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Journal articles on the topic 'Sulfate recognition'

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Published: 4 June 2021
Last updated: 9 February 2022

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1

Kanyo, Z. F., and D. W. Christianson. "Biological recognition of phosphate and sulfate." Journal of Biological Chemistry 266, no. 7 (March 1991): 4264–68. http://dx.doi.org/10.1016/s0021-9258(20)64316-2.

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2

Ravikumar, I., and Pradyut Ghosh. "Recognition and separation of sulfate anions." Chemical Society Reviews 41, no. 8 (2012): 3077. http://dx.doi.org/10.1039/c2cs15293b.

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3

Carruthers, Vern B., Sebastian Håkansson, Olivia K. Giddings, and L. David Sibley. "Toxoplasma gondii Uses Sulfated Proteoglycans for Substrate and Host Cell Attachment." Infection and Immunity 68, no. 7 (July 1, 2000): 4005–11. http://dx.doi.org/10.1128/iai.68.7.4005-4011.2000.

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ABSTRACT Toxoplasma gondii is an obligate intracellular parasite that actively invades a wide variety of vertebrate cells, although the basis of this pervasive cell recognition is not understood. We demonstrate here that binding to the substratum and to host cells is partially mediated by interaction with sulfated glycosaminoglycans (GAGs). Addition of excess soluble GAGs blocked parasite attachment to serum-coated glass, thereby preventing gliding motility of extracellular parasites. Similarly, excess soluble GAGs decreased the attachment of parasites to human host cells from a variety of lineages, including monocytic, fibroblast, endothelial, epithelial, and macrophage cells. The inhibition of parasite attachment by GAGs was observed with heparin and heparan sulfate and also with chondroitin sulfates, indicating that the ligands for attachment are capable of recognizing a broad range of GAGs. The importance of sulfated proteoglycan recognition was further supported by the demonstration that GAG-deficient mutant host cells, and wild-type cells treated enzymatically to remove GAGs, were partially resistant to parasite invasion. Collectively, these studies reveal that sulfated proteoglycans are one determinant used for substrate and cell recognition by Toxoplasma. The widespread distribution of these receptors may contribute to the broad host and tissue ranges of this highly successful intracellular parasite.
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4

Baydemir, Gözde. "Molecularly imprinted cryogels for chondroitin sulfate recognition." Artificial Cells, Nanomedicine, and Biotechnology 44, no. 2 (October 29, 2014): 610–17. http://dx.doi.org/10.3109/21691401.2014.975236.

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5

Mateus, Pedro, Rita Delgado, Vânia André, and M. Teresa Duarte. "Sulfate recognition by a hexaaza cryptand receptor." Organic & Biomolecular Chemistry 13, no. 3 (2015): 834–42. http://dx.doi.org/10.1039/c4ob02027h.

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6

Shishkanova, Tatiana V, David Sykora, Hana Vinšová, Vladimír Král, Iulia Mihai, and Natalia P Gospodinova. "A Novel Way to Improve Sulfate Recognition." Electroanalysis 21, no. 17-18 (September 2009): 2010–13. http://dx.doi.org/10.1002/elan.200904632.

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7

OLIVEIRA, F. O. R., C. R. ALVES, F. SOUZA-SILVA, C. M. CALVET, L. M. C. CÔRTES, M. S. GONZALEZ, L. TOMA, R. I. BOUÇAS, H. B. NADER, and M. C. S. PEREIRA. "Trypanosoma cruzi heparin-binding proteins mediate the adherence of epimastigotes to the midgut epithelial cells of Rhodnius prolixus." Parasitology 139, no. 6 (February 7, 2012): 735–43. http://dx.doi.org/10.1017/s0031182011002344.

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SUMMARYHeparin-binding proteins (HBPs) have been demonstrated in both infective forms of Trypanosoma cruzi and are involved in the recognition and invasion of mammalian cells. In this study, we evaluated the potential biological function of these proteins during the parasite-vector interaction. HBPs, with molecular masses of 65·8 kDa and 59 kDa, were isolated from epimastigotes by heparin affinity chromatography and identified by biotin-conjugated sulfated glycosaminoglycans (GAGs). Surface plasmon resonance biosensor analysis demonstrated stable receptor-ligand binding based on the association and dissociation values. Pre-incubation of epimastigotes with GAGs led to an inhibition of parasite binding to immobilized heparin. Competition assays were performed to evaluate the role of the HBP-GAG interaction in the recognition and adhesion of epimastigotes to midgut epithelial cells of Rhodnius prolixus. Epithelial cells pre-incubated with HBPs yielded a 3·8-fold inhibition in the adhesion of epimastigotes. The pre-treatment of epimastigotes with heparin, heparan sulfate and chondroitin sulfate significantly inhibited parasite adhesion to midgut epithelial cells, which was confirmed by scanning electron microscopy. We provide evidence that heparin-binding proteins are found on the surface of T. cruzi epimastigotes and demonstrate their key role in the recognition of sulfated GAGs on the surface of midgut epithelial cells of the insect vector.
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8

Lee, Haeri, Dongwon Kim, Hyejin Oh, and Ok-Sang Jung. "Molecular balloon, Pd6L8 cages: recognition of alkyl sulfate surfactants." Chemical Communications 56, no. 19 (2020): 2841–44. http://dx.doi.org/10.1039/c9cc09742b.

