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1

Choy, Tak-Kee, Chih-Yang Wang, Nam Nhut Phan, Hoang Dang Khoa Ta, Gangga Anuraga, Yen-Hsi Liu, Yung-Fu Wu, Kuen-Haur Lee, Jian-Ying Chuang, and Tzu-Jen Kao. "Identification of Dipeptidyl Peptidase (DPP) Family Genes in Clinical Breast Cancer Patients via an Integrated Bioinformatics Approach." Diagnostics 11, no. 7 (July 2, 2021): 1204. http://dx.doi.org/10.3390/diagnostics11071204.

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Breast cancer is a heterogeneous disease involving complex interactions of biological processes; thus, it is important to develop therapeutic biomarkers for treatment. Members of the dipeptidyl peptidase (DPP) family are metalloproteases that specifically cleave dipeptides. This family comprises seven members, including DPP3, DPP4, DPP6, DPP7, DPP8, DPP9, and DPP10; however, information on the involvement of DPPs in breast cancer is lacking in the literature. As such, we aimed to study their roles in this cancerous disease using publicly available databases such as cBioportal, Oncomine, and Kaplan–Meier Plotter. These databases comprise comprehensive high-throughput transcriptomic profiles of breast cancer across multiple datasets. Furthermore, together with investigating the messenger RNA expression levels of these genes, we also aimed to correlate these expression levels with breast cancer patient survival. The results showed that DPP3 and DPP9 had significantly high expression profiles in breast cancer tissues relative to normal breast tissues. High expression levels of DPP3 and DPP4 were associated with poor survival of breast cancer patients, whereas high expression levels of DPP6, DPP7, DPP8, and DPP9 were associated with good prognoses. Additionally, positive correlations were also revealed of DPP family genes with the cell cycle, transforming growth factor (TGF)-beta, kappa-type opioid receptor, and immune response signaling, such as interleukin (IL)-4, IL6, IL-17, tumor necrosis factor (TNF), and interferon (IFN)-alpha/beta. Collectively, DPP family members, especially DPP3, may serve as essential prognostic biomarkers in breast cancer.
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2

Funston, Alison M., Carleen Cullinane, Kenneth P. Ghiggino, W. David McFadyen, Stanley S. Stylli, and Peter A. Tregloan. "Dipyridophenazine Complexes of Cobalt(III): DNA Photocleavage and Photobiology." Australian Journal of Chemistry 58, no. 3 (2005): 206. http://dx.doi.org/10.1071/ch04206.

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The UV-visible spectroscopy and photochemistry of [Co(en)2(DPPZ)](ClO4)3 (DPPZ = dipyrido[3,2-a:2´,3´-c]-phenazine) in the presence of plasmid DNA and the nucleoside 2´-deoxygaunosine have been investigated. Evidence for the intercalation of the complex with DNA and photoinduced DNA strand breakage is found. The structurally related complexes [Co(en)2(DPPN)]Cl3 and [Co(en)2(DPPA)]Cl2, where DPPN = benzo[i]dipyrido[3,2-a:2´,3´-c]phenazine and DPPA = dipyrido[3,2-a:2´,3´-c] phenazine-11-carboxylic acid, have also been synthesized and characterized. In vitro cytotoxicity studies and photocytotoxicity studies of the complexes using the C6 rat glioma cell line are reported and indicate significant increases in toxicity following irradation.
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3

QI, Shu Y., Pierre J. RIVIERE, Jerzy TROJNAR, Jean-Louis JUNIEN, and Karen O. AKINSANYA. "Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases." Biochemical Journal 373, no. 1 (July 1, 2003): 179–89. http://dx.doi.org/10.1042/bj20021914.

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Two dipeptidyl peptidase IV (DPPIV, DPP4)-related proteins, DPP8 and DPP9, have been identified recently [Abbott, Yu, Woollatt, Sutherland, McCaughan, and Gorrell (2000) Eur. J. Biochem. 267, 6140–6150; Olsen and Wagtmann (2002) Gene 299, 185–193; Qi, Akinsanya, Riviere, and Junien (2002) Patent application WO0231134]. In the present study, we describe the cloning of DPP10, a novel 796-amino-acid protein, with significant sequence identity to DPP4 (32%) and DPP6 (51%) respectively. We propose that DPP10 is a new member of the S9B serine proteases subfamily. The DPP10 gene is located on the long arm of chromosome 2 (2q12.3-2q14.2), close to the DPP4 (2q24.3) and FAP (2q23) genes. The active-site serine residue is replaced by a glycine residue in DPP10, resulting in the loss of DPP activity. The serine residue is also replaced in DPP6, which lacks peptidase activity. DPP8 and DPP9 share an identical active site with DPP4 (Gly-Trp-Ser-Tyr-Gly). In contrast with the previous results suggesting that DPP9 is inactive, we show that DPP9 is a DPP, hydrolysing Ala-Pro-(7-amino-4-methyl-coumarin) with similar pH-specificity and protease-inhibitor-sensitivity to those of DPP4 and DPP8. Northern-blot analysis shows that whereas DPP8 and DPP9 are widely expressed, DPP10 is expressed mainly in the brain and pancreas. DPP6, which has the highest amino acid identity with DPP10, has been shown previously [Nadal, Ozaita, Amarillo, de Miera, Ma, Mo, Goldberg, Misumi, Ikehara, Neubert et al. (2003) Neuron 37, 449–461] to associate with A-type K+ channel subunits, modulating their transport and function in somatodendritic compartments of neurons. It is possible that DPP10 is involved in similar functions in the brain. Elucidation of the physiological or pathophysiological role of DPP8, DPP9 and DPP10 and characterization of their structure–function relationships will add impetus to the development of inhibitor molecules for pharmacological or therapeutic use.
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4

Al-Samrai, Osama'a A. Y., Ahmed S. M. Al-Janabi2, and Eman A. Othman1. "Mixed Ligand Complexes of Hg-tetrazole-thiolate with phosphine, Synthesis and spectroscopic studies." Tikrit Journal of Pure Science 24, no. 5 (September 13, 2019): 10. http://dx.doi.org/10.25130/j.v24i5.860.

