Results 241 to 250 of about 101,597 (287)

Functional anatomy, jaw mechanisms, and feeding behavior of Dunkleosteus terrelli (Placodermi, Arthrodira)

The Anatomical Record, EarlyView.
A new musculoskeletal reconstruction and revision of the cranio‐mandibular anatomy of the Devonian arthrodire placoderm Dunkleosteus terrelli from a comparative and functional anatomical perspective. Dunkleosteus is a specialized arthrodire with many specializations for feeding on large vertebrates, and many of its features are part of broader ...
Russell K. Engelman, Robert K. Carr, Kate Trinajstic, Zerina Johanson, Oleg A. Lebedev   +4 more
wiley   +1 more source

Characterization of Polyphenolic Compounds and Antioxidant Activities of <i>Tagetes</i> Flowers With Varying Treatments Using LC-ESI-QToF-MS/MS. [PDF]

Food Sci Nutr
Siddiqa A, Khaliq A, Sultan MT, Chugthai MFJ, Ahsan S, Khalid W, Suleria H.   +6 more
europepmc   +1 more source

Potent antioxidant and mitochondrial-protective effects of ATH434, a moderate affinity iron chaperone. [PDF]

J Biol Chem
Bailey DK, Nihlawi R, Bradbury MJ, Bond S, Kosman DJ.   +4 more
europepmc   +1 more source

Three decades of selective product formation <i>via</i> Griesbaum co-ozonolysis: insight and advances (1995-2025). [PDF]

RSC Adv
Zain-Ul-Abideen M, Saeed A, Haider MB, Shabir G, El-Seedi HR.   +4 more
europepmc   +1 more source

Rational design of indoleamine 2,3-dioxygenase 1 (IDO1) inhibitors featuring 1,2,3-triazole derivatives with enhanced anti-inflammatory and analgesic efficacy. [PDF]

Front Pharmacol
Liu Q, Hou X, Wang Y, Tian M, He B, Guo J, Yang J.   +6 more
europepmc   +1 more source

Ferroptosis-The "Double-Edged Sword" in Cancer: Mechanisms of Tumor Suppression/Resistance and Therapeutic Manipulation. [PDF]

Biology (Basel)
Quaranto D, DeSouza NR, Carnazza M, Moscatello A, Islam HK, Li XM, Tiwari RK, Geliebter J.   +7 more
europepmc   +1 more source

Preparation and characteristics evaluation of chitosan-coated nanoliposomes containing ferrous sulfate. [PDF]

Sci Rep
Shirnoush N, Emamifar A, Davati N.
europepmc   +1 more source

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The nitrosyl compounds of ferrous animal haloperoxidases

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
Human myeloperoxidase, human eosinophil peroxidase and bovine lactoperoxidase (donor: hydrogen-peroxide oxidoreductase, EC 1.11.1.7) reduced with ascorbic acid form nitrosyl compounds which show rhombic EPR signals centered at g = 2. Using 14NO (IN = 1), the central resonance signal exhibited a hyperfine structure of nine lines originating from a ...
B G, Bolscher, R, Wever
openaire   +2 more sources

The nitrosyl compound of ferrous lactoperoxidase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
Abstract The nitrosyl compound of reduced bovine lactoperoxidase (donor:hydrogen-peroxide oxidoreductase, EC 1.11.1.7) has been prepared using two methods of initial reduction prior to exposure to NO; namely, dithionite and electrochemical reduction.
Gunnel Sievers, Jim Peterson, Paul M.A. Gadsby, Andrew J. Thomson   +3 more
openaire   +1 more source

A Superoxo-Ferrous State in a Reduced Oxy-Ferrous Hemoprotein and Model Compounds

Journal of the American Chemical Society, 2003
Cryoreduction of the [FeO2]6 (n = 6 is the number of electrons in 3d orbitals on Fe and pi* orbitals on O2) dioxygen-bound ferroheme through irradiation at 77 K generates an [FeO2]7 reduced oxy-heme. Numerous investigations have examined [FeO2]7 centers that have been characterized as peroxo-ferric centers, denoted [FeO2]per7, in which a ferriheme ...
Roman, Davydov, James D, Satterlee, Hiroshi, Fujii, Alexandra, Sauer-Masarwa, Daryle H, Busch, Brian M, Hoffman   +5 more
openaire   +2 more sources