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Showing 1 to 12 of 191 entries
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Girls' Stuff, boys' stuff and mental rotation: fourth graders rotate faster with gender-congruent stimuli

STEM and boys

Schürmann L.
GSID: e-m333lYK6IJ
V Ruthsatz, M Rahe, L Schürmann… - Journal of Cognitive …, 2019 - Taylor & Francis

Males outperform females in mental-rotation for various reasons, eg stimuli characteristics. This study tested the hypothesis that girls and boys solve mental-rotation tests with female- or …

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Ruthsatz, V., Rahe, M., Schürmann, L., & Quaiser-Pohl, C. (2019). Girls’ Stuff, boys’ stuff and mental rotation: fourth graders rotate faster with gender-congruent stimuli. Journal of Cognitive Psychology, 31(2), 225-239.
Ruthsatz, Vera, et al. "Girls’ Stuff, boys’ stuff and mental rotation: fourth graders rotate faster with gender-congruent stimuli." Journal of Cognitive Psychology 31.2 (2019): 225-239.
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Initial impacts of No Child Left Behind on elementary science education

Science education

Scharmann L.
GSID: FNoSi3jID1QJ
G Griffith, L Scharmann - Journal of elementary science education, 2008 - Springer

This research examines the impact of the No Child Left Behind (NCLB) Act on elementary science education within a Midwestern state possessing strong national education …

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Griffith, G., & Scharmann, L. (2008). Initial impacts of No Child Left Behind on elementary science education. Journal of elementary science education, 20(3), 35-48.
Griffith, George, and Lawrence Scharmann. "Initial impacts of No Child Left Behind on elementary science education." Journal of elementary science education 20.3 (2008): 35-48.
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Reduction of ferredoxin:thioredoxin reductase by artificial electron donors.

Photosynthesis research

Schürmann P, Stritt-Etter AL, Li J.
PMID: 24301597
Photosynth Res. 1995 Nov;46(1):309-12. doi: 10.1007/BF00020445.

The ferredoxin:thioredoxin reductase is an essential enzyme of the light dependent regulatory system in oxygenic photosynthesis. It is composed of two dissimilar subunits and contains a 4Fe-4S cluster and a redox-active disulfide bridge. Artificial electron donors of redox potentials...

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Schürmann P, Stritt-Etter AL, Li J. Reduction of ferredoxin:thioredoxin reductase by artificial electron donors. Photosynth Res. 1995;46(1):309-12doi: 10.1007/BF00020445.
Schürmann, P., Stritt-Etter, A. L., & Li, J. (1995). Reduction of ferredoxin:thioredoxin reductase by artificial electron donors. Photosynthesis research, 46(1), 309-12. https://doi.org/10.1007/BF00020445
Schürmann, P, et al. "Reduction of ferredoxin:thioredoxin reductase by artificial electron donors." Photosynthesis research vol. 46,1 (1995): 309-12. doi: https://doi.org/10.1007/BF00020445
Schürmann P, Stritt-Etter AL, Li J. Reduction of ferredoxin:thioredoxin reductase by artificial electron donors. Photosynth Res. 1995 Nov;46(1):309-12. doi: 10.1007/BF00020445. PMID: 24301597.
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Stability of the Parent Anion of the Potential Radiosensitizer 8-Bromoadenine Formed by Low-Energy (<3 eV) Electron Attachment.

The journal of physical chemistry. B

Schürmann R, Tanzer K, Dąbkowska I, Denifl S, Bald I.
PMID: 28525718
J Phys Chem B. 2017 Jun 15;121(23):5730-5734. doi: 10.1021/acs.jpcb.7b02130. Epub 2017 Jun 02.

