Programming cell communications with pH-responsive DNA nanodevices

2021 ◽  
Author(s):  
Junjun Hou ◽  
Shitai Zhu ◽  
Ziwei Zhao ◽  
Jianlei Shen ◽  
Jie Chao ◽  
...  
Keyword(s):  
Cell Surface ◽  
Chain Structure ◽  
Ph Responsive ◽  
Double Chain ◽  
Physiological Conditions

The DNA nanoswitchs on cell surface could respond to the changes of pH under physiological conditions by switching from a three-chain structure to a double-chain structure, thus connecting another set...

Poly[bis[[4-(1H-1,3,7,8-tetraazacyclopenta[l]phenanthren-2-yl)phenol-κ2 N 7,N 8]manganese(II)]-di-μ3-benzene-1,3-dicarboxylato-κ4 O:O′:O′′,O′′′]

2006 ◽  
Vol 62 (7) ◽  
pp. m1686-m1688 ◽  
Author(s):  
Guang-Bo Che
Keyword(s):  
Supramolecular Structure ◽  
Chain Structure ◽  
Title Complex ◽  
Two Dimensional ◽  
Double Chain ◽  
Phenanthroline Ligand

In the title complex, [Mn2(C8H4O4)2(C19H12N4O)2] n , the MnII atom is six-coordinated by two N atoms from the substituted phenanthroline ligand and four O atoms from three different benzene-1,3-dicarboxylate (1,3-BDC) ligands. Adjacent MnII atoms are bridged by the 1,3-BDC ligands to form a double-chain structure which, in turn, is linked to neighboring double chains via π–π contacts to form a two-dimensional supramolecular structure.

scholarly journals 2-(2-Hydroxy-3-methoxyphenyl)-1H-benzimidazol-3-ium perchlorate

2012 ◽  
Vol 68 (6) ◽  
pp. o1920-o1920
Author(s):  
Chuan Chen ◽  
Hong-Xing Li ◽  
Guang-Feng Hou ◽  
Guang-Ming Li
Keyword(s):  
Hydrogen Bonds ◽  
Dihedral Angle ◽  
Chain Structure ◽  
Double Chain ◽  
Intramolecular Hydrogen Bonds ◽  
Ring Systems ◽  
Intramolecular Hydrogen ◽  
Molecular Salt

In the title molecular salt, C14H13N2O2 +·ClO4 −, the ring systems in the cation are almost coplanar [dihedral angle = 5.53 (13)°]. Intramolecular N—H...O and O—H...O hydrogen bonds generate S(6) and S(5) rings, respectively. In the crystal, the two H atoms involved in the intramolecular hydrogen bonds also participate in intermolecular links to acceptor O atoms of the perchlorate anions. A simple intermolecular N—H...O bond also occurs. Together, these form a double-chain structure along [101].

Side-Chain Structure of Cell Surface Polysaccharide, Mannan, Affects Hypocholesterolemic Activity of Yeast

2009 ◽  
Vol 57 (17) ◽  
pp. 8003-8009 ◽  
Author(s):  
Yasuto Yoshida ◽  
Eiichiro Naito ◽  
Harumi Mizukoshi ◽  
Yoko Watanabe ◽  
Kazumasa Kimura ◽  
...  
Keyword(s):  
Cell Surface ◽  
Chain Structure ◽  
Side Chain ◽  
Surface Polysaccharide

A copper(II) chain compound with hydrogenphosphate bridges organized in a double-chain structure. Synthesis, structure and magnetic properties of [Cu(1,10-phenanthroline)(μ-HPO4)(H2O)2]n

2005 ◽  
Vol 8 (4) ◽  
pp. 335-338 ◽  
Author(s):  
Sujittra Youngme ◽  
Pongthipun Phuengphai ◽  
Chaveng Pakawatchai ◽  
Gerard A. van Albada ◽  
Stefania Tanase ◽  
...  
Keyword(s):  
Magnetic Properties ◽  
Chain Structure ◽  
Double Chain ◽  
Structure Synthesis ◽  
Chain Compound

Ecto-Phosphatase Activities on the Cell Surface of the Amastigote Forms of Trypanosoma cruzi