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Seven new complexes [Hg(k1-ptt)2](1), [Hg(k1-ptt)2(dppm)](2), [Hg(k1-ptt)2(dppe)](3), [Hg(k1-ptt)2(dppp)](4), [Hg(k1-ptt)2(dppb)](5), [Hg(k1-ptt)2(dppf)] (6), and [Hg(k1-ptt)2(PPh3)2] (7) have been synthesized and characterized. The reaction of two moles equivalent of 1-Phenyl-1H-tetrazole-5-thiol (Hptt) with one mole equivalent of Hg(oAc)2.xH2O in ethanol solution afford [Hg(k1-ptt)2] (1). Treatment of (1) with one mole equivalent of diphos (diphos : dppm, dppe, dppp, dppb, dppf) or two moles equivalent of PPh3 afforded a complexes of the types [Hg(k1-ptt)2(diphos)] (2-6) or [Hg(k1-ptt)2(PPh3)2] (7). The prepared complexes have been characterized by CHNS elemental analyses, molar conductivity, IR and NMR (1H, 13C and 31P) spectroscopy. In all complexes, the ptt- ligand is bonded through the sulfur atom of deprotonated thiol group, whereas the diphosphine ligands bonded as bidentate chelating and PPh3 bonded as a monodentate, to afford a tetrahedral geometry around the Hg+2 ion. http://dx.doi.org/10.25130/tjps.24.2019.083
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5

Wilson, Claire H., Hui Emma Zhang, Mark D. Gorrell, and Catherine A. Abbott. "Dipeptidyl peptidase 9 substrates and their discovery: current progress and the application of mass spectrometry-based approaches." Biological Chemistry 397, no. 9 (September 1, 2016): 837–56. http://dx.doi.org/10.1515/hsz-2016-0174.

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Abstract The enzyme members of the dipeptidyl peptidase 4 (DPP4) gene family have the very unusual capacity to cleave the post-proline bond to release dipeptides from the N-terminus of peptide/protein substrates. DPP4 and related enzymes are current and potential therapeutic targets in the treatment of type II diabetes, inflammatory conditions and cancer. Despite this, the precise biological function of individual dipeptidyl peptidases (DPPs), other than DPP4, and knowledge of their in vivo substrates remains largely unknown. For many years, identification of physiological DPP substrates has been difficult due to limitations in the available tools. Now, with advances in mass spectrometry based approaches, we can discover DPP substrates on a system wide-scale. Application of these approaches has helped reveal some of the in vivo natural substrates of DPP8 and DPP9 and their unique biological roles. In this review, we provide a general overview of some tools and approaches available for protease substrate discovery and their applicability to the DPPs with a specific focus on DPP9 substrates. This review provides comment upon potential approaches for future substrate elucidation.
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6

Liang, Xi-Ling, and Li-Feng Tan. "Nucleic Acid (Calf Thymus-DNA, Yeast tRNA) Binding and Cytotoxic Properties of a Dinuclear (Ru,Co) Metal Polypyridyl Complex." Australian Journal of Chemistry 63, no. 10 (2010): 1453. http://dx.doi.org/10.1071/ch10178.

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Based on [L2Ru{DPPZ(11–11′)DPPZ}RuL2]4+ (where L = 1,10-phenanthroline or 2,2′-bipyridyl, DPPZ(11–11′)DPPZ = 11,11′-bi(dipyrido-[3,2-a:2′,3′-c]-phenazinyl)), a heterodinuclear (Ru,Co) metal polypyridyl complex [(phen)2Ru{DPPZ(11–11′)DPPZ}Co(phen)2]5+ (phen = 1,10-phenanthroline) has been designed and synthesized. A comparative study on the interaction of the complex with calf thymus DNA and yeast tRNA was investigated by UV-visible spectroscopy, fluorescence spectroscopy and viscosity measurements, as well as equilibrium dialysis and circular dichroism. The antitumour activities of the complex were evaluated by the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetraazolium bromide method and Giemsa staining experiment. These results indicate that the configuration and structures of nucleic acids have significant effects on the binding behaviours of metal complexes. Furthermore, the complex shows different antitumour activities against selected tumour cell lines, and can cause cell apoptosis.
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7

Di Pietro, Maria Letizia, Giuseppina La Ganga, Francesco Nastasi, and Fausto Puntoriero. "Ru(II)-Dppz Derivatives and Their Interactions with DNA: Thirty Years and Counting." Applied Sciences 11, no. 7 (March 29, 2021): 3038. http://dx.doi.org/10.3390/app11073038.

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Transition metal complexes with dppz-type ligands (dppz = dipyrido[3,2-a:2′,3′-c]phenazine) are extensively studied and attract a considerable amount of attention, becoming, from the very beginning and increasingly over time, a powerful tool for investigating the structure of the DNA helix. In particular, [Ru(bpy)2(dppz)]2+ and [Ru(phen)2(dppz)]2+ and their derivatives were extensively investigated as DNA light-switches. The purpose of this mini-review, which is not and could not be exhaustive, was to first introduce DNA and its importance at a biological level and research in the field of small molecules that are capable of interacting with it, in all its forms. A brief overview is given of the results obtained on the Ru-dppz complexes that bind to DNA. The mechanism of the light-switch active in this type of species is also briefly introduced along with its effects on structural modifications on both the dppz ligand and the ancillary ligands. Finally, a brief mention is made of biological applications and the developments obtained due to new spectroscopic techniques, both for understanding the mechanism of action and for cellular imaging applications.
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8

Shahabadi, Nahid, and Maryam Mahdavi. "DNA Interaction Studies of a Cobalt(II) Mixed-Ligand Complex Containing Two Intercalating Ligands: 4,7-Dimethyl-1, 10-Phenanthroline and Dipyrido[3,2-a:2′,3′-c]phenazine." ISRN Inorganic Chemistry 2013 (December 30, 2013): 1–7. http://dx.doi.org/10.1155/2013/604218.