8-Bromoadenine (

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Schürmann R, Tanzer K, Dąbkowska I, et al. Stability of the Parent Anion of the Potential Radiosensitizer 8-Bromoadenine Formed by Low-Energy (<3 eV) Electron Attachment. J Phys Chem B. 2017;121(23):5730-5734doi: 10.1021/acs.jpcb.7b02130.
Schürmann, R., Tanzer, K., Dąbkowska, I., Denifl, S., & Bald, I. (2017). Stability of the Parent Anion of the Potential Radiosensitizer 8-Bromoadenine Formed by Low-Energy (<3 eV) Electron Attachment. The journal of physical chemistry. B, 121(23), 5730-5734. https://doi.org/10.1021/acs.jpcb.7b02130
Schürmann, Robin, et al. "Stability of the Parent Anion of the Potential Radiosensitizer 8-Bromoadenine Formed by Low-Energy (<3 eV) Electron Attachment." The journal of physical chemistry. B vol. 121,23 (2017): 5730-5734. doi: https://doi.org/10.1021/acs.jpcb.7b02130
Schürmann R, Tanzer K, Dąbkowska I, Denifl S, Bald I. Stability of the Parent Anion of the Potential Radiosensitizer 8-Bromoadenine Formed by Low-Energy (<3 eV) Electron Attachment. J Phys Chem B. 2017 Jun 15;121(23):5730-5734. doi: 10.1021/acs.jpcb.7b02130. Epub 2017 Jun 02. PMID: 28525718.
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Ring Finger Protein 11 Inhibits Melanocortin 3 and 4 Receptor Signaling.

Frontiers in endocrinology

Müller A, Niederstadt L, Jonas W, Yi CX, Meyer F, Wiedmer P, Fischer J, Grötzinger C, Schürmann A, Tschöp M, Kleinau G, Grüters A, Krude H, Biebermann H.
PMID: 27551276
Front Endocrinol (Lausanne). 2016 Aug 08;7:109. doi: 10.3389/fendo.2016.00109. eCollection 2016.

Intact melanocortin signaling via the G protein-coupled receptors (GPCRs), melanocortin receptor 4 (MC4R), and melanocortin receptor 3 (MC3R) is crucial for body weight maintenance. So far, no connection between melanocortin signaling and hypothalamic inflammation has been reported. Using a...

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Müller A, Niederstadt L, Jonas W, et al. Ring Finger Protein 11 Inhibits Melanocortin 3 and 4 Receptor Signaling. Front Endocrinol (Lausanne). 2016;7:109doi: 10.3389/fendo.2016.00109.
Müller, A., Niederstadt, L., Jonas, W., Yi, C. X., Meyer, F., Wiedmer, P., Fischer, J., Grötzinger, C., Schürmann, A., Tschöp, M., Kleinau, G., Grüters, A., Krude, H., & Biebermann, H. (2016). Ring Finger Protein 11 Inhibits Melanocortin 3 and 4 Receptor Signaling. Frontiers in endocrinology, 7109. https://doi.org/10.3389/fendo.2016.00109
Müller, Anne, et al. "Ring Finger Protein 11 Inhibits Melanocortin 3 and 4 Receptor Signaling." Frontiers in endocrinology vol. 7 (2016): 109. doi: https://doi.org/10.3389/fendo.2016.00109
Müller A, Niederstadt L, Jonas W, Yi CX, Meyer F, Wiedmer P, Fischer J, Grötzinger C, Schürmann A, Tschöp M, Kleinau G, Grüters A, Krude H, Biebermann H. Ring Finger Protein 11 Inhibits Melanocortin 3 and 4 Receptor Signaling. Front Endocrinol (Lausanne). 2016 Aug 08;7:109. doi: 10.3389/fendo.2016.00109. eCollection 2016. PMID: 27551276; PMCID: PMC4976663.
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A dicistronic construct for the expression of functional spinach chloroplast ferredoxin:thioredoxin reductase in Escherichia coli.

Plant science : an international journal of experimental plant biology

Gaymard E, Franchini L, Manieri W, Stutz E, Schürmann P.
PMID: 10996250
Plant Sci. 2000 Sep 08;158(1):107-113. doi: 10.1016/s0168-9452(00)00310-1.

