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Two phase 3 trials of bapineuzumab in mild-to-moderate Alzheimer's disease.
Salloway S, Sperling R, Fox NC, Blennow K, Klunk W, Raskind M, Sabbagh M, Honig LS, Porsteinsson AP, Ferris S, Reichert M, Ketter N, Nejadnik B, Guenzler V, Miloslavsky M, Wang D, Lu Y, Lull J, Tudor IC, Liu E, Grundman M, Yuen E, Black R, Brashear HR; Bapineuzumab 301 and 302 Clinical Trial Investigators. Salloway S, et al. N Engl J Med. 2014 Jan 23;370(4):322-33. doi: 10.1056/NEJMoa1304839. N Engl J Med. 2014. PMID: 24450891 Free PMC article. Clinical Trial.
BACKGROUND: Bapineuzumab, a humanized anti-amyloid-beta monoclonal antibody, is in clinical development for the treatment of Alzheimer's disease. METHODS: We conducted two double-blind, randomized, placebo-controlled, phase 3 trials involving patients with mild-to-moderate …
BACKGROUND: Bapineuzumab, a humanized anti-amyloid-beta monoclonal antibody, is in clinical development for the treatment of Alzheimer's …
Tunable emission of Li4SrCaSi2O4-yN2y/3:Eu2+ phosphors based on anion substitution induction for WLEDs and optical thermometry.
Yu H, Zhou L, Ye R, Deng D, Xu S. Yu H, et al. Dalton Trans. 2022 May 10;51(18):7333-7342. doi: 10.1039/d2dt00485b. Dalton Trans. 2022. PMID: 35485841
The white LED that utilized blue-orange-emitting Li(4)SrCaSi(2)O(4)N(8/3):Eu(2+) and green-emitting BaSi(2)O(2)N(2):Eu(2+) (500 nm) displayed an outstanding color rendering index (R(a)) of 85.1. Based on the fluorescence intensity ratio (FIR) technique, an optical temperat …
The white LED that utilized blue-orange-emitting Li(4)SrCaSi(2)O(4)N(8/3):Eu(2+) and green-emitting BaSi(2)O(2)N(2):Eu(2+) (500 nm) d …
Kinetics and energetics of the binding between barley alpha-amylase/subtilisin inhibitor and barley alpha-amylase 2 analyzed by surface plasmon resonance and isothermal titration calorimetry.
Nielsen PK, Bønsager BC, Berland CR, Sigurskjold BW, Svensson B. Nielsen PK, et al. Biochemistry. 2003 Feb 18;42(6):1478-87. doi: 10.1021/bi020508+. Biochemistry. 2003. PMID: 12578360
Binding kinetics were in accordance with a 1:1 binding model. At pH 5.5, [Ca(2+)] = 5 mM, and 25 degrees C, the k(on) and k(off) values were 8.3 x 10(+4) M(-1) s(-1) and 26.0 x 10(-4) s(-1), respectively, corresponding to a K(D) of 31 nM. ...Sub …
Binding kinetics were in accordance with a 1:1 binding model. At pH 5.5, [Ca(2+)] = 5 mM, and 25 degrees C, the k(on) and k(of …
Purification and characterization of the beta-trefoil fold protein barley alpha-amylase/subtilisin inhibitor overexpressed in Escherichia coli.
Bønsager BC, Praetorius-Ibba M, Nielsen PK, Svensson B. Bønsager BC, et al. Protein Expr Purif. 2003 Aug;30(2):185-93. doi: 10.1016/s1046-5928(03)00103-7. Protein Expr Purif. 2003. PMID: 12880767
In Pichia pastoris, rBASI was secreted at 0.1 mgl(-1). The recombinant BASI forms and natural seed BASI (sBASI) all had an identical isoelectric point of 7.2 and a mass of 19,879 Da, as determined by mass spectrometry. The fold of rBASI from the different preparatio …
In Pichia pastoris, rBASI was secreted at 0.1 mgl(-1). The recombinant BASI forms and natural seed BASI (sBASI) all had an ide …
Dissecting molecular interactions involved in recognition of target disulfides by the barley thioredoxin system.