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Significant structural contraction and expansion of flexible Pd6L8 cages by encapsulation of alkyl sulfate were demonstrated. The contact angles on the fine-ground microcrystal layers shift according to the chain length of the alkyl sulfate.
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9

Ravikumar, I., and Pradyut Ghosh. "ChemInform Abstract: Recognition and Separation of Sulfate Anions." ChemInform 43, no. 29 (June 21, 2012): no. http://dx.doi.org/10.1002/chin.201229279.

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10

Liu, Yang, Arthur J. Chirino, Ziva Misulovin, Christine Leteux, Ten Feizi, Michel C. Nussenzweig, and Pamela J. Bjorkman. "Crystal Structure of the Cysteine-Rich Domain of Mannose Receptor Complexed with a Sulfated Carbohydrate Ligand." Journal of Experimental Medicine 191, no. 7 (March 27, 2000): 1105–16. http://dx.doi.org/10.1084/jem.191.7.1105.

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The macrophage and epithelial cell mannose receptor (MR) binds carbohydrates on foreign and host molecules. Two portions of MR recognize carbohydrates: tandemly arranged C-type lectin domains facilitate carbohydrate-dependent macrophage uptake of infectious organisms, and the NH2-terminal cysteine-rich domain (Cys-MR) binds to sulfated glycoproteins including pituitary hormones. To elucidate the mechanism of sulfated carbohydrate recognition, we determined crystal structures of Cys-MR alone and complexed with 4-sulfated-N-acetylgalactosamine at 1.7 and 2.2 Å resolution, respectively. Cys-MR folds into an approximately three-fold symmetric β-trefoil shape resembling fibroblast growth factor. The sulfate portions of 4-sulfated-N-acetylgalactosamine and an unidentified ligand found in the native crystals bind in a neutral pocket in the third lobe. We use the structures to rationalize the carbohydrate binding specificities of Cys-MR and compare the recognition properties of Cys-MR with other β-trefoil proteins.
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11

Parveen, Nikhat, Douglas Robbins, and John M. Leong. "Strain Variation in Glycosaminoglycan Recognition Influences Cell-Type-Specific Binding by Lyme Disease Spirochetes." Infection and Immunity 67, no. 4 (April 1, 1999): 1743–49. http://dx.doi.org/10.1128/iai.67.4.1743-1749.1999.

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ABSTRACT Lyme disease, a chronic multisystemic disorder that can affect the skin, heart, joints, and nervous system is caused by Borrelia burgdorferi sensu lato. Lyme disease spirochetes were previously shown to bind glycosaminoglycans (GAGs). In the current study, the GAG-binding properties of eight Lyme disease strains were determined. Binding by two high-passage HB19 derivatives to Vero cells could not be inhibited by enzymatic removal of GAGs or by the addition of exogenous GAG. The other six strains, which included a different high-passage HB19 derivative (HB19 clone 1), were shown to recognize both heparan sulfate and dermatan sulfate in cell-binding assays, but the relative efficiency of binding to these two GAGs varied among the strains. Strains N40, CA20-2A, and PBi bound predominantly to heparan sulfate, PBo bound both heparan sulfate and dermatan sulfate roughly equally, and VS461 and HB19 clone 1 recognized primarily dermatan sulfate. Cell binding by strain HB19 clone 1 was inhibited better by exogenous dermatan sulfate than by heparin, whereas heparin was the better inhibitor of binding by strain N40. The GAG-binding preference of a Lyme disease strain was reflected in its cell-type-specific binding. Strains that recognized predominantly heparan sulfate bound efficiently to both C6 glioma cells and EA-Hy926 cells, whereas strains that recognized predominantly dermatan sulfate bound well only to the glial cells. The effect of lyase treatment of these cells on bacterial binding was consistent with the model that cell-type-specific binding was a reflection of the GAG-binding preference. We conclude that the GAG-binding preference varies with the strain of Lyme disease spirochete and that this variation influences cell-type-specific binding in vitro.
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12

Darnaudéry, Muriel, Muriel Koehl, Pier-Vincenzo Piazza, Michel Le Moal, and Willy Mayo. "Pregnenolone sulfate increases hippocampal acetylcholine release and spatial recognition." Brain Research 852, no. 1 (January 2000): 173–79. http://dx.doi.org/10.1016/s0006-8993(99)01964-2.

