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Direct probing of copper active site and free radical formed during bicarbonate-dependent peroxidase activity of bovine and human copper, zinc-superoxide dismutases. Low-temperature electron paramagnetic resonance and electron nuclear double resonance studies
Direct probing of copper active site and free radical formed during bicarbonate-dependent peroxidase activity of bovine and human copper, zinc-superoxide dismutases. Low-temperature electron paramagnetic resonance and electron nuclear double resonance studies
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Direct probing of copper active site and free radical formed during bicarbonate-dependent peroxidase activity of bovine and human copper, zinc-superoxide dismutases. Low-temperature electron paramagnetic resonance and electron nuclear double resonance studies

Karunakaran, Chandran ; Zhang, Hao ; Crow, John P ; Antholine, William E ; Kalyanaraman, B

The Journal of biological chemistry, 2004-07, Vol.279 (31), p.32534 [Periódico revisado por pares]

United States

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2
Room-temperature structural studies of SARS-CoV-2 protein NendoU with an X-ray free-electron laser
Room-temperature structural studies of SARS-CoV-2 protein NendoU with an X-ray free-electron laser
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Room-temperature structural studies of SARS-CoV-2 protein NendoU with an X-ray free-electron laser

Jernigan, Rebecca J. ; Logeswaran, Dhenugen ; Doppler, Diandra ; Nagaratnam, Nirupa ; Sonker, Mukul ; Yang, Jay-How ; Ketawala, Gihan ; Martin-Garcia, Jose M. ; Shelby, Megan L. ; Grant, Thomas D. ; Mariani, Valerio ; Tolstikova, Alexandra ; Sheikh, Michelle Z. ; Yung, Mimi Cho ; Coleman, Matthew A. ; Zaare, Sahba ; Kaschner, Emily K. ; Rabbani, Mohammad Towshif ; Nazari, Reza ; Zacks, Michele A. ; Hayes, Brandon ; Sierra, Raymond G. ; Hunter, Mark S. ; Lisova, Stella ; Batyuk, Alexander ; Kupitz, Christopher ; Boutet, Sebastien ; Hansen, Debra T. ; Kirian, Richard A. ; Schmidt, Marius ; Fromme, Raimund ; Frank, Matthias ; Ros, Alexandra ; Chen, Julian J.-L. ; Botha, Sabine ; Fromme, Petra

Structure (London), 2023-02, Vol.31 (2), p.138-151.e5 [Periódico revisado por pares]

United States: Elsevier Ltd

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3
Comparing the temperature dependence of FMN to heme electron transfer in full length and truncated inducible nitric oxide synthase proteins
Comparing the temperature dependence of FMN to heme electron transfer in full length and truncated inducible nitric oxide synthase proteins
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Comparing the temperature dependence of FMN to heme electron transfer in full length and truncated inducible nitric oxide synthase proteins

Li, Wenbing ; Chen, Li ; Fan, Weihong ; Feng, Changjian

FEBS letters, 2012-01, Vol.586 (2), p.159-162 [Periódico revisado por pares]

England: Elsevier B.V

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4
Biological Assessment of the NO-Dependent Endothelial Function
Biological Assessment of the NO-Dependent Endothelial Function
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Biological Assessment of the NO-Dependent Endothelial Function

Boughaleb, Hasnae ; Lobysheva, Irina ; Dei Zotti, Flavia ; Balligand, Jean-Luc ; Montiel, Virginie

Molecules (Basel, Switzerland), 2022-11, Vol.27 (22), p.7921 [Periódico revisado por pares]

Switzerland: MDPI AG

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5
NMR and EPR reveal a compaction of the RNA-binding protein FUS upon droplet formation
NMR and EPR reveal a compaction of the RNA-binding protein FUS upon droplet formation
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NMR and EPR reveal a compaction of the RNA-binding protein FUS upon droplet formation

Emmanouilidis, Leonidas ; Esteban-Hofer, Laura ; Damberger, Fred F ; de Vries, Tebbe ; Nguyen, Cristina K X ; Ibáñez, Luis Fábregas ; Mergenthal, Simon ; Klotzsch, Enrico ; Yulikov, Maxim ; Jeschke, Gunnar ; Allain, Frédéric H-T

Nature chemical biology, 2021-05, Vol.17 (5), p.608-614 [Periódico revisado por pares]

United States: Nature Publishing Group

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6
Modified Metformin as a More Potent Anticancer Drug: Mitochondrial Inhibition, Redox Signaling, Antiproliferative Effects and Future EPR Studies
Modified Metformin as a More Potent Anticancer Drug: Mitochondrial Inhibition, Redox Signaling, Antiproliferative Effects and Future EPR Studies
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Modified Metformin as a More Potent Anticancer Drug: Mitochondrial Inhibition, Redox Signaling, Antiproliferative Effects and Future EPR Studies

Kalyanaraman, Balaraman ; Cheng, Gang ; Hardy, Micael ; Ouari, Olivier ; Sikora, Adam ; Zielonka, Jacek ; Dwinell, Michael B.

Cell biochemistry and biophysics, 2017-12, Vol.75 (3-4), p.311-317 [Periódico revisado por pares]

New York: Springer US

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7
A comparative study of microstructural development in paired human hepatic and gallbladder biles
A comparative study of microstructural development in paired human hepatic and gallbladder biles
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A comparative study of microstructural development in paired human hepatic and gallbladder biles

Weihs, Daphne ; Schmidt, Judith ; Danino, Dganit ; Goldiner, Ilana ; Leikin-Gobbi, Diana ; Eitan, Arieh ; Rubin, Moshe ; Talmon, Yeshayahu ; Konikoff, Fred M.

Biochimica et biophysica acta. Molecular and cell biology of lipids, 2007-10, Vol.1771 (10), p.1289-1298 [Periódico revisado por pares]

Elsevier B.V

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8
Exploring the dynamics and structure of PpiB in living Escherichia coli cells using electron paramagnetic resonance spectroscopy
Exploring the dynamics and structure of PpiB in living Escherichia coli cells using electron paramagnetic resonance spectroscopy
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Exploring the dynamics and structure of PpiB in living Escherichia coli cells using electron paramagnetic resonance spectroscopy

Ben‐Ishay, Yasmin ; Barak, Yoav ; Feintuch, Akiva ; Ouari, Olivier ; Pierro, Annalisa ; Mileo, Elisabetta ; Su, Xun‐Cheng ; Goldfarb, Daniella

Protein science, 2024-03, Vol.33 (3), p.e4903-n/a [Periódico revisado por pares]

Hoboken, USA: John Wiley & Sons, Inc

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9
Chain dynamics in the low-temperature phases of lipid membranes by electron spin-echo spectroscopy
Chain dynamics in the low-temperature phases of lipid membranes by electron spin-echo spectroscopy
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Chain dynamics in the low-temperature phases of lipid membranes by electron spin-echo spectroscopy

Bartucci, Rosa ; Guzzi, Rita ; Marsh, Derek ; Sportelli, Luigi

Journal of magnetic resonance (1997), 2003-06, Vol.162 (2), p.371-379 [Periódico revisado por pares]

United States: Elsevier Inc

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10
Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding. Relaxation kinetic studies with coenzyme analogues
Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding. Relaxation kinetic studies with coenzyme analogues
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Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding. Relaxation kinetic studies with coenzyme analogues

Gutierrez, Aldo ; Munro, Andrew W ; Grunau, Alex ; Wolf, C Roland ; Scrutton, Nigel S ; Roberts, Gordon C K

European journal of biochemistry, 2003-06, Vol.270 (12), p.2612-2621 [Periódico revisado por pares]

England

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