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A new cobalt(II) complex [Co(dppz)2(4,7-dmp)]2+ (4,7-dmp = 4,7-dimethyl-1,10-phenanthrolline) and dppz = dipyrido[3,2-a:2′-3′-c]phenazine has been synthesized and characterized by elemental analysis (CHN), FT-IR, and UV-visible (UV-Vis) spectroscopic techniques. The DNA-binding property of the complex has been investigated employing absorption spectroscopy, fluorescence spectroscopy, circular dichroism, and viscosity measurements. The experimental results show that the complex can bind to DNA in an intercalation mode. In comparison with previous study, the DNA-binding affinity of [Co(dppz)2(4,7-dmp)]2+ (Kb=1.1·106 M−1) is smaller than that of complex [Co(dppz)2(2,9-dmp)]2+ (Kb=2.5·106 M−1).
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9

He, Xiaojun, Lianhe Jin, and Lifeng Tan. "DNA-binding, topoisomerases I and II inhibition and in vitro cytotoxicity of ruthenium(II) polypyridyl complexes: [Ru(dppz)2L]2+ (L=dppz-11-CO2Me and dppz)." Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 135 (January 2015): 101–9. http://dx.doi.org/10.1016/j.saa.2014.06.147.

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10

Rochford, Garret, Zara Molphy, Kevin Kavanagh, Malachy McCann, Michael Devereux, Andrew Kellett, and Orla Howe. "Cu(ii) phenanthroline–phenazine complexes dysregulate mitochondrial function and stimulate apoptosis." Metallomics 12, no. 1 (2020): 65–78. http://dx.doi.org/10.1039/c9mt00187e.

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Herein we report the central role of the mitochondria in the cytotoxicity of four developmental cytotoxic copper(ii) complexes [Cu(phen)2]2+, [Cu(DPQ)(Phen)]2+, [Cu(DPPZ)(Phen)]2+ and [Cu(DPPN)(Phen)]2+ superior to cisplatin and independent of resistance in a range of cells.
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11

Smith, Jr., Dale C., Jérémie Cadoret, Laleh Jafarpour, Edwin D. Stevens, and Steven P. Nolan. "Synthetic and solution calorimetric investigations of chelating phosphine ligands in Ru(allyl)2(PP) complexes (PP = diphosphine)." Canadian Journal of Chemistry 79, no. 5-6 (May 1, 2001): 626–31. http://dx.doi.org/10.1139/v00-164.

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Reaction enthalpies of (COD)Ru(allyl)2 (COD = η4-1,5-cyclooctadiene; allyl = 2-methylpropenyl) with a series of bidentate phosphines (dppm, dppf, dppe, dppb, dppp, depe, dmpe) have been measured by anaerobic solution calorimetry. The relative stability of the resulting complexes is strongly influenced by the electronic donor properties of the bidentate phosphine ligand. Reactions involving ligands that are better σP) donors result in higher enthalpy values and, therefore, more thermodynamically stable complexes. Additionally, the synthesis and characterization of two new ruthenium allyl complexes Ru(allyl)2(dppf) (3) and Ru(allyl)2(depe) (8) and the X-ray crystal structure of 3 are reported.Key words: ruthenium, allyl, solution calorimetry, thermodynamics, X-ray structure.
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12

Mårtensson, Anna K. F., and Per Lincoln. "Binding of Ru(terpyridine)(pyridine)dipyridophenazine to DNA studied with polarized spectroscopy and calorimetry." Dalton Transactions 44, no. 8 (2015): 3604–13. http://dx.doi.org/10.1039/c4dt02642j.

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Achiral Ru(tpy)(py)dppz2+ intercalated into DNA has similar intermolecular interactions as opposite enantiomers of its structural isomer, the “light-switch” complex Ru(bpy)2dppz2+.
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13

Savić, Aleksandar, Anna M. Kaczmarek, Rik Van Deun, and Kristof Van Hecke. "DNA Intercalating Near-Infrared Luminescent Lanthanide Complexes Containing Dipyrido[3,2-a:2′,3′-c]phenazine (dppz) Ligands: Synthesis, Crystal Structures, Stability, Luminescence Properties and CT-DNA Interaction." Molecules 25, no. 22 (November 13, 2020): 5309. http://dx.doi.org/10.3390/molecules25225309.

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In order to create near-infrared (NIR) luminescent lanthanide complexes suitable for DNA-interaction, novel lanthanide dppz complexes with general formula [Ln(NO3)3(dppz)2] (Ln = Nd3+, Er3+ and Yb3+; dppz = dipyrido[3,2-a:2′,3′-c]phenazine) were synthesized, characterized and their luminescence properties were investigated. In addition, analogous compounds with other lanthanide ions (Ln = Ce3+, Pr3+, Sm3+, Eu3+, Tb3+, Dy3+, Ho3+, Tm3+, Lu3+) were prepared. All complexes were characterized by IR spectroscopy and elemental analysis. Single-crystal X-ray diffraction analysis of the complexes (Ln = La3+, Ce3+, Pr3+, Nd3+, Eu3+, Er3+, Yb3+, Lu3+) showed that the lanthanide’s first coordination sphere can be described as a bicapped dodecahedron, made up of two bidentate dppz ligands and three bidentate-coordinating nitrate anions. Efficient energy transfer was observed from the dppz ligand to the lanthanide ion (Nd3+, Er3+ and Yb3+), while relatively high luminescence lifetimes were detected for these complexes. In their excitation spectra, the maximum of the strong broad band is located at around 385 nm and this wavelength was further used for excitation of the chosen complexes. In their emission spectra, the following characteristic NIR emission peaks were observed: for a) Nd3+: 4F3/2 → 4I9/2 (870.8 nm), 4F3/2 → 4I11/2 (1052.7 nm) and 4F3/2 → 4I13/2 (1334.5 nm); b) Er3+: 4I13/2 → 4I15/2 (1529.0 nm) c) Yb3+: 2F5/2 → 2F7/2 (977.6 nm). While its low triplet energy level is ideally suited for efficient sensitization of Nd3+ and Er3+, the dppz ligand is considered not favorable as a sensitizer for most of the visible emitting lanthanide ions, due to its low-lying triplet level, which is too low for the accepting levels of most visible emitting lanthanides. Furthermore, the DNA intercalation ability of the [Nd(NO3)3(dppz)2] complex with calf thymus DNA (CT-DNA) was confirmed using fluorescence spectroscopy.
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14

Chao, Xi-Juan, Miao Tang, Rong Huang, Chun-Hua Huang, Jie Shao, Zhu-Ying Yan, and Ben-Zhan Zhu. "Targeted live-cell nuclear delivery of the DNA ‘light-switching’ Ru(II) complex via ion-pairing with chlorophenolate counter-anions: the critical role of binding stability and lipophilicity of the ion-pairing complexes." Nucleic Acids Research 47, no. 20 (October 4, 2019): 10520–28. http://dx.doi.org/10.1093/nar/gkz152.