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13

Ideo, Hiroko, Akira Seko, and Katsuko Yamashita. "Recognition Mechanism of Galectin-4 for Cholesterol 3-Sulfate." Journal of Biological Chemistry 282, no. 29 (June 1, 2007): 21081–89. http://dx.doi.org/10.1074/jbc.m703770200.

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14

Tomasini, BR, and DF Mosher. "Conformational states of vitronectin: preferential expression of an antigenic epitope when vitronectin is covalently and noncovalently complexed with thrombin-antithrombin III or treated with urea." Blood 72, no. 3 (September 1, 1988): 903–12. http://dx.doi.org/10.1182/blood.v72.3.903.903.

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Abstract A difference in recognition of the adhesive glycoprotein vitronectin (also called S-protein, serum spreading factor, and epibolin) by monoclonal antibody 8E6 (Hayman EG, et al, Proc Natl Acad Sci USA 80:4003, 1983) was investigated using a competitive enzyme- immunosorbent assay and immunoaffinity chromatography. Recognition of vitronectin in serum was approximately 50-fold greater than recognition of vitronectin in plasma. Recognition of vitronectin incubated with heparin, thrombin-antithrombin III complex, or heparin and thrombin- antithrombin III complex together was 2.5-, 7-, or 32-fold greater, respectively, than recognition of vitronectin alone. Thrombin or antithrombin III by itself did not induce the antigenic change. Factor Xa-antithrombin III was less effective than thrombin-antithrombin III in induction of the change. Dextran sulfate and fucoidan were more potent than heparin in induction of the antigenic change, whereas dermatan sulfate, hyaluronic acid, heparan sulfate, chondroitin sulfate, or keratan sulfate were less effective. Immunoblotting analysis of serum and of vitronectin incubated with thrombin and antithrombin III demonstrated the presence of complexes composed of vitronectin and thrombin-antithrombin III that could only be dissociated with reducing agent. N-ethylmaleimide completely blocked the formation of the presumably disulfide-bonded complexes and partially blocked the antigenic change. Both non-disulfide-bonded and disulfide-bonded vitronectin bound to antibody-Sepharose from a mixture of vitronectin and thrombin-antithrombin III. Treatment of vitronectin with 8 mol/L urea resulted in enhanced recognition by the monoclonal antibody. Thus, the 8E6 antibody reacts with an epitope that is preferentially expressed by noncovalently and covalently linked vitronectin/thrombin-antithrombin III complexes and by urea-treated vitronectin. The change in vitronectin induced by thrombin-antithrombin III, therefore, is a physiological correlate of urea treatment and of adsorption of vitronectin onto tissue culture plastic (as is done in cell adhesion assays). The change may be important for expression of vitronectin activity.
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15

Tomasini, BR, and DF Mosher. "Conformational states of vitronectin: preferential expression of an antigenic epitope when vitronectin is covalently and noncovalently complexed with thrombin-antithrombin III or treated with urea." Blood 72, no. 3 (September 1, 1988): 903–12. http://dx.doi.org/10.1182/blood.v72.3.903.bloodjournal723903.

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A difference in recognition of the adhesive glycoprotein vitronectin (also called S-protein, serum spreading factor, and epibolin) by monoclonal antibody 8E6 (Hayman EG, et al, Proc Natl Acad Sci USA 80:4003, 1983) was investigated using a competitive enzyme- immunosorbent assay and immunoaffinity chromatography. Recognition of vitronectin in serum was approximately 50-fold greater than recognition of vitronectin in plasma. Recognition of vitronectin incubated with heparin, thrombin-antithrombin III complex, or heparin and thrombin- antithrombin III complex together was 2.5-, 7-, or 32-fold greater, respectively, than recognition of vitronectin alone. Thrombin or antithrombin III by itself did not induce the antigenic change. Factor Xa-antithrombin III was less effective than thrombin-antithrombin III in induction of the change. Dextran sulfate and fucoidan were more potent than heparin in induction of the antigenic change, whereas dermatan sulfate, hyaluronic acid, heparan sulfate, chondroitin sulfate, or keratan sulfate were less effective. Immunoblotting analysis of serum and of vitronectin incubated with thrombin and antithrombin III demonstrated the presence of complexes composed of vitronectin and thrombin-antithrombin III that could only be dissociated with reducing agent. N-ethylmaleimide completely blocked the formation of the presumably disulfide-bonded complexes and partially blocked the antigenic change. Both non-disulfide-bonded and disulfide-bonded vitronectin bound to antibody-Sepharose from a mixture of vitronectin and thrombin-antithrombin III. Treatment of vitronectin with 8 mol/L urea resulted in enhanced recognition by the monoclonal antibody. Thus, the 8E6 antibody reacts with an epitope that is preferentially expressed by noncovalently and covalently linked vitronectin/thrombin-antithrombin III complexes and by urea-treated vitronectin. The change in vitronectin induced by thrombin-antithrombin III, therefore, is a physiological correlate of urea treatment and of adsorption of vitronectin onto tissue culture plastic (as is done in cell adhesion assays). The change may be important for expression of vitronectin activity.
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16

Leong, John M., Douglas Robbins, Louis Rosenfeld, Biswajit Lahiri, and Nikhat Parveen. "Structural Requirements for Glycosaminoglycan Recognition by the Lyme Disease Spirochete, Borrelia burgdorferi." Infection and Immunity 66, no. 12 (December 1, 1998): 6045–48. http://dx.doi.org/10.1128/iai.66.12.6045-6048.1998.