Ferredoxin:thioredoxin reductase (FTR) is a heterodimeric Fe&z.sbnd;S containing disulfide reductase involved in the light-dependent activation of photosynthetic enzymes. We have designed a dicistronic construct for the heterologous expression of this nucleus encoded chloroplast protein in Escherichia coli. The coding...

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Gaymard E, Franchini L, Manieri W, et al. A dicistronic construct for the expression of functional spinach chloroplast ferredoxin:thioredoxin reductase in Escherichia coli. Plant Sci. 2000;158(1):107-113doi: 10.1016/s0168-9452(00)00310-1.
Gaymard, E., Franchini, L., Manieri, W., Stutz, E., & Schürmann, P. (2000). A dicistronic construct for the expression of functional spinach chloroplast ferredoxin:thioredoxin reductase in Escherichia coli. Plant science : an international journal of experimental plant biology, 158(1), 107-113. https://doi.org/10.1016/s0168-9452(00)00310-1
Gaymard, et al. "A dicistronic construct for the expression of functional spinach chloroplast ferredoxin:thioredoxin reductase in Escherichia coli." Plant science : an international journal of experimental plant biology vol. 158,1 (2000): 107-113. doi: https://doi.org/10.1016/s0168-9452(00)00310-1
Gaymard E, Franchini L, Manieri W, Stutz E, Schürmann P. A dicistronic construct for the expression of functional spinach chloroplast ferredoxin:thioredoxin reductase in Escherichia coli. Plant Sci. 2000 Sep 08;158(1):107-113. doi: 10.1016/s0168-9452(00)00310-1. PMID: 10996250.
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Local atomic environment of Si suboxides at the SiO2/Si(111) interface determined by angle-scanned photoelectron diffraction.

Physical review letters

Dreiner S, Schürmann M, Westphal C, Zacharias H.
PMID: 11328097
Phys Rev Lett. 2001 Apr 30;86(18):4068-71. doi: 10.1103/PhysRevLett.86.4068.

Local environments of Si suboxides at the interface between a thermally grown SiO2 film and Si(111) were studied by angle-scanned photoelectron diffraction. Si 2p core-level spectra containing chemically shifted components were recorded. The components were deconvoluted by least squares...

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Dreiner S, Schürmann M, Westphal C, et al. Local atomic environment of Si suboxides at the SiO2/Si(111) interface determined by angle-scanned photoelectron diffraction. Phys Rev Lett. 2001;86(18):4068-71doi: 10.1103/PhysRevLett.86.4068.
Dreiner, S., Schürmann, M., Westphal, C., & Zacharias, H. (2001). Local atomic environment of Si suboxides at the SiO2/Si(111) interface determined by angle-scanned photoelectron diffraction. Physical review letters, 86(18), 4068-71. https://doi.org/10.1103/PhysRevLett.86.4068
Dreiner, S, et al. "Local atomic environment of Si suboxides at the SiO2/Si(111) interface determined by angle-scanned photoelectron diffraction." Physical review letters vol. 86,18 (2001): 4068-71. doi: https://doi.org/10.1103/PhysRevLett.86.4068
Dreiner S, Schürmann M, Westphal C, Zacharias H. Local atomic environment of Si suboxides at the SiO2/Si(111) interface determined by angle-scanned photoelectron diffraction. Phys Rev Lett. 2001 Apr 30;86(18):4068-71. doi: 10.1103/PhysRevLett.86.4068. PMID: 11328097.
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VTE Risk assessment - a prognostic Model: BATER Cohort Study of young women.

Thrombosis journal

Heinemann LA, Dominh T, Assmann A, Schramm W, Schürmann R, Hilpert J, Spannagl M.
PMID: 15836797
Thromb J. 2005 Apr 18;3(1):5. doi: 10.1186/1477-9560-3-5.

BACKGROUND: Community-based cohort studies are not available that evaluated the predictive power of both clinical and genetic risk factors for venous thromboembolism (VTE). There is, however, clinical need to forecast the likelihood of future occurrence of VTE, at least...