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Abstract We have found recently that nuclear uptake of the cell-impermeable DNA light-switching Ru(II)-polypyridyl cationic complexes such as [Ru(bpy)2(dppz)]Cl2 was remarkably enhanced by pentachlorophenol (PCP), by forming ion-pairing complexes via a passive diffusion mechanism. However, it is not clear whether the enhanced nuclear uptake of [Ru(bpy)2(dppz)]2+ is only limited to PCP, or it is a general phenomenon for other highly chlorinated phenols (HCPs); and if so, what are the major physicochemical factors in determining nuclear uptake? Here, we found that the nuclear uptake of [Ru(bpy)2(dppz)]2+ can also be facilitated by other two groups of HCPs including three tetrachlorophenol (TeCP) and six trichlorophenol (TCP) isomers. Interestingly and unexpectedly, 2,3,4,5-TeCP was found to be the most effective one for nuclear delivery of [Ru(bpy)2(dppz)]2+, which is even better than the most-highly chlorinated PCP, and much better than its two other TeCP isomers. Further studies showed that the nuclear uptake of [Ru(bpy)2(dppz)]2+ was positively correlated with the binding stability, but to our surprise, inversely correlated with the lipophilicity of the ion-pairing complexes formed between [Ru(bpy)2(dppz)]Cl2 and HCPs. These findings should provide new perspectives for future investigations on using ion-pairing as an effective method for delivering other bio-active metal complexes into their intended cellular targets.
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15

Higgs, P. L., A. W. McKinley, and E. M. Tuite. "[Ru(phen)2dppz]2+ luminescence reveals nanoscale variation of polarity in the cyclodextrin cavity." Chemical Communications 52, no. 9 (2016): 1883–86. http://dx.doi.org/10.1039/c5cc09755j.

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Insertion of dppz with phosphorylated β-cyclodextrin results in multi-exponential [Ru(phen)2dppz]2+ emission; binding is weaker than [Ru(phen)3]2+, but shows stereoselectivity.
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16

Wijaya, Karna, Daryono H. Tjahjono, Naoki Yoshioka, and Hidenari Inoue. "DNA-Binding Properties of Iron(II) Mixed-Ligand Complexes Containing 1,10-Phenanthroline and Dipyrido[3,2-a:2’,3’-c]phenazine." Zeitschrift für Naturforschung B 59, no. 3 (March 1, 2004): 310–18. http://dx.doi.org/10.1515/znb-2004-0313.

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An iron(II) mixed-ligand complex with 1,10-phenanthroline (phen) and dipyrido[3,2-a:2’,3’- c]phenazine (dppz), [Fe(phen)2(dppz)]2+, has been synthesized. The DNA-binding properties of the mixed-ligand complex have been studied in terms of equilibrium binding constant, thermodynamic parameter, thermal denaturation as well as Pfeiffer effect upon binding to DNA. The spectrophotometric titration of [Fe(phen)2(dppz)]2+ with calf thymus DNA (ct-DNA) has shown that the iron(II) mixed-ligand complex binds effectively to ct-DNA in an intercalation mode as indicated by remarkable hypochromicity (ca. 36%) and moderate bathochromic shift (8 nm) of the absorption spectra. This intercalative mode is supported by a significant increase (Δ Tm = 21 °C) in the melting temperature (Tm) of ct-DNA at R([complex]/[ct-DNA]) = 1.5. The binding of [Fe(phen)2(dppz)]2+ to ct-DNA is entropically driven as characterized by a positive enthalpy change and a large negative TΔ S term. An intense CD signal in the UV and visible region develops upon addition of ct-DNA to the racemate solution of [Fe(phen)2(dppz)]2+. This has revealed that a shift in diastereomeric inversion equilibrium takes place in the solution to yield an excess of one enantiomer of the DNA-iron(II) complex (Pfeiffer effect). The striking resemblance of the CD spectral profiles to those of the corresponding Δ -enantiomer indicates that Δ -[Fe(phen)2(dppz)]2+ is preferentially bound to ct-DNA
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17

Nagaraj, Karuppiah, Krishnan Senthil Murugan, Pilavadi Thangamuniyandi, and Subramanian Sakthinathan. "Nucleic acid binding study of surfactant copper(ii) complex containing dipyrido[3,2-a:2′-3′-c]phenazine ligand as an intercalator: in vitro antitumor activity of complex in human liver carcinoma (HepG2) cancer cells." RSC Adv. 4, no. 99 (2014): 56084–94. http://dx.doi.org/10.1039/c4ra08049a.

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A new surfactant copper(ii) complex, [Cu(dppz)2DA](ClO4)2, where dppz = dipyrido[3,2-a:2′-3′-c]phenazine and DA-dodecylamine, has been synthesized and characterized by physico-chemical and spectroscopic methods.
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18

Hall, James P., Hanna Beer, Katrin Buchner, David J. Cardin, and Christine J. Cardin. "Preferred orientation in an angled intercalation site of a chloro-substituted Λ -[Ru(TAP) 2 (dppz)] 2+ complex bound to d(TCGGCGCCGA) 2." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 371, no. 1995 (July 28, 2013): 20120525. http://dx.doi.org/10.1098/rsta.2012.0525.