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ABSTRACT Borrelia burgdorferi, the Lyme disease agent, binds glycosaminoglycans (GAGs) such as heparin, heparan sulfate, and dermatan sulfate. Heparin or heparan sulfate fractions separated by size or charge were tested for their ability to inhibit attachment ofB. burgdorferi to Vero cells. GAG chains of increasing length and/or charge showed increasing inhibitory potency, and detectable heparin inhibition of bacterial binding required a minimum of 16 residues. The ability of a given heparin fraction to inhibit binding to Vero cells was strongly predictive of its ability to inhibit hemagglutination, suggesting that hemagglutination reflects the capacity of B. burgdorferi to bind to GAGs.
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17

Morales-Álvarez, Edwin D., Claudia M. Rivera-Hoyos, Patricia Landázuri, Raúl A. Poutou-Piñales, and Aura M. Pedroza-Rodríguez. "Bioinformatic Analysis of the Human Recombinant Iduronate 2-Sulfate Sulfatase." Open Microbiology Journal 10, no. 1 (May 31, 2016): 124–32. http://dx.doi.org/10.2174/1874285801610010124.

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Mucopolysaccharidosis type II is a human recessive disease linked to the X chromosome caused by deficiency of lysosomal enzyme Iduronate 2-Sulfate Sulfatase (IDS), which leads to accumulation of glycosaminoglycans in tissues and organs. The human enzyme has been expressed inEscherichia coliandPichia pastorisin attempt to develop more successful expression systems that allow the production of recombinant IDS for Enzyme Replacement Therapy (ERT). However, the preservation of native signal peptide in the sequence has caused conflicts in processing and recognition in the past, which led to problems in expression and enzyme activity. With the main object being the improvement of the expression system, we eliminate the native signal peptide of human recombinant IDS. The resulting sequence showed two modified codons, thus, our study aimed to analyze computationally the nucleotide sequence of theIDSnhwithout signal peptide in order to determine the 3D structure and other biochemical properties to compare them with the native human IDS (IDSnh). Results showed that there are no significant differences between both molecules in spite of the two-codon modifications detected in the recombinant DNA sequence.
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18

Clark, Simon J., Paul N. Bishop, and Anthony J. Day. "Complement factor H and age-related macular degeneration: the role of glycosaminoglycan recognition in disease pathology." Biochemical Society Transactions 38, no. 5 (September 24, 2010): 1342–48. http://dx.doi.org/10.1042/bst0381342.

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AMD (age-related macular degeneration) is the major cause of blindness in the western world, associated with the formation of extracellular deposits called drusen in the macula, i.e. the central region of the retina. These drusen contain cellular debris and proteins, including components of the complement system such as the regulator CFH (complement factor H); dysregulation of complement is thought to play a major role in the development of AMD. CFH acts through its capacity to recognize polyanionic structures [e.g. sulfated GAGs (glycosaminoglycans)] found on host tissues, and thereby inactivates any C3b that becomes deposited. Importantly, a common polymorphism in CFH (Y402H) has been strongly associated with an increased risk of AMD. This polymorphism, which causes a tyrosine to histidine coding change, has been shown to alter the binding of CFH to sulfated GAGs, as well as to other ligands including C-reactive protein, necrotic cells and bacterial coat proteins. Of these, the change in the GAG-recognition properties of CFH is likely to be of most significance to AMD. Recent research has revealed that the disease-associated 402H allotype interacts less well (compared with 402Y) with binding sites within the macula (e.g. Bruch's membrane), where the GAGs heparan sulfate and dermatan sulfate play a major role in mediating the interaction with CFH. Reduced binding of the 402H allotype could result in impaired regulation of complement leading to chronic local inflammation that may contribute to the accumulation of drusen and thus the initiation, development and progression of AMD.
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19

Berrocal, Maria J., Aurelio Cruz, Ibrahim H. A. Badr, and Leonidas G. Bachas. "Tripodal Ionophore with Sulfate Recognition Properties for Anion-Selective Electrodes." Analytical Chemistry 72, no. 21 (November 2000): 5295–99. http://dx.doi.org/10.1021/ac000241p.

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20

Jin, Can, Man Zhang, Lin Wu, Yangfan Guan, Yi Pan, Juli Jiang, Chen Lin, and Leyong Wang. "Squaramide-based tripodal receptors for selective recognition of sulfate anion." Chemical Communications 49, no. 20 (2013): 2025. http://dx.doi.org/10.1039/c3cc00196b.