1999 ◽  
Vol 54 (11) ◽  
pp. 977-984 ◽  
Author(s):  
José Roberto Meyer-Fernandes ◽  
Mario Alberto da Silva-Neto ◽  
Mirna dos Santos Soares ◽  
Eloise Fernandes ◽  
Anibal Eugênio Vercesi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Surface ◽  
Trypanosoma Cruzi ◽  
Phosphatase Activity ◽  
Sodium Fluoride ◽  
Competitive Inhibitor ◽  
Physiological Conditions ◽  
Basal Activity ◽  
Activity Difference ◽  
Pnpp Hydrolysis

Abstract Live Trypanosoma cruzi amastigotes hydrolyzed p-nitrophenylphosphate (PNPP), phos-pho-amino-acids and 32P-casein under physiologically appropriate conditions. PNPP was hy­drolysed at a rate of 80 nmol ·mg -1 ·h -1 in the presence of 5 mм MgCl2, pH 7.2 at 30 °C. In the absence of Mg2+ the activity was reduced 40% and we call this basal activity. At saturating concentration of PNPP, half-maximal PNPP hydrolysis was obtained with 0.22 mм MgCl2· Ca2+ had no effect on the basal activity, could not substitute Mg2+ as an activator and in contrast inhibited the PNPP hydrolysis stimulated by Mg2+ (I50 = 0.43 mм ) . In the absence of Mg2+ (basal activity) the stimulating half concentration (S0. 5) for PNPP was 1.57 mм , while at saturating MgCl2 concentrations the corresponding S0.5 for PNPP for Mg2+-stimulated phosphatase activity (difference between total minus basal phosphatase activity) was 0.99 mм . The Mg-dependent PNPP hydrolysis was strongly inhibited by sodium fluoride (NaF), vanadate and Zn2+ but not by tartrate and levamizole. The Mg-independent basal phosphatase activity was insensitive to tartrate, levamizole as well NaF and less inhibited by vanadate and Zn2+. Intact amastigotes were also able to hydrolyse phosphoserine, phos-phothreonine and phosphotyrosine but only the phosphotyrosine hydrolysis was stimulated by MgCl2 and inhibited by CaCl2 and phosphotyrosine was a competitive inhibitor of the PNPP hydrolysis stimulated by Mg2+. The cells were also able to hydrolyse 32P-casein phosphorylated on serine and threonine residues but only in the presence of MgCl2. These results indicate that in the amastigote form of T. cruzi there are at least two ectophosphatase activities, one of which is Mg2+ dependent and can dephosphorylate phospho-aminoacids and phosphoproteins under physiological conditions.

Mechanism of Collagen: Glucosyl-transferase and its Relation to Platelet: Collagen Adhesion

1975 ◽  
Author(s):  
D. F. Smith ◽  
D. P. Kosow ◽  
G. A. Jamieson
Keyword(s):  
Steady State ◽  
Cell Surface ◽  
Platelet Function ◽  
Kinetic Data ◽  
Soluble Form ◽  
Physiological Conditions ◽  
Substrate Complex ◽  
Enzymatic Mechanism ◽  
Enzyme Substrate ◽  
Induced Aggregation

Elucidation of the enzymatic mechanism of collagen: glucosyltransferase is essential to an understanding of its role in platelet function. A soluble form of the enzyme has been purified 100-fold and a sensitive new assay system developed. Studies with effectors such as UDP, ADP and ristocetin under steady state conditions have shown that only two of the possible sequential mechanisms are consistent with the kinetic data. Inhibition by UDP and ADP is competitive with UDPG but non-competitive with galactosylhydroxylysine. They would not, therefore, be expected to inhibit the formation of an enzyme-substrate complex with collagen. Under physiological conditions, their presence would be expected to increase the affinity of the cell surface enzyme for its acceptor on collagen in the case of the ordered mechanism, or not to affect it in the case of the random mechanism. These data are consistent with the potentiation of collagen-induced aggregation by ADP, and the lack of effect of UDP on the adherence of platelets to collagen.(Supported, in part, by USPHS.)

Double-Chain Structure of (pipzH2) [MnF2(HPO4)(H2O)] (H2PO4).

ChemInform ◽  
2004 ◽  
Vol 35 (45) ◽  
Author(s):  
Ronald Stief ◽  
Werner Massa
Keyword(s):  
Chain Structure ◽  
Double Chain
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