The Experts below are selected from a list of 276 Experts worldwide ranked by ideXlab platform
Volker Müller - One of the best experts on this subject based on the ideXlab platform.
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sodium ion dependence of inhibition of the na translocating f1f0 atpase from acetobacterium woodii probing the site s involved in ion transport
Biochimica et Biophysica Acta, 1995Co-Authors: Martin Spruth, Jutta Reidlinger, Volker MüllerAbstract:The Na+-translocating F1F0-ATPase of Acetobacterium woodii was stimulated not only by Na+ but also by Li+ and was protected by Na+ or Li+ from inactivation by N,N′-dicyclohexylcarbodiimide (DCCD), diethylstilbestrol (DES) and tributyltin (TBSn) but not N-ethylmaleimide (NEM) or azide. The amount of Na+ required for half-maximal protection from DCCD inhibition corresponded to the apparent Km for Na+ of ATP hydrolysis. The inhibition by the amiloride derivatives hexamethylene-amiloride (HMA), ethylisopropylamiloride (EIPA), N-10-benzyl-amiloride (benzamil) and N-10-phenamil-amiloride (phenamil) could be relieved by Na+ to various degrees. EIPA and HMA effectively protected the ATPase from DCCD inactivation, whereas the protection by benzamil and phenamil was only marginal indicating that the unsubstituted guanidinium group is essential for maximal protection from DCCD inactivation. These results indicate that the amiloride derivatives and Na+ or DCCD compete for a common binding site. Chemical modification of histidine, Arginine, Aspartate or glutamate residues of the F1F0, complex resulted in an inhibition of ATP hydrolysis, indicating an essential function of these residues in the catalytic mechanism but this inhibition could not be relieved by Na+.
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Sodium ion dependence of inhibition of the Na+-translocating F1F0-ATPase from Acetobacterium woodii. Probing the site(s) involved in ion transport
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1995Co-Authors: Martin Spruth, Jutta Reidlinger, Volker MüllerAbstract:The Na+-translocating F1F0-ATPase of Acetobacterium woodii was stimulated not only by Na+ but also by Li+ and was protected by Na+ or Li+ from inactivation by N,N′-dicyclohexylcarbodiimide (DCCD), diethylstilbestrol (DES) and tributyltin (TBSn) but not N-ethylmaleimide (NEM) or azide. The amount of Na+ required for half-maximal protection from DCCD inhibition corresponded to the apparent Km for Na+ of ATP hydrolysis. The inhibition by the amiloride derivatives hexamethylene-amiloride (HMA), ethylisopropylamiloride (EIPA), N-10-benzyl-amiloride (benzamil) and N-10-phenamil-amiloride (phenamil) could be relieved by Na+ to various degrees. EIPA and HMA effectively protected the ATPase from DCCD inactivation, whereas the protection by benzamil and phenamil was only marginal indicating that the unsubstituted guanidinium group is essential for maximal protection from DCCD inactivation. These results indicate that the amiloride derivatives and Na+ or DCCD compete for a common binding site. Chemical modification of histidine, Arginine, Aspartate or glutamate residues of the F1F0, complex resulted in an inhibition of ATP hydrolysis, indicating an essential function of these residues in the catalytic mechanism but this inhibition could not be relieved by Na+.
Hiroshi Okada - One of the best experts on this subject based on the ideXlab platform.