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Heinemann LA, Dominh T, Assmann A, et al. VTE Risk assessment - a prognostic Model: BATER Cohort Study of young women. Thromb J. 2005;3(1):5doi: 10.1186/1477-9560-3-5.
Heinemann, L. A., Dominh, T., Assmann, A., Schramm, W., Schürmann, R., Hilpert, J., & Spannagl, M. (2005). VTE Risk assessment - a prognostic Model: BATER Cohort Study of young women. Thrombosis journal, 3(1), 5. https://doi.org/10.1186/1477-9560-3-5
Heinemann, Lothar Aj, et al. "VTE Risk assessment - a prognostic Model: BATER Cohort Study of young women." Thrombosis journal vol. 3,1 (2005): 5. doi: https://doi.org/10.1186/1477-9560-3-5
Heinemann LA, Dominh T, Assmann A, Schramm W, Schürmann R, Hilpert J, Spannagl M. VTE Risk assessment - a prognostic Model: BATER Cohort Study of young women. Thromb J. 2005 Apr 18;3(1):5. doi: 10.1186/1477-9560-3-5. PMID: 15836797; PMCID: PMC1087887.
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Effect of powdery mildew infection on photosynthesis by leaves and chloroplasts of sugar beets.

Plant physiology

Magyarosy AC, Schürmann P, Buchanan BB.
PMID: 16659511
Plant Physiol. 1976 Apr;57(4):486-9. doi: 10.1104/pp.57.4.486.

Chloroplasts isolated from powdery mildew-infected (Erysiphe polygoni DC) sugar beet leaves (Beta vulgaris L) showed a reduction in the rate of electron transport and in the accompanying ATP formation in noncyclic photophosphorylation (water as electron donor, NADP as electron...

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Magyarosy AC, Schürmann P, Buchanan BB. Effect of powdery mildew infection on photosynthesis by leaves and chloroplasts of sugar beets. Plant Physiol. 1976;57(4):486-9doi: 10.1104/pp.57.4.486.
Magyarosy, A. C., Schürmann, P., & Buchanan, B. B. (1976). Effect of powdery mildew infection on photosynthesis by leaves and chloroplasts of sugar beets. Plant physiology, 57(4), 486-9. https://doi.org/10.1104/pp.57.4.486
Magyarosy, A C, et al. "Effect of powdery mildew infection on photosynthesis by leaves and chloroplasts of sugar beets." Plant physiology vol. 57,4 (1976): 486-9. doi: https://doi.org/10.1104/pp.57.4.486
Magyarosy AC, Schürmann P, Buchanan BB. Effect of powdery mildew infection on photosynthesis by leaves and chloroplasts of sugar beets. Plant Physiol. 1976 Apr;57(4):486-9. doi: 10.1104/pp.57.4.486. PMID: 16659511; PMCID: PMC542057.
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Characterization of the regulatory function of the 46-kDa isoform of Rubisco activase from Arabidopsis.

Photosynthesis research

Zhang N, Schürmann P, Portis AR.
PMID: 16228326
Photosynth Res. 2001;68(1):29-37. doi: 10.1023/A:1011845506196.

Arabidopsis Rubisco activase was recently shown to be regulated by redox changes in the larger (46-kDa) isoform specifically mediated by thioredoxin-f [Zhang and Portis (1999) Proc Natl Acad Sci USA 96: 9438-9443]. Reduction greatly increases the activity of the...

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Zhang N, Schürmann P, Portis AR. Characterization of the regulatory function of the 46-kDa isoform of Rubisco activase from Arabidopsis. Photosynth Res. 2001;68(1):29-37doi: 10.1023/A:1011845506196.
Zhang, N., Schürmann, P., & Portis, A. R. (2001). Characterization of the regulatory function of the 46-kDa isoform of Rubisco activase from Arabidopsis. Photosynthesis research, 68(1), 29-37. https://doi.org/10.1023/A:1011845506196
Zhang, N, et al. "Characterization of the regulatory function of the 46-kDa isoform of Rubisco activase from Arabidopsis." Photosynthesis research vol. 68,1 (2001): 29-37. doi: https://doi.org/10.1023/A:1011845506196
Zhang N, Schürmann P, Portis AR. Characterization of the regulatory function of the 46-kDa isoform of Rubisco activase from Arabidopsis. Photosynth Res. 2001;68(1):29-37. doi: 10.1023/A:1011845506196. PMID: 16228326.
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Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts.