Björnberg O, Maeda K, Svensson B, Hägglund P. Björnberg O, et al. Biochemistry. 2012 Dec 11;51(49):9930-9. doi: 10.1021/bi301051b. Epub 2012 Nov 29. Biochemistry. 2012. PMID: 23163229
In the three-dimensional structure of a complex with barley alpha-amylase/subtilisin inhibitor (BASI), two loops in barley thioredoxin h2 (HvTrxh2), containing an invariant cis-proline ((86)EAMP(89)) and a conserved glycine ((104)VGA(106)), surround the active site cystein …
In the three-dimensional structure of a complex with barley alpha-amylase/subtilisin inhibitor (BASI), two loops in barley thioredoxi …
Persistence of Immunity Following 2-Dose Priming with a 10-Valent Pneumococcal Conjugate Vaccine at 6 and 10 Weeks or 6 and 14 Weeks of Age in Nepalese Toddlers.
Gurung M, Bijukchhe SM, Hariri P, Voysey M, Kandasamy R, Thorson S, Maskey P, Pandit R, Shrestha B, Gautam MC, Maharjan M, Lama L, Acharya B, Basi R, K C M, O'Reilly P, Shrestha S, Ansari I, Shah GP, Kelly S, O'Brien KL, Goldblatt D, Kelly DF, Murdoch DR, Pollard AJ, Shrestha S. Gurung M, et al. Pediatr Infect Dis J. 2021 Oct 1;40(10):937-943. doi: 10.1097/INF.0000000000003223. Pediatr Infect Dis J. 2021. PMID: 34292271
Mutational analysis of target enzyme recognition of the beta-trefoil fold barley alpha-amylase/subtilisin inhibitor.
Bønsager BC, Nielsen PK, Abou Hachem M, Fukuda K, Praetorius-Ibba M, Svensson B. Bønsager BC, et al. J Biol Chem. 2005 Apr 15;280(15):14855-64. doi: 10.1074/jbc.M412222200. Epub 2005 Jan 18. J Biol Chem. 2005. PMID: 15657043 Free article.
The barley alpha-amylase/subtilisin inhibitor (BASI) inhibits alpha-amylase 2 (AMY2) with subnanomolar affinity. ...Seven BASI residues along the AMY2-BASI interface and four residues in the putative protease-binding loop on the opposite side of the inhibitor …
The barley alpha-amylase/subtilisin inhibitor (BASI) inhibits alpha-amylase 2 (AMY2) with subnanomolar affinity. ...Seven BASI …
Structural and mutational analyses of the interaction between the barley alpha-amylase/subtilisin inhibitor and the subtilisin savinase reveal a novel mode of inhibition.
Micheelsen PO, Vévodová J, De Maria L, Ostergaard PR, Friis EP, Wilson K, Skjøt M. Micheelsen PO, et al. J Mol Biol. 2008 Jul 18;380(4):681-90. doi: 10.1016/j.jmb.2008.05.034. Epub 2008 May 22. J Mol Biol. 2008. PMID: 18556023
Structural analysis revealed that BASI inhibits Savinase in a novel way, as the interacting loop is shorter than loops previously reported. Mutational analysis showed that Thr88 is crucial for the inhibition, as it stabilises the interacting loop through intramolecular int …
Structural analysis revealed that BASI inhibits Savinase in a novel way, as the interacting loop is shorter than loops previously rep …
Stopped-flow kinetic studies of the reaction of barley alpha-amylase/subtilisin inhibitor and the high pI barley alpha-amylase.
Sidenius U, Olsen K, Svensson B, Christensen U. Sidenius U, et al. FEBS Lett. 1995 Mar 20;361(2-3):250-4. doi: 10.1016/0014-5793(95)00187-e. FEBS Lett. 1995. PMID: 7698332 Free article.
The results are in accordance with a two-step reaction model: [formula: see text] The resulting values of the kinetic parameters were: k2/K1 = (1.0 +/- 0.2) x 10(6) M-1.s-1, K1 = 0.4 +/- 0.21 mM, k2 = 320 +/- 150 s-1, k-2 = (7.2 +/- 0.6) x 10(-5)s-1, a …
The results are in accordance with a two-step reaction model: [formula: see text] The resulting values of the kinetic parameters were: k2/K1 …
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