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effects of a supplement combining pycnogenol and l Arginine Aspartate on lower urinary dysfunction compared with saw palmetto extract
Journal of Traditional and Complementary Medicine, 2017Co-Authors: Hiroshi Yagi, Ryo Sato, Kojiro Nishio, Gaku Arai, Shigehiro Soh, Hiroshi OkadaAbstract:Abstract Objectives Lower urinary tract symptoms (LUTS) and sexual dysfunction (SDys) are common problems that affect quality of life (QOL) in elderly men. In addition to prescribed drugs, many over-the-counter medications including supplements are used to treat QOL diseases. Phosphodiesterase inhibitors are reported to be effective for both LUTS and SDys by increasing nitric oxide levels. French maritime pine bark extract Pycnogenol®, which is a potent nitric oxide donor, is reported to be effective for SDys. However, no reports have been published on whether it ameliorates LUTS. Design Open-labeled, randomized study. The effects of two supplements, Nokogiriyashi EX® containing 160 mg saw palmetto (SP) extract per tablet and Edicare® containing 10 mg of Pycnogenol®, 115 mg of l -Arginine and 92 mg of Aspartate (PAA) per tablet on International Prostate Symptom Score (IPSS), IPSS–QOL, Overactive Bladder Symptom Score (OABSS), International Index of Erectile Function 5 (IIEF5), Consultation on Incontinence Questionnaire-Short Form (ICIQ-SF), urinary 8-OHdG and uroflowmetry (UFM) of total 40 men with LUTS and SDys were examined. Results 19 subjects were instructed to take two tablets of SP, on the other 20 were on four tablets of PAA for 16 weeks. IPSS and IPSS–QOL showed statistically significant improvements in both groups. OABSS and IIEF5 were significantly improved in the PAA group. Conversely, ICIQ-SF, 8-OHdG and UFM did not change in either group. Conclusions PAA might be an effective therapeutic alternative for elderly patients with LUTS and SDys.
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Effects of a supplement combining Pycnogenol® and l-Arginine Aspartate on lower urinary dysfunction compared with saw palmetto extract
Journal of traditional and complementary medicine, 2016Co-Authors: Hiroshi Yagi, Ryo Sato, Kojiro Nishio, Gaku Arai, Shigehiro Soh, Hiroshi OkadaAbstract:Lower urinary tract symptoms (LUTS) and sexual dysfunction (SDys) are common problems that affect quality of life (QOL) in elderly men. In addition to prescribed drugs, many over-the-counter medications including supplements are used to treat QOL diseases. Phosphodiesterase inhibitors are reported to be effective for both LUTS and SDys by increasing nitric oxide levels. French maritime pine bark extract Pycnogenol®, which is a potent nitric oxide donor, is reported to be effective for SDys. However, no reports have been published on whether it ameliorates LUTS. Open-labeled, randomized study. The effects of two supplements, Nokogiriyashi EX® containing 160 mg saw palmetto (SP) extract per tablet and Edicare® containing 10 mg of Pycnogenol®, 115 mg of l-Arginine and 92 mg of Aspartate (PAA) per tablet on International Prostate Symptom Score (IPSS), IPSS-QOL, Overactive Bladder Symptom Score (OABSS), International Index of Erectile Function 5 (IIEF5), Consultation on Incontinence Questionnaire-Short Form (ICIQ-SF), urinary 8-OHdG and uroflowmetry (UFM) of total 40 men with LUTS and SDys were examined. 19 subjects were instructed to take two tablets of SP, on the other 20 were on four tablets of PAA for 16 weeks. IPSS and IPSS-QOL showed statistically significant improvements in both groups. OABSS and IIEF5 were significantly improved in the PAA group. Conversely, ICIQ-SF, 8-OHdG and UFM did not change in either group. PAA might be an effective therapeutic alternative for elderly patients with LUTS and SDys.
Martin Spruth - One of the best experts on this subject based on the ideXlab platform.
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sodium ion dependence of inhibition of the na translocating f1f0 atpase from acetobacterium woodii probing the site s involved in ion transport
Biochimica et Biophysica Acta, 1995Co-Authors: Martin Spruth, Jutta Reidlinger, Volker MüllerAbstract:The Na+-translocating F1F0-ATPase of Acetobacterium woodii was stimulated not only by Na+ but also by Li+ and was protected by Na+ or Li+ from inactivation by N,N′-dicyclohexylcarbodiimide (DCCD), diethylstilbestrol (DES) and tributyltin (TBSn) but not N-ethylmaleimide (NEM) or azide. The amount of Na+ required for half-maximal protection from DCCD inhibition corresponded to the apparent Km for Na+ of ATP hydrolysis. The inhibition by the amiloride derivatives hexamethylene-amiloride (HMA), ethylisopropylamiloride (EIPA), N-10-benzyl-amiloride (benzamil) and N-10-phenamil-amiloride (phenamil) could be relieved by Na+ to various degrees. EIPA and HMA effectively protected the ATPase from DCCD inactivation, whereas the protection by benzamil and phenamil was only marginal indicating that the unsubstituted guanidinium group is essential for maximal protection from DCCD inactivation. These results indicate that the amiloride derivatives and Na+ or DCCD compete for a common binding site. Chemical modification of histidine, Arginine, Aspartate or glutamate residues of the F1F0, complex resulted in an inhibition of ATP hydrolysis, indicating an essential function of these residues in the catalytic mechanism but this inhibition could not be relieved by Na+.
