding Sequences and the Antimicrobial Activity of Calprotectin." Journal of Infectious Diseases 177, no. 3 (1998): 812–14. http://dx.doi.org/10.1086/517816.

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