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The crystal structure of the ruthenium DNA ‘light-switch’ complex Λ -[Ru(TAP) 2 (11-Cl-dppz)] 2+ (TAP=tetraazaphenanthrene, dppz=dipyrido[3,2- a ′:2′,3′- c ]phenazine) bound to the oligonucleotide duplex d(TCGGCGCCGA) 2 is reported. The synthesis of the racemic ruthenium complex is described for the first time, and the racemate was used in this study. The crystal structure, at atomic resolution (1.0 Å), shows one ligand as a wedge in the minor groove, resulting in the 51 ° kinking of the double helix, as with the parent Λ -[Ru(TAP) 2 (dppz)] 2+ . Each complex binds to one duplex by intercalation of the dppz ligand and also by semi-intercalation of one of the orthogonal TAP ligands into a second symmetrically equivalent duplex. The 11-chloro substituent binds with the major component (66%) oriented with the 11-chloro substituent on the purine side of the terminal step of the duplex.
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19

Huang, Jiali Carrie, Abdullah Al Emran, Justine Moreno Endaya, Geoffrey W. McCaughan, Mark D. Gorrell, and Hui Emma Zhang. "DPP9: Comprehensive In Silico Analyses of Loss of Function Gene Variants and Associated Gene Expression Signatures in Human Hepatocellular Carcinoma." Cancers 13, no. 7 (April 1, 2021): 1637. http://dx.doi.org/10.3390/cancers13071637.

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Dipeptidyl peptidase (DPP) 9, DPP8, DPP4 and fibroblast activation protein (FAP) are the four enzymatically active members of the S9b protease family. Associations of DPP9 with human liver cancer, exonic single nucleotide polymorphisms (SNPs) in DPP9 and loss of function (LoF) variants have not been explored. Human genomic databases, including The Cancer Genome Atlas (TCGA), were interrogated to identify DPP9 LoF variants and associated cancers. Survival and gene signature analyses were performed on hepatocellular carcinoma (HCC) data. We found that DPP9 and DPP8 are intolerant to LoF variants. DPP9 exonic LoF variants were most often associated with uterine carcinoma and lung carcinoma. All four DPP4-like genes were overexpressed in liver tumors and their joint high expression was associated with poor survival in HCC. Increased DPP9 expression was associated with obesity in HCC patients. High expression of genes that positively correlated with overexpression of DPP4, DPP8, and DPP9 were associated with very poor survival in HCC. Enriched pathways analysis of these positively correlated genes featured Toll-like receptor and SUMOylation pathways. This comprehensive data mining suggests that DPP9 is important for survival and that the DPP4 protease family, particularly DPP9, is important in the pathogenesis of human HCC.
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20

Ross, Breyan, Stephan Krapp, Martin Augustin, Reiner Kierfersauer, Marcelino Arciniega, Ruth Geiss-Friedlander, and Robert Huber. "Structures and mechanism of dipeptidyl peptidases 8 and 9, important players in cellular homeostasis and cancer." Proceedings of the National Academy of Sciences 115, no. 7 (January 30, 2018): E1437—E1445. http://dx.doi.org/10.1073/pnas.1717565115.

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Dipeptidyl peptidases 8 and 9 are intracellular N-terminal dipeptidyl peptidases (preferentially postproline) associated with pathophysiological roles in immune response and cancer biology. While the DPP family member DPP4 is extensively characterized in molecular terms as a validated therapeutic target of type II diabetes, experimental 3D structures and ligand-/substrate-binding modes of DPP8 and DPP9 have not been reported. In this study we describe crystal and molecular structures of human DPP8 (2.5 Å) and DPP9 (3.0 Å) unliganded and complexed with a noncanonical substrate and a small molecule inhibitor, respectively. Similar to DPP4, DPP8 and DPP9 molecules consist of one β-propeller and α/β hydrolase domain, forming a functional homodimer. However, they differ extensively in the ligand binding site structure. In intriguing contrast to DPP4, where liganded and unliganded forms are closely similar, ligand binding to DPP8/9 induces an extensive rearrangement at the active site through a disorder-order transition of a 26-residue loop segment, which partially folds into an α-helix (R-helix), including R160/133, a key residue for substrate binding. As vestiges of this helix are also seen in one of the copies of the unliganded form, conformational selection may contributes to ligand binding. Molecular dynamics simulations support increased flexibility of the R-helix in the unliganded state. Consistently, enzyme kinetics assays reveal a cooperative allosteric mechanism. DPP8 and DPP9 are closely similar and display few opportunities for targeted ligand design. However, extensive differences from DPP4 provide multiple cues for specific inhibitor design and development of the DPP family members as therapeutic targets or antitargets.
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21

Phillips, Tim, Ihtshamul Haq, Anthony J. H. M. Meijer, Harry Adams, Ian Soutar, Linda Swanson, Matthew J. Sykes, and Jim A. Thomas. "DNA Binding of an Organic dppz-Based Intercalator†." Biochemistry 43, no. 43 (November 2004): 13657–65. http://dx.doi.org/10.1021/bi049146r.

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22

Shi, Shuo, Jin-Hong Xu, Xing Gao, Hai-Liang Huang, and Tian-Ming Yao. "Binding Behaviors for Different Types of DNA G-Quadruplexes: Enantiomers of [Ru(bpy)2(L)]2+(L=dppz, dppz-idzo)." Chemistry - A European Journal 21, no. 32 (June 26, 2015): 11435–45. http://dx.doi.org/10.1002/chem.201501093.

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23

van der Salm, Holly, Christopher B. Larsen, James R. W. McLay, Michael G. Fraser, Nigel T. Lucas, and Keith C. Gordon. "Stretching the phenazine MO in dppz: the effect of phenyl and phenyl–ethynyl groups on the photophysics of Re(i) dppz complexes." Dalton Trans. 43, no. 47 (2014): 17775–85. http://dx.doi.org/10.1039/c4dt01415d.

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24

Bouzada, David, Iria Salvadó, Ghofrane Barka, Gustavo Rama, José Martínez-Costas, Romina Lorca, Álvaro Somoza, Manuel Melle-Franco, M. Eugenio Vázquez, and Miguel Vázquez López. "Selective G-quadruplex binding by oligoarginine-Ru(dppz) metallopeptides." Chemical Communications 54, no. 6 (2018): 658–61. http://dx.doi.org/10.1039/c7cc08286j.