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Sodium ion dependence of inhibition of the Na+-translocating F1F0-ATPase from Acetobacterium woodii. Probing the site(s) involved in ion transport
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1995Co-Authors: Martin Spruth, Jutta Reidlinger, Volker MüllerAbstract:The Na+-translocating F1F0-ATPase of Acetobacterium woodii was stimulated not only by Na+ but also by Li+ and was protected by Na+ or Li+ from inactivation by N,N′-dicyclohexylcarbodiimide (DCCD), diethylstilbestrol (DES) and tributyltin (TBSn) but not N-ethylmaleimide (NEM) or azide. The amount of Na+ required for half-maximal protection from DCCD inhibition corresponded to the apparent Km for Na+ of ATP hydrolysis. The inhibition by the amiloride derivatives hexamethylene-amiloride (HMA), ethylisopropylamiloride (EIPA), N-10-benzyl-amiloride (benzamil) and N-10-phenamil-amiloride (phenamil) could be relieved by Na+ to various degrees. EIPA and HMA effectively protected the ATPase from DCCD inactivation, whereas the protection by benzamil and phenamil was only marginal indicating that the unsubstituted guanidinium group is essential for maximal protection from DCCD inactivation. These results indicate that the amiloride derivatives and Na+ or DCCD compete for a common binding site. Chemical modification of histidine, Arginine, Aspartate or glutamate residues of the F1F0, complex resulted in an inhibition of ATP hydrolysis, indicating an essential function of these residues in the catalytic mechanism but this inhibition could not be relieved by Na+.
Pamela C. Ronald - One of the best experts on this subject based on the ideXlab platform.
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Non-Arginine-Aspartate (non-RD) kinases are associated with innate immune receptors that recognize conserved microbial signatures.
Current opinion in plant biology, 2012Co-Authors: Chris Dardick, Benjamin Schwessinger, Pamela C. RonaldAbstract:An important question in the field of plant–pathogen interactions is how the detection of pathogens is converted into an effective immune response. In recent years, substantial insight has been gained into the identities of both the plant receptors and the microbial molecules they recognize. Likewise, many of the downstream signaling proteins and transcriptions factors that activate defense responses have been characterized. However, the early molecular events that comprise ‘recognition’ and how defense signaling specificity is achieved are not as well understood. In this review we discuss the significance of non-Arginine-Aspartate (non-RD) kinases, a subclass of kinases that are often found in association with pattern recognition receptors (PRRs).
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Plant Innate Immunity: Perception of Conserved Microbial Signatures
Annual review of plant biology, 2012Co-Authors: Benjamin Schwessinger, Pamela C. RonaldAbstract:Plants and animals sense conserved microbial signatures through receptors localized to the plasma membrane and cytoplasm. These receptors typically carry or associate with non-Arginine-Aspartate (non-RD) kinases that initiate complex signaling networks cumulating in robust defense responses. In plants, coregulatory receptor kinases have been identified that not only are critical for the innate immune response but also serve an essential function in other regulatory signaling pathways.
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A conserved threonine residue in the juxtamembrane domain of the XA21 pattern recognition receptor is critical for kinase autophosphorylation and xa21-mediated immunity.