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21

Orenha, Renato Pereira, Claudia Haber Cintra, Letícia Bermudes Peixoto, Éder Henrique da Silva, Giovanni Finoto Caramori, Alexandre Osmar Ortolan, Maurício Jeomar Piotrowski, and Renato Luis Tame Parreira. "The anionic recognition mechanism based on polyol and boronic acid receptors." New Journal of Chemistry 44, no. 14 (2020): 5564–71. http://dx.doi.org/10.1039/c9nj06200a.

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22

Ke, Ya-Ting, Wei-Tzu Chou, Yi-Fen Chiang, Chang-Chih Hsieh, and Yih-Chern Horng. "Efficient and selective separation of aqueous sulfate through recognition and precipitation." New Journal of Chemistry 41, no. 6 (2017): 2249–54. http://dx.doi.org/10.1039/c6nj03710k.

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23

Bąk, Krzysztof M., Krystyna Masłowska, and Michał J. Chmielewski. "Selective turn-on fluorescence sensing of sulfate in aqueous–organic mixtures by an uncharged bis(diamidocarbazole) receptor." Organic & Biomolecular Chemistry 15, no. 28 (2017): 5968–75. http://dx.doi.org/10.1039/c7ob01358b.

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24

Bobot, Mickaël, Laurent Thomas, Anaïs Moyon, Samantha Fernandez, Nathalie McKay, Laure Balasse, Philippe Garrigue, et al. "Uremic Toxic Blood-Brain Barrier Disruption Mediated by AhR Activation Leads to Cognitive Impairment during Experimental Renal Dysfunction." Journal of the American Society of Nephrology 31, no. 7 (June 11, 2020): 1509–21. http://dx.doi.org/10.1681/asn.2019070728.

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BackgroundUremic toxicity may play a role in the elevated risk of developing cognitive impairment found among patients with CKD. Some uremic toxins, like indoxyl sulfate, are agonists of the transcription factor aryl hydrocarbon receptor (AhR), which is widely expressed in the central nervous system and which we previously identified as the receptor of indoxyl sulfate in endothelial cells.MethodsTo characterize involvement of uremic toxins in cerebral and neurobehavioral abnormalities in three rat models of CKD, we induced CKD in rats by an adenine-rich diet or by 5/6 nephrectomy; we also used AhR−/− knockout mice overloaded with indoxyl sulfate in drinking water. We assessed neurologic deficits by neurobehavioral tests and blood-brain barrier disruption by SPECT/CT imaging after injection of 99mTc-DTPA, an imaging marker of blood-brain barrier permeability.ResultsIn CKD rats, we found cognitive impairment in the novel object recognition test, the object location task, and social memory tests and an increase of blood-brain barrier permeability associated with renal dysfunction. We found a significant correlation between 99mTc-DTPA content in brain and both the discrimination index in the novel object recognition test and indoxyl sulfate concentrations in serum. When we added indoxyl sulfate to the drinking water of rats fed an adenine-rich diet, we found an increase in indoxyl sulfate concentrations in serum associated with a stronger impairment in cognition and a higher permeability of the blood-brain barrier. In addition, non-CKD AhR−/− knockout mice were protected against indoxyl sulfate–induced blood-brain barrier disruption and cognitive impairment.ConclusionsAhR activation by indoxyl sulfate, a uremic toxin, leads to blood-brain barrier disruption associated with cognitive impairment in animal models of CKD.
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Singabraya, Dominique, Laurent Bultel, Fernando Siñeriz, Mouna Mothéré, David Lesur, José Kovensky, and Dulce Papy-Garcia. "Molecular imprinting technology for specific recognition of heparan sulfate like disaccharides." Talanta 99 (September 2012): 833–39. http://dx.doi.org/10.1016/j.talanta.2012.07.037.

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26

Mothéré, Mouna, Dominique Singabraya, Pierre-Alexandre Driguez, Fernando Siñeriz, and Dulce Papy-Garcia. "Poly(ethylene glycol acrylate)-functionalized hydrogels for heparan sulfate oligosaccharide recognition." Journal of Molecular Recognition 30, no. 3 (October 28, 2016): e2584. http://dx.doi.org/10.1002/jmr.2584.

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Cao, Li, Runsheng Jiang, Yulan Zhu, Xinlong Wang, Yongjun Li, and Yuliang Li. "Synthesis of 1,2,3-Triazole-4-carboxamide-Containing Foldamers for Sulfate Recognition." European Journal of Organic Chemistry 2014, no. 13 (February 27, 2014): 2687–93. http://dx.doi.org/10.1002/ejoc.201301838.