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We demonstrate that both the R8 functionalization and its interplay with the ancillary ligand have and an important role in the G-quadruplex recognition process by Ru(dppz) metallopeptides.
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25

Moncada, Alejandra Saavedra, Eduart Gutiérrez-Pineda, Iván Maisuls, Gustavo T. Ruiz, Alexander G. Lappin, Guillermo J. Ferraudi, and Ezequiel Wolcan. "Photochemical properties of a Re(I) polymer containing dppz in its structure. An interplay between dark and bright states of dppz." Journal of Photochemistry and Photobiology A: Chemistry 353 (February 2018): 86–100. http://dx.doi.org/10.1016/j.jphotochem.2017.11.007.

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26

Klein, Axel, Natascha Hurkes, André Kaiser, and Wolfram Wielandt. "π-Stacking Modulates the Luminescence of [(dppz)Ni(Mes)Br] (dppz = dipyrido[3,2-a:2′,3′-c]phenazine, Mes = 2,4,6-trimethylphenyl)." Zeitschrift für anorganische und allgemeine Chemie 633, no. 10 (August 2007): 1659–65. http://dx.doi.org/10.1002/zaac.200700082.

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27

Li, Guanying, Lingli Sun, Liangnian Ji, and Hui Chao. "Ruthenium(ii) complexes with dppz: from molecular photoswitch to biological applications." Dalton Transactions 45, no. 34 (2016): 13261–76. http://dx.doi.org/10.1039/c6dt01624c.

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The present article describes the recent advances in biological applications of the Ru-dppz systems in DNA binding, cellular imaging, anticancer drugs, phototherapy, protein aggregation detecting and chemosensors.
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28

van der Salm, Holly, Christopher B. Larsen, James R. W. McLay, Gregory S. Huff, and Keith C. Gordon. "Effects of protonation on the optical and photophysical properties of ReCl(CO)3(dppz–TAA) and [Ru(bpy)2(dppz–TAA)]2+." Inorganica Chimica Acta 428 (March 2015): 1–7. http://dx.doi.org/10.1016/j.ica.2015.01.006.

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29

Santos, Teresa M., João Madureira, Brian J. Goodfellow, Michael G. B. Drew, Júlio Pedrosa de Jesus, and Vitor Félix. "Interaction of Ruthenium(II)-dipyridophenazine Complexes with CT-DNA: Effects of the Polythioether Ancillary Ligands." Metal-Based Drugs 8, no. 3 (January 1, 2001): 125–36. http://dx.doi.org/10.1155/mbd.2001.125.

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The complexes [Ru([9]aneS3)(dppz)Cl]Cl 1 and [Ru([12]aneS4)(dppz)]Cl2,2 ([9]aneS3 = 1,4,7- trithiaciclononane and [12]aneS4 = 1,4,7,10-tetrathiaciclododecane) were synthesised and fully characterised . These complexes belong to a small family of dipyridophenazine complexes with non-polypyridyl ancillary ligands . Interaction studies of these complexes with CT-DNA (UV/Vis titrations, steady-state emission and thermal denaturation) revealed their high affinity for DNA . Intercalation constants determined by UV/Vis titrations are of the same order of magnitude (106) as other dppz metallointercalators, namely [Ru(II)(bpy)2dppz]S2+. Differences between l and2 were identified by steady-state emission and thermal denaturation studies . Emission results are in accordance with structural data, which indicate how geometric distortions and different donor and/or acceptor ligand abilities affect luminescence . The possibility of noncovalent interactions between ancillary ligands and nucleobases by van der Waals contacts and H-bridges is discussed . Furthermore, complex l undergoes aquation under intra-cellular conditions and an equilibrium with the aquated form l' is attained . This behaviour may increase the diversity of available interaction modes.
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30

Coates, Colin G., John J. McGarvey, Steven E. J. Bell, Luc Jacquet, John M. Kelly, Tia Keyes, and Johannes G. Vos. "Transient Resonance Raman Studies of Ru(II) Complexes in DNA and in Homogeneous Media." Laser Chemistry 19, no. 1-4 (January 1, 1999): 237–43. http://dx.doi.org/10.1155/1999/74587.

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Transient resonance Raman (TR2) spectroscopy has been used to investigate the metalligand charge-transfer (MLCT) excited states of Ru(II) polypyridyl complexes inDNAand in homogeneous solution. In DNA, complexes of the type [Ru(L)2(L′)]2+ were studied, where L=2, 2’-bipyridyl (bpy), 1,4, 5, 8-tetraazaphenanthrene (tap), and L′ dipyrido [3,2:a-2′ ,3′:c]-phenazine (dppz) or 1,4,5,8,9,12-hexaazatriphenylene (HAT). For [Ru(bpy)2(HAT)]2+, the enhancement pattern of vibrational modes in the TR2 spectra attributable to reduced HAT⋅− in the triplet MLCT state suggest perturbations to the intraligand transition of HAT⋅− in the presence of DNA. Transient RR spectra for [Ru(tap)2(dppz)]2+ are indicative of formation of the species RunII(tap⋅−)(tap)(dppz) by electron transfer from DNA to the triplet MLCT state of the complex.TR2 spectra for complexes of the type, [(Ru(bpy)2)n(L)]2+ , n=1, 2 where L=a triazole bridging ligand, illustrate the use of the technique as a probe of the response of MLCT states to the electronic environment.
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31

Alsaedi, Sammar, Bandar A. Babgi, Magda H. Abdellattif, Muhammad N. Arshad, Abdul-Hamid M. Emwas, Mariusz Jaremko, Mark G. Humphrey, Abdullah M. Asiri, and Mostafa A. Hussien. "DNA-Binding and Cytotoxicity of Copper(I) Complexes Containing Functionalized Dipyridylphenazine Ligands." Pharmaceutics 13, no. 5 (May 20, 2021): 764. http://dx.doi.org/10.3390/pharmaceutics13050764.

