Hem A (Slovak Wikipedia)

Analysis of information sources in references of the Wikipedia article "Hem A" in Slovak language version.

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7doi.org

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6nih.gov

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1semanticscholar.org

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doi.org

dx.doi.org

Heme A of Cytochrome c Oxidase. Journal of Biological Chemistry, 1975, s. 7602–7622. DOI: 10.1016/S0021-9258(19)40860-0. PMID 170266.
Isolation, crystallisation, and synthesis of the dimethyl ester of porphyrin a, the iron-free prosthetic group of cytochrome c oxidase. Journal of the Chemical Society, Perkin Transactions 1, 1985, s. 135. DOI: 10.1039/P19850000135.
Cytohämin aus Herzmuskel. Zeitschrift für Physiologische Chemie, 1951, s. 1–4. DOI: 10.1515/bchm2.1951.288.1.1. PMID 14860765.
Yamashita E, Aoyama H, Yao M, Muramoto K, Shinzawa-Itoh K, Yoshikawa S, Tsukihara T.; AOYAMA; YAO. Absolute configuration of the hydroxyfarnesylethyl group of heme A, determined by X-ray structural analysis of bovine heart cytochrome c oxidase using methods applicable at 2.8 Angstrom resolution. Acta Crystallographica D, 2005, s. 1373–1377. DOI: 10.1107/S0907444905023358. PMID 16204889.
Tsukihara T, Shimokata K, Katayama Y, Shimada H, Muramoto K, Aoyama H, Mochizuki M, Shinzawa-Itoh K, Yamashita E, Yao M, Ishimura Y, Yoshikawa S.; SHIMOKATA; KATAYAMA. The low-spin heme of cytochrome c oxidase as the driving element of the proton-pumping process. PNAS, 2003, s. 15304–15309. DOI: 10.1073/pnas.2635097100. PMID 14673090.
Redox-Coupled Crystal Structural Changes in Bovine Heart Cytochrome c Oxidase. Science, 1998, s. 1723–1729. Dostupné online. DOI: 10.1126/science.280.5370.1723. PMID 9624044.
Shimokata K, Katayama Y, Murayama H, Suematsu M, Tsukihara T, Muramoto K, Aoyama H, Yoshikawa S, Shimada H.; KATAYAMA; MURAYAMA. The proton pumping pathway of bovine heart cytochrome c oxidase. PNAS, 2007, s. 4200–4205. DOI: 10.1073/pnas.0611627104. PMID 17360500.

nih.gov

ncbi.nlm.nih.gov

Heme A of Cytochrome c Oxidase. Journal of Biological Chemistry, 1975, s. 7602–7622. DOI: 10.1016/S0021-9258(19)40860-0. PMID 170266.
Cytohämin aus Herzmuskel. Zeitschrift für Physiologische Chemie, 1951, s. 1–4. DOI: 10.1515/bchm2.1951.288.1.1. PMID 14860765.
Yamashita E, Aoyama H, Yao M, Muramoto K, Shinzawa-Itoh K, Yoshikawa S, Tsukihara T.; AOYAMA; YAO. Absolute configuration of the hydroxyfarnesylethyl group of heme A, determined by X-ray structural analysis of bovine heart cytochrome c oxidase using methods applicable at 2.8 Angstrom resolution. Acta Crystallographica D, 2005, s. 1373–1377. DOI: 10.1107/S0907444905023358. PMID 16204889.
Tsukihara T, Shimokata K, Katayama Y, Shimada H, Muramoto K, Aoyama H, Mochizuki M, Shinzawa-Itoh K, Yamashita E, Yao M, Ishimura Y, Yoshikawa S.; SHIMOKATA; KATAYAMA. The low-spin heme of cytochrome c oxidase as the driving element of the proton-pumping process. PNAS, 2003, s. 15304–15309. DOI: 10.1073/pnas.2635097100. PMID 14673090.
Redox-Coupled Crystal Structural Changes in Bovine Heart Cytochrome c Oxidase. Science, 1998, s. 1723–1729. Dostupné online. DOI: 10.1126/science.280.5370.1723. PMID 9624044.
Shimokata K, Katayama Y, Murayama H, Suematsu M, Tsukihara T, Muramoto K, Aoyama H, Yoshikawa S, Shimada H.; KATAYAMA; MURAYAMA. The proton pumping pathway of bovine heart cytochrome c oxidase. PNAS, 2007, s. 4200–4205. DOI: 10.1073/pnas.0611627104. PMID 17360500.

semanticscholar.org

Redox-Coupled Crystal Structural Changes in Bovine Heart Cytochrome c Oxidase. Science, 1998, s. 1723–1729. Dostupné online. DOI: 10.1126/science.280.5370.1723. PMID 9624044.