Photosynthesis research

Balmer Y, Koller A, Val GD, Schürmann P, Buchanan BB.
PMID: 16328793
Photosynth Res. 2004;79(3):275-80. doi: 10.1023/B:PRES.0000017207.88257.d4.

The ability of thioredoxin f to form an electrostatic (non-covalent) complex, earlier found with fructose-1,6-bisphosphatase, was extended to include 27 previously unrecognized proteins functional in 11 processes of chloroplasts. The proteins were identified by combining thioredoxin f affinity chromatography...

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Balmer Y, Koller A, Val GD, et al. Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynth Res. 2004;79(3):275-80doi: 10.1023/B:PRES.0000017207.88257.d4.
Balmer, Y., Koller, A., Val, G. D., Schürmann, P., & Buchanan, B. B. (2004). Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynthesis research, 79(3), 275-80. https://doi.org/10.1023/B:PRES.0000017207.88257.d4
Balmer, Yves, et al. "Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts." Photosynthesis research vol. 79,3 (2004): 275-80. doi: https://doi.org/10.1023/B:PRES.0000017207.88257.d4
Balmer Y, Koller A, Val GD, Schürmann P, Buchanan BB. Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynth Res. 2004;79(3):275-80. doi: 10.1023/B:PRES.0000017207.88257.d4. PMID: 16328793.
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Solubilizing sodium fluoride in acetonitrile: synthesis, molecular structure, and complexation behavior of bis(organostannyl)methyl-substituted crown ethers.

Chemistry (Weinheim an der Bergstrasse, Germany)

Reeske G, Bradtmöller G, Schürmann M, Jurkschat K.
PMID: 17948329
Chemistry. 2007;13(36):10239-45. doi: 10.1002/chem.200701141.

The synthesis of the crown-ether-substituted bis(organostannyl)methanes Ph(3)SnCH(2)Sn(Ph(2))-CH(2)-[16]crown-5 (1) and Ph(2)ISnCH(2)Sn(I)(Ph)-CH(2)-[16]crown-5 (2) is reported. Both compounds have been characterized by elemental analyses, (1)H, (13)C, (19)F, and (119)Sn NMR spectroscopy, and in the case of compound 2 also by electrospray ionization...

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Reeske G, Bradtmöller G, Schürmann M, et al. Solubilizing sodium fluoride in acetonitrile: synthesis, molecular structure, and complexation behavior of bis(organostannyl)methyl-substituted crown ethers. Chemistry. 2007;13(36):10239-45doi: 10.1002/chem.200701141.
Reeske, G., Bradtmöller, G., Schürmann, M., & Jurkschat, K. (2007). Solubilizing sodium fluoride in acetonitrile: synthesis, molecular structure, and complexation behavior of bis(organostannyl)methyl-substituted crown ethers. Chemistry (Weinheim an der Bergstrasse, Germany), 13(36), 10239-45. https://doi.org/10.1002/chem.200701141
Reeske, Gregor, et al. "Solubilizing sodium fluoride in acetonitrile: synthesis, molecular structure, and complexation behavior of bis(organostannyl)methyl-substituted crown ethers." Chemistry (Weinheim an der Bergstrasse, Germany) vol. 13,36 (2007): 10239-45. doi: https://doi.org/10.1002/chem.200701141
Reeske G, Bradtmöller G, Schürmann M, Jurkschat K. Solubilizing sodium fluoride in acetonitrile: synthesis, molecular structure, and complexation behavior of bis(organostannyl)methyl-substituted crown ethers. Chemistry. 2007;13(36):10239-45. doi: 10.1002/chem.200701141. PMID: 17948329.
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Showing 1 to 12 of 191 entries