The Journal of biological chemistry, 2010Co-Authors: Xuewei Chen, Mawsheng Chern, Patrick E. Canlas, Caiying Jiang, Deling Ruan, Peijian Cao, Pamela C. RonaldAbstract:Despite the key role that pattern recognition receptors (PRRs) play in regulating immunity in plants and animals, the mechanism of activation of the associated non-Arginine-Aspartate (non-RD) kinases is unknown. The rice PRR XA21 recognizes the pathogen-associated molecular pattern, Ax21 (activator of XA21-mediated immunity). Here we show that the XA21 juxtamembrane (JM) domain is required for kinase autophosphorylation. Threonine 705 in the XA21 JM domain is essential for XA21 autophosphorylation in vitro and XA21-mediated innate immunity in vivo. The replacement of Thr(705) by an alanine or glutamic acid abolishes XA21 autophosphorylation and eliminates interactions between XA21 and four XA21-binding proteins in yeast and rice. Although threonine residues analogous to Thr(705) of XA21 are present in the JM domains of most RD and non-RD plant receptor-like kinases, this residue is not required for autophosphorylation of the Arabidopsis RD RLK BRI1 (brassinosteroid insensitive 1). The threonine 705 of XA21 is conserved only in the JM domains of plant RLKs but not in those of fly, human, or mouse suggesting distinct regulatory mechanisms. These results contribute to growing knowledge regarding the mechanism by which non-RD RLKs function in plant.
Juquan Jiang - One of the best experts on this subject based on the ideXlab platform.
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characterization of a functionally unknown Arginine Aspartate Aspartate family protein from halobacillus andaensis and functional analysis of its conserved Arginine Aspartate residues
Frontiers in Microbiology, 2018Co-Authors: Li Shao, Zhenglai Zhang, Fankui Meng, Huiwen Chen, Lin Meng, Heba Abdelmotaal, Jin Chen, Tong Xu, Juquan JiangAbstract:Arginine-Aspartate-Aspartate (RDD) family representing a category of transmembrane proteins containing one highly conserved Arginine and two highly conserved Aspartates has been functionally uncharacterized as yet. Here we present the characterization of a member of this family designated RDD from the moderate halophile Halobacillus andaensis NEAU-ST10-40T and report for the first time that RDD should function as a novel Na+(Li+, K+)/H+ antiporter. It's more interesting whether the highly conserved Arginine/Aspartate residues among the whole family or between RDD and its selected homologs are related to the protein function. Therefore, we analyzed their roles in the cation-transporting activity through site-directed mutagenesis and found that D154, R124, R129 and D158 are indispensable for Na+(Li+, K+)/H+ antiport activity whereas neither R35 nor D42 is involved in Na+(Li+, K+)/H+ antiport activity. As a dual representative of Na+(Li+, K+)/H+ antiporters and RDD family proteins, the characterization of RDD and analysis of its important residues will positively contribute to the knowledge of the cation-transporting mechanisms of this novel antiporter and the roles of highly conserved Arginine/Aspartate residues in the functions of RDD family proteins.
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Characterization of a Functionally Unknown Arginine-Aspartate-Aspartate Family Protein From Halobacillus andaensis and Functional Analysis of Its Conserved Arginine/Aspartate Residues.
Frontiers in microbiology, 2018Co-Authors: Li Shao, Zhenglai Zhang, Fankui Meng, Huiwen Chen, Lin Meng, Jin Chen, Heba Abdel-motaal, Juquan JiangAbstract:Arginine-Aspartate-Aspartate (RDD) family, representing a category of transmembrane proteins containing one highly conserved Arginine and two highly conserved Aspartates, has been functionally uncharacterized as yet. Here we present the characterization of a member of this family designated RDD from the moderate halophile Halobacillus andaensis NEAU-ST10-40T and report for the first time that RDD should function as a novel Na+(Li+, K+)/H+ antiporter. It's more interesting whether the highly conserved Arginine/Aspartate residues among the whole family or between RDD and its selected homologs are related to the protein function. Therefore, we analyzed their roles in the cation-transporting activity through site-directed mutagenesis and found that D154, R124, R129, and D158 are indispensable for Na+(Li+, K+)/H+ antiport activity whereas neither R35 nor D42 is involved in Na+(Li+, K+)/H+ antiport activity. As a dual representative of Na+(Li+, K+)/H+ antiporters and RDD family proteins, the characterization of RDD and the analysis of its important residues will positively contribute to the knowledge of the cation-transporting mechanisms of this novel antiporter and the roles of highly conserved Arginine/Aspartate residues in the functions of RDD family proteins.