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A set of copper(I) coordination compounds with general formula [CuBr(PPh3)(dppz-R)] (dppz-R = dipyrido[3,2-a:2’,3’-c]phenazine (Cu-1), 11-nitrodipyrido[3,2-a:2’,3’-c]phenazine (Cu-2), 11-cyanodipyrido[3,2-a:2’,3’-c]phenazine (Cu-3), dipyrido[3,2-a:2’,3’-c]phenazine-11-phenone (Cu-4), 11,12-dimethyldipyrido[3,2-a:2’,3’-c]phenazine (Cu-5)) have been prepared and characterized by elemental analysis, 1H-NMR and 31P-NMR spectroscopies as well as mass spectrometry. The structure of Cu-1 was confirmed by X-ray crystallography. The effect of incorporating different functional groups on the dppz ligand on the binding into CT-DNA was evaluated by absorption spectroscopy, fluorescence quenching of EtBr-DNA adducts, and viscosity measurements. The functional groups affected the binding modes and hence the strength of binding affinities, as suggested by the changes in the relative viscosity. The differences in the quenching constants (Ksv) obtained from the fluorescence quenching assay highlight the importance of the functional groups in altering the binding sites on the DNA. The molecular docking data support the DNA-binding studies, with the sites and mode of interactions against B-DNA changing with the different functional groups. Evaluation of the anticancer activities of the five copper compounds against two different cancer cell lines (M-14 and MCF-7) indicated the importance of the functional groups on the dppz ligand on the anticancer activities. Among the five copper complexes, the cyano-containing complex (Cu-3) has the best anticancer activities.
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32

Coogan, M. P., and J. A. Platts. "Blue rhenium tricarbonyl DPPZ complexes – low energy charge-transfer absorption at tissue-penetrating wavelengths." Chemical Communications 52, no. 84 (2016): 12498–501. http://dx.doi.org/10.1039/c6cc07125b.

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33

Chen, Xiangke, Zishuai Huang, Wei Hua, Hardy Castada, and Heather C. Allen. "Reorganization and Caging of DPPC, DPPE, DPPG, and DPPS Monolayers Caused by Dimethylsulfoxide Observed Using Brewster Angle Microscopy." Langmuir 26, no. 24 (December 21, 2010): 18902–8. http://dx.doi.org/10.1021/la102842a.

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34

Kawano, Hiroyuki, Rie Tanaka, Tomoko Fujikawa, Katsuma Hiraki, and Masayoshi Onishi. "Novel Dihydridoruthenium(II) Complexes with Chelating Diphosphine Ligands, RuH2(CO)(diphosphine)(PPh3) (diphosphine = dppe, dppp, dppb, and dppf)." Chemistry Letters 28, no. 5 (May 1999): 401–2. http://dx.doi.org/10.1246/cl.1999.401.

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35

Roy, Nilmadhab, Utsav Sen, Shreya Ray Chaudhuri, Venkatesan Muthukumar, Prithvi Moharana, Priyankar Paira, Bipasha Bose, Ashna Gauthaman, and Anbalagan Moorthy. "Mitochondria specific highly cytoselective iridium(iii)–Cp* dipyridophenazine (dppz) complexes as cancer cell imaging agents." Dalton Transactions 50, no. 6 (2021): 2268–83. http://dx.doi.org/10.1039/d0dt03586f.

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36

Liu, Xue-Wen, Jun Li, Hong Li, Kang-Cheng Zheng, Hui Chao, and Liang-Nian Ji. "Synthesis, characterization, DNA-binding and photocleavage of complexes [Ru(phen)2(6-OH-dppz)]2+ and [Ru(phen)2(6-NO2-dppz)]2+." Journal of Inorganic Biochemistry 99, no. 12 (December 2005): 2372–80. http://dx.doi.org/10.1016/j.jinorgbio.2005.09.004.

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37

McQuaid, Kane, James P. Hall, Lena Baumgaertner, David J. Cardin, and Christine J. Cardin. "Three thymine/adenine binding modes of the ruthenium complex Λ-[Ru(TAP)2(dppz)]2+ to the G-quadruplex forming sequence d(TAGGGTT) shown by X-ray crystallography." Chemical Communications 55, no. 62 (2019): 9116–19. http://dx.doi.org/10.1039/c9cc04316k.

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38

Liu, Clive, Patricia Marshall, Ian Schreibman, Ann Vu, Weiming Gai, and Michael Whitlow. "Interaction Between Terminal Complement Proteins C5b-7 and Anionic Phospholipids." Blood 93, no. 7 (April 1, 1999): 2297–301. http://dx.doi.org/10.1182/blood.v93.7.2297.407k19_2297_2301.

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We have recently shown that C5b-6 binds to the erythrocyte membrane via an ionic interaction with sialic acid before the addition of C7 and subsequent membrane insertion. In this study we assessed the role of anionic lipids in the binding of the terminal complement proteins to the membrane and the efficiency of subsequent hemolysis. Human erythrocytes were modified by insertion of dipalmitoyl phosphatidylcholine (DPPC), dipalmitoyl phosphatidylserine (DPPS), dipalmitoyl phosphatidylethanolamine (DPPE), or dipalmitoyl phosphatidic acid (DPPA). Lipid incorporation and the hemolytic assays were done in the presence of 100 μmol/L sodium orthovanadate to prevent enzymatic redistribution of lipid. We found that the neutral lipids, DPPC and DPPE, did not affect C5b-7 uptake or hemolysis by C5b-9. In contrast, the two acidic phospholipids, DPPS and DPPA, caused a dose-dependent increase in both lysis and C5b-7 uptake. We conclude that the presence of anionic lipids on the exterior face of the membrane increases C5b-7 uptake and subsequent hemolysis. It is known that sickle cell erythrocytes have increased exposure of phosphatidylserine on their external face and are abnormally sensitive to lysis by C5b-9. The data presented here provide a plausible mechanism for this increased sensitivity.
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39

Kuhnt, Christian, Michael Karnahl, Stefanie Tschierlei, Kristin Griebenow, Michael Schmitt, Bernhard Schäfer, Sven Krieck, et al. "Substitution-controlled ultrafast excited-state processes in Ru–dppz-derivatives." Phys. Chem. Chem. Phys. 12, no. 6 (2010): 1357–68. http://dx.doi.org/10.1039/b915770k.

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40

Bates, W. Doug, Pingyun Chen, Dana M. Dattelbaum, Wayne E. Jones, and Thomas J. Meyer. "Excited State Competition infac-[ReI(dppz)(CO)3(py-PTZ)]+." Journal of Physical Chemistry A 103, no. 27 (July 1999): 5227–31. http://dx.doi.org/10.1021/jp990543z.