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28

Custelcean, Radu, Priscilla Remy, Peter V Bonnesen, De-en Jiang, and Bruce A Moyer. "Sulfate Recognition by Persistent Crystalline Capsules with Rigidified Hydrogen-Bonding Cavities." Angewandte Chemie 120, no. 10 (February 22, 2008): 1892–96. http://dx.doi.org/10.1002/ange.200704937.

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Custelcean, Radu, Priscilla Remy, Peter V Bonnesen, De-en Jiang, and Bruce A Moyer. "Sulfate Recognition by Persistent Crystalline Capsules with Rigidified Hydrogen-Bonding Cavities." Angewandte Chemie International Edition 47, no. 10 (February 22, 2008): 1866–70. http://dx.doi.org/10.1002/anie.200704937.

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30

Wei, TaiBao, Jun Wang, and YouMing Zhang. "The hydrogen sulfate recognition properties of azo-salicylaldehyde schiff base receptors." Science in China Series B: Chemistry 51, no. 11 (October 24, 2008): 1051–56. http://dx.doi.org/10.1007/s11426-008-0113-5.

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31

Gesteira, Tarsis Ferreira, Tainah Dorina Marforio, Jonathan Wolf Mueller, Matteo Calvaresi, and Vivien Jane Coulson-Thomas. "Structural Determinants of Substrate Recognition and Catalysis by Heparan Sulfate Sulfotransferases." ACS Catalysis 11, no. 17 (August 18, 2021): 10974–87. http://dx.doi.org/10.1021/acscatal.1c03088.

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32

Ramamoorthy, S., H. Sass, H. Langner, P. Schumann, R. M. Kroppenstedt, S. Spring, J. Overmann, and R. F. Rosenzweig. "Desulfosporosinus lacus sp. nov., a sulfate-reducing bacterium isolated from pristine freshwater lake sediments." International Journal of Systematic and Evolutionary Microbiology 56, no. 12 (December 1, 2006): 2729–36. http://dx.doi.org/10.1099/ijs.0.63610-0.

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A novel sulfate-reducing bacterium was isolated from pristine sediments of Lake Stechlin, Germany. This strain, STP12T, was found to contain predominantly c-type cytochromes and to reduce sulfate, sulfite and thiosulfate using lactate as an electron donor. Although STP12T could not utilize elemental sulfur as an electron acceptor, it could support growth by dissimilatory Fe(III) reduction. In a comparison of 16S rRNA gene sequences, STP12T was 96.7 % similar to Desulfosporosinus auripigmenti DSM 13351T, 96.5 % similar to Desulfosporosinus meridiei DSM 13257T and 96.4 % similar to Desulfosporosinus orientis DSM 765T. DNA–DNA hybridization experiments revealed that strain STP12T shows only 32 % reassociation with the type strain of the type species of the genus, D. orientis DSM 765T. These data, considered in conjunction with strain-specific differences in heavy metal tolerance, cell-wall chemotaxonomy and riboprint patterns, support recognition of strain STP12T (=DSM 15449T=JCM 12239T) as the type strain of a distinct and novel species within the genus Desulfosporosinus, Desulfosporosinus lacus sp. nov.
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33

Diamond, M. S., R. Alon, C. A. Parkos, M. T. Quinn, and T. A. Springer. "Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD1)." Journal of Cell Biology 130, no. 6 (September 15, 1995): 1473–82. http://dx.doi.org/10.1083/jcb.130.6.1473.

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Previous studies have demonstrated that the leukocyte integrin Mac-1 adheres to several cell surface and soluble ligands including intercellular adhesion molecule-1, fibrinogen, iC3b, and factor X. However, experiments with Mac-1-expressing transfectants, purified Mac-1, and mAbs to Mac-1 indicate the existence of additional ligands. In this paper, we demonstrate a direct interaction between Mac-1 and heparan sulfate glycans. Heparin affinity resins immunoprecipitate Mac-1, and neutrophils and transfectant cells that express Mac-1 bind to heparin and heparan sulfate, but not to other sulfated glycosaminoglycans. Inhibition studies with mAbs and chemically modified forms of heparin suggest the I domain as a recognition site on Mac-1 for heparin, and suggest that either N- or O-sulfation is sufficient for heparin to bind efficiently to Mac-1. Under conditions of continuous flow in which heparins and E-selectin are cosubstrates, neutrophils tether to E-selectin and form firm adhesions through a Mac-1-heparin interaction.
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34

Sakuragi, Miho, Ryoko Suzuki, Kazuya I. P. J. Hidari, Takashi Yamanaka, and Hirofumi Nakano. "Synthesis of p-methoxyphenyl sulfated β-GalNAc derivatives with inhibitory activity against Japanese encephalitis virus." Pure and Applied Chemistry 89, no. 9 (August 28, 2017): 1251–66. http://dx.doi.org/10.1515/pac-2016-0921.

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AbstractThe N-acetylgalactosamine (GalNAc) residue is one of the units of chondroitin sulfate E (CS-E) which has been reported to have inhibitory activity against Japanese encephalitis virus (JEV). Herein, we describe the synthesis of a series of p-methoxyphenyl β-GalNAc derivatives with a sulfate group at 3-, 4-, and/or 6-positions using an efficient route through a common synthetic intermediate. By measuring the inhibition activity of these compounds that bear different numbers and positions of sulfate groups, the effect of position specificity for interaction with the virus was determined. From these results, GalNAc6S and GalNAc4S6S derivatives inhibited JEV infections well; we suggest the 6-O-sulfate group is necessary for selective recognition by the virus.
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35

Prats-Ejarque, Guillem, Javier Arranz-Trullén, Jose A. Blanco, David Pulido, M. Victòria Nogués, Mohammed Moussaoui, and Ester Boix. "The first crystal structure of human RNase 6 reveals a novel substrate-binding and cleavage site arrangement." Biochemical Journal 473, no. 11 (May 27, 2016): 1523–36. http://dx.doi.org/10.1042/bcj20160245.

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We describe the first human RNase 6 crystal structure in complex with sulfate anions. Kinetic analysis, site-directed mutagenesis and molecular dynamics simulations identified novel substrate recognition and cleavage sites.
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36

Beer, Paul D., James Cadman, José M. Lloris, Ramón Martínez-Máñez, Miguel E. Padilla, Teresa Pardo, David K. Smith, and Juan Soto. "Selective electrochemical recognition of sulfate over phosphate and phosphate over sulfate using polyaza ferrocene macrocyclic receptors in aqueous solution." Journal of the Chemical Society, Dalton Transactions, no. 2 (1999): 127–34. http://dx.doi.org/10.1039/a806944a.

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37

Wander, Rylee, Andrea M. Kaminski, Yongmei Xu, Vijayakanth Pagadala, Juno M. Krahn, Truong Quang Pham, Jian Liu, and Lars C. Pedersen. "Deciphering the substrate recognition mechanisms of the heparan sulfate 3-O-sulfotransferase-3." RSC Chemical Biology 2, no. 4 (2021): 1239–48. http://dx.doi.org/10.1039/d1cb00079a.

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Co-crystallization and biochemical analyses with structurally defined oligosaccharides show the low reactivity of HS 3-OST-3 toward 6-O-sulfated substrates is due to inhibition of enzyme activity by 6-O-sulfated oligosaccharides.
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38

Kaur, Simanpreet, Amanpreet Kaur, and Navneet Kaur. "ZnO nanoparticles decorated with organic anion receptor: Selective recognition of sulfate anion." Materials Letters 100 (June 2013): 19–22. http://dx.doi.org/10.1016/j.matlet.2013.02.100.

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39

Keşan, Gürkan, Burcu Topaloğlu, Emrah Özcan, Hasan Hüseyin Kazan, Esra Tanrıverdi Eçik, Elif Şenkuytu, Ibrahim F. Sengul, Hakan Kandemir, and Bünyemin Çoşut. "Azaindole-BODIPYs: Synthesis, fluorescent recognition of hydrogen sulfate anion and biological evaluation." Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 213 (April 2019): 73–82. http://dx.doi.org/10.1016/j.saa.2019.01.047.

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40

Cormode, David P., Sean S. Murray, Andrew R. Cowley, and Paul D. Beer. "Sulfate selective anion recognition by a novel tetra-imidazolium zinc metalloporphyrin receptor." Dalton Transactions, no. 43 (2006): 5135. http://dx.doi.org/10.1039/b609817g.

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41

Ohtake, Shiori, Koji Kimata, and Osami Habuchi. "Recognition of Sulfation Pattern of Chondroitin Sulfate by Uronosyl 2-O-Sulfotransferase." Journal of Biological Chemistry 280, no. 47 (September 27, 2005): 39115–23. http://dx.doi.org/10.1074/jbc.m508816200.

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42

Tzioumis, Nikki A., Karen K. Y. Yuen, and Katrina A. Jolliffe. "Investigating the effects of structure on sulfate recognition by neutral dipeptide receptors." Supramolecular Chemistry 30, no. 8 (January 29, 2018): 667–73. http://dx.doi.org/10.1080/10610278.2018.1430896.

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43

Lemonnier, Jean-François, Sébastien Floquet, Jérôme Marrot, and Emmanuel Cadot. "Polyoxothiomolybdenum Wheels as Anionic Receptors for Recognition of Sulfate and Sulfonate Anions." European Journal of Inorganic Chemistry 2009, no. 34 (December 2009): 5233–39. http://dx.doi.org/10.1002/ejic.200900613.

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44

Agafontsev, Aleksandr M., Tatiana A. Shumilova, Pavel A. Panchenko, Sharon Janz, Olga A. Fedorova, and Evgeny A. Kataev. "Utilizing a pH-Sensitive Dye in the Selective Fluorescent Recognition of Sulfate." Chemistry - A European Journal 22, no. 42 (September 5, 2016): 15069–74. http://dx.doi.org/10.1002/chem.201602623.