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41

Holmlin, R. Erik, and Jacqueline K. Barton. "Os(phen)2(dppz)2+: A Red-Emitting DNA Probe." Inorganic Chemistry 34, no. 1 (January 1995): 7–8. http://dx.doi.org/10.1021/ic00105a004.

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42

Yu, Hui-juan, Jiang-ping Liu, Zhi-feng Hao, Jun He, Ming Sun, Sheng Hu, Lin Yu, and Hui Chao. "Synthesis, characterization and biological evaluation of ruthenium(II) complexes [Ru(dtzp)(dppz)Cl] + and [Ru(dtzp)(dppz)CH 3 CN] 2+ for photodynamic therapy." Dyes and Pigments 136 (January 2017): 416–26. http://dx.doi.org/10.1016/j.dyepig.2016.08.059.

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43

Gao, Xing, Shuo Shi, Jun-Liang Yao, Juan Zhao, and Tian-Ming Yao. "Impacts of terminal modification of [Ru(phen)2dppz]2+on the luminescence properties: a theoretical study." Dalton Transactions 44, no. 44 (2015): 19264–74. http://dx.doi.org/10.1039/c5dt03373j.

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44

Hayashi, Yuichiro, Ami Morimoto, Takeshi Maeda, Toshiaki Enoki, Yousuke Ooyama, Yasunori Matsui, Hiroshi Ikeda, and Shigeyuki Yagi. "Synthesis of novel π-extended D–A–D-type dipyrido[3,2-a:2′,3′-c]phenazine derivatives and their photosensitized singlet oxygen generation." New Journal of Chemistry 45, no. 4 (2021): 2264–75. http://dx.doi.org/10.1039/d0nj05526c.

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45

Chengke, Wu, An Xiaoyu, Yue yuanyuan Yue yuanyuan, Feng Suling, and Niu Xiaoqing. "Effect of polypyridine copper complex [Cu(dppz)(l-Ser)]NO3·H2O on the stabilization of triplex DNA based on gold-nanoparticles." Analytical Methods 7, no. 8 (2015): 3425–30. http://dx.doi.org/10.1039/c5ay00139k.

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46

Schoch, Thomas K., John L. Hubbard, Christopher R. Zoch, Geun-Bae Yi, and Morten Sørlie. "Synthesis and Structure of the Ruthenium(II) Complexes [(η-C5Me5)Ru(NO)(bipy)]2+and [(η-C5Me5)Ru(NO)(dppz)]2+. DNA Cleavage by an Organometallic dppz Complex (bipy = 2,2‘-Bipyridine; dppz = Dipyrido[3,2-a:2‘,3‘-c]phenazine)." Inorganic Chemistry 35, no. 15 (January 1996): 4383–90. http://dx.doi.org/10.1021/ic950743z.

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47

Devereux, Stephen J., Páraic M. Keane, Suni Vasudevan, Igor V. Sazanovich, Michael Towrie, Qian Cao, Xue-Zhong Sun, et al. "Study of picosecond processes of an intercalated dipyridophenazine Cr(iii) complex bound to defined sequence DNAs using transient absorption and time-resolved infrared methods." Dalton Trans. 43, no. 47 (2014): 17606–9. http://dx.doi.org/10.1039/c4dt01989j.

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48

Sun, Weize, Rena Boerhan, Na Tian, Yang Feng, Jian Lu, Xuesong Wang, and Qianxiong Zhou. "Fluorination in enhancing photoactivated antibacterial activity of Ru(ii) complexes with photo-labile ligands." RSC Advances 10, no. 42 (2020): 25364–69. http://dx.doi.org/10.1039/d0ra01806f.

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Fluorination in the dppz ligand efficiently enhanced the photoactivated antibacterial activity of Ru(ii) complexes with photo-labile ligands against antibiotic-resistant bacteria both under normoxic and hypoxic conditions.
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49

Liu, Clive, Patricia Marshall, Ian Schreibman, Ann Vu, Weiming Gai, and Michael Whitlow. "Interaction Between Terminal Complement Proteins C5b-7 and Anionic Phospholipids." Blood 93, no. 7 (April 1, 1999): 2297–301. http://dx.doi.org/10.1182/blood.v93.7.2297.

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Abstract We have recently shown that C5b-6 binds to the erythrocyte membrane via an ionic interaction with sialic acid before the addition of C7 and subsequent membrane insertion. In this study we assessed the role of anionic lipids in the binding of the terminal complement proteins to the membrane and the efficiency of subsequent hemolysis. Human erythrocytes were modified by insertion of dipalmitoyl phosphatidylcholine (DPPC), dipalmitoyl phosphatidylserine (DPPS), dipalmitoyl phosphatidylethanolamine (DPPE), or dipalmitoyl phosphatidic acid (DPPA). Lipid incorporation and the hemolytic assays were done in the presence of 100 μmol/L sodium orthovanadate to prevent enzymatic redistribution of lipid. We found that the neutral lipids, DPPC and DPPE, did not affect C5b-7 uptake or hemolysis by C5b-9. In contrast, the two acidic phospholipids, DPPS and DPPA, caused a dose-dependent increase in both lysis and C5b-7 uptake. We conclude that the presence of anionic lipids on the exterior face of the membrane increases C5b-7 uptake and subsequent hemolysis. It is known that sickle cell erythrocytes have increased exposure of phosphatidylserine on their external face and are abnormally sensitive to lysis by C5b-9. The data presented here provide a plausible mechanism for this increased sensitivity.
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50

Liu, Guocheng, Shuang Liang, Qiaomin Li, Jiao Guo, Na Xu, Xiuli Wang, Yan Li, and Baokuan Chen. "Metal/N-donor-induced versatile structures and properties of seven 0D → 3D complexes based on dpq/dppz and O-bridged tricarboxylate: fluorescence and electrochemical behaviors." CrystEngComm 22, no. 7 (2020): 1209–19. http://dx.doi.org/10.1039/c9ce01878f.

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Seven 0D → 3D coordination polymers based on dpq/dppz and O-bridged tricarboxylates have been hydrothermally synthesized and structurally directed by metal ions, which show different electrochemical and fluorescence behaviors.
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