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45

Elmes, Robert B. P., Karen K. Y. Yuen, and Katrina A. Jolliffe. "Sulfate-Selective Recognition by Using Neutral Dipeptide Anion Receptors in Aqueous Solution." Chemistry - A European Journal 20, no. 24 (May 14, 2014): 7373–80. http://dx.doi.org/10.1002/chem.201400292.

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46

Mendy, John S., Marcy L. Pilate, Toyketa Horne, Victor W. Day, and Md Alamgir Hossain. "Encapsulation and selective recognition of sulfate anion in an azamacrocycle in water." Chemical Communications 46, no. 33 (2010): 6084. http://dx.doi.org/10.1039/c0cc01699c.

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47

Bistrup, Annette, Sunil Bhakta, Jin Kyu Lee, Yevgeniy Y. Belov, Michael Dee Gunn, Feng-Rong Zuo, Chiao-Chain Huang, Reiji Kannagi, Steven D. Rosen, and Stefan Hemmerich. "Sulfotransferases of Two Specificities Function in the Reconstitution of High Endothelial Cell Ligands for L-selectin." Journal of Cell Biology 145, no. 4 (May 17, 1999): 899–910. http://dx.doi.org/10.1083/jcb.145.4.899.

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L-selectin, a lectin-like receptor, mediates rolling of lymphocytes on high endothelial venules (HEVs) in secondary lymphoid organs by interacting with HEV ligands. These ligands consist of a complex of sialomucins, candidates for which are glycosylation- dependent cell adhesion molecule 1 (GlyCAM-1), CD34, and podocalyxin. The ligands must be sialylated, fucosylated, and sulfated for optimal recognition by L-selectin. Our previous structural characterization of GlyCAM-1 has demonstrated two sulfation modifications, Gal-6-sulfate and GlcNAc-6-sulfate in the context of sialyl Lewis x. We now report the cloning of a Gal-6-sulfotransferase and a GlcNAc-6-sulfotransferase, which can modify GlyCAM-1 and CD34. The Gal-6-sulfotransferase shows a wide tissue distribution. In contrast, the GlcNAc-6-sulfotransferase is highly restricted to HEVs, as revealed by Northern analysis and in situ hybridization. Expression of either enzyme in Chinese hamster ovary cells, along with CD34 and fucosyltransferase VII, results in ligand activity, as detected by binding of an L-selectin/IgM chimera. When coexpressed, the two sulfotransferases synergize to produce strongly enhanced chimera binding.
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48

André, Claire, and Yves Claude Guillaume. "Development of nano affinity columns for the study of ligand (including SARS-CoV-2 related proteins) binding to heparan sulfate proteoglycans." Analytical Methods 13, no. 27 (2021): 3050–58. http://dx.doi.org/10.1039/d1ay00506e.

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A Heparan Sulfate Proteoglycan (HSPG) nano HPLC capillary column was developed for ligand/HSPG recognition and showed excellent repeatability, a strong resistance to changes in temperature and pH and a negligible number of non-specific sites.
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49

Kamimura, Keisuke, John M. Rhodes, Ryu Ueda, Melissa McNeely, Deepak Shukla, Koji Kimata, Patricia G. Spear, Nicholas W. Shworak, and Hiroshi Nakato. "Regulation of Notch signaling by Drosophila heparan sulfate 3-O sulfotransferase." Journal of Cell Biology 166, no. 7 (September 27, 2004): 1069–79. http://dx.doi.org/10.1083/jcb.200403077.

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Heparan sulfate (HS) regulates the activity of various ligands and is involved in molecular recognition events on the cell surface and in the extracellular matrix. Specific binding of HS to different ligand proteins depends on the sulfation pattern of HS. For example, the interaction between antithrombin and a particular 3-O sulfated HS motif is thought to modulate blood coagulation. However, a recent study of mice defective for this modification suggested that 3-O sulfation plays other biological roles. Here, we show that Drosophila melanogaster HS 3-O sulfotransferase-b (Hs3st-B), which catalyzes HS 3-O sulfation, is a novel component of the Notch pathway. Reduction of Hs3st-B function by transgenic RNA interference compromised Notch signaling, producing neurogenic phenotypes. We also show that levels of Notch protein on the cell surface were markedly decreased by loss of Hs3st-B. These findings suggest that Hs3st-B is involved in Notch signaling by affecting stability or intracellular trafficking of Notch protein.
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50

Rambabu, Darsi, Pooja Pooja, Chullikkattil P. Pradeep, and Abhimanew Dhir. "A cytochrome C encapsulated metal organic framework as a bio-material for sulfate ion recognition." J. Mater. Chem. A 2, no. 23 (2014): 8628–31. http://dx.doi.org/10.1039/c4ta01599a.

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