НАДФ-зависимая декарбоксилирующая малатдегидрогеназа (Russian Wikipedia)

Analysis of information sources in references of the Wikipedia article "НАДФ-зависимая декарбоксилирующая малатдегидрогеназа" in Russian language version.

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6doi.org

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2archive.org

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1books.google.com

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1plantphysiol.org

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1fasebj.org

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1wikipedia.org

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1nature.com

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1worldcat.org

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archive.org (Global: 6^th place; Russian: 9^th place)

Furumoto T., Hata S., Izui K. cDNA cloning and characterization of maize phosphoenolpyruvate carboxykinase, a bundle sheath cell-specific enzyme (англ.) // Plant Molecular Biology : journal. — 1999. — October (vol. 41, no. 3). — P. 301—311. — doi:10.1023/A:1006317120460. — PMID 10598098.
Edwards G.E., Franceschi V.R., Voznesenskaya E.V. Single-cell C(4) photosynthesis versus the dual-cell (Kranz) paradigm (англ.) // Annual Review of Plant Biology : journal. — 2004. — Vol. 55. — P. 173—196. — doi:10.1146/annurev.arplant.55.031903.141725. — PMID 15377218.

books.google.com (Global: 3^rd place; Russian: 10^th place)

Kanai, Ryuzi; Edwards, Gerald E. The Biochemistry of C₄ Photosynthesis // C₄ Plant Biology / Rowan F. Sage, Russell K. Monson. — Academic Press, 1999. — С. 49—87. — ISBN 978-0-08-052839-7.

doi.org (Global: 2^nd place; Russian: 3^rd place)

dx.doi.org

Christopher J.T., Holtum J. Patterns of Carbon Partitioning in Leaves of Crassulacean Acid Metabolism Species during Deacidification (англ.) // Plant Physiology : journal. — American Society of Plant Biologists, 1996. — September (vol. 112, no. 1). — P. 393—399. — doi:10.1104/pp.112.1.393. — PMID 12226397. — PMC 157961.
Furumoto T., Hata S., Izui K. cDNA cloning and characterization of maize phosphoenolpyruvate carboxykinase, a bundle sheath cell-specific enzyme (англ.) // Plant Molecular Biology : journal. — 1999. — October (vol. 41, no. 3). — P. 301—311. — doi:10.1023/A:1006317120460. — PMID 10598098.
Rossman, Michael G.; Liljas, Anders; Brändén, Carl-Ivar; Banaszak, Leonard J. Evolutionary and Structural Relationships among Dehydrogenases // The Enzymes / Boyer, Paul D.. — 1975. — Т. 11. — С. 61—102. — ISBN 978-0-12-122711-1. — doi:10.1016/S1874-6047(08)60210-3.
Coleman, David E.; Rao, G. S. Jagannatha; Goldsmith, E. J.; Cook, Paul F.; Harris, Ben G. Crystal Structure of the Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide at 2.3 Å Resolution (англ.) // Biochemistry : journal. — 2002. — June (vol. 41, no. 22). — P. 6928—6938. — doi:10.1021/bi0255120. — PMID 12033925.
Edwards G.E., Franceschi V.R., Voznesenskaya E.V. Single-cell C(4) photosynthesis versus the dual-cell (Kranz) paradigm (англ.) // Annual Review of Plant Biology : journal. — 2004. — Vol. 55. — P. 173—196. — doi:10.1146/annurev.arplant.55.031903.141725. — PMID 15377218.
Veronica G. Maurino, Martin J. Lercher, Maria F. Drincovich, Luitgard Nagel-Steger, Alejandro Buschiazzo. Molecular adaptations of NADP-malic enzyme for its function in C 4 photosynthesis in grasses (англ.) // Nature Plants. — 2019-06-24. — P. 1. — ISSN 2055-0278. — doi:10.1038/s41477-019-0451-7. Архивировано 20 июня 2022 года.

fasebj.org (Global: low place; Russian: 9,960^th place)

Bellamacina C.R. The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins (англ.) // The FASEB Journal^[англ.] : journal. — Federation of American Societies for Experimental Biology^[англ.], 1996. — September (vol. 10, no. 11). — P. 1257—1269. — PMID 8836039. Архивировано 13 апреля 2020 года.

jbc.org (Global: 4,455^th place; Russian: 4,527^th place)

Rothermel B.A., Nelson T. Primary structure of the maize NADP-dependent malic enzyme (англ.) // The Journal of Biological Chemistry : journal. — 1989. — November (vol. 264, no. 33). — P. 19587—19592. — PMID 2584183.

nature.com (Global: 234^th place; Russian: 157^th place)

Veronica G. Maurino, Martin J. Lercher, Maria F. Drincovich, Luitgard Nagel-Steger, Alejandro Buschiazzo. Molecular adaptations of NADP-malic enzyme for its function in C 4 photosynthesis in grasses (англ.) // Nature Plants. — 2019-06-24. — P. 1. — ISSN 2055-0278. — doi:10.1038/s41477-019-0451-7. Архивировано 20 июня 2022 года.

nih.gov (Global: 4^th place; Russian: 6^th place)

ncbi.nlm.nih.gov

Christopher J.T., Holtum J. Patterns of Carbon Partitioning in Leaves of Crassulacean Acid Metabolism Species during Deacidification (англ.) // Plant Physiology : journal. — American Society of Plant Biologists, 1996. — September (vol. 112, no. 1). — P. 393—399. — doi:10.1104/pp.112.1.393. — PMID 12226397. — PMC 157961.
Furumoto T., Hata S., Izui K. cDNA cloning and characterization of maize phosphoenolpyruvate carboxykinase, a bundle sheath cell-specific enzyme (англ.) // Plant Molecular Biology : journal. — 1999. — October (vol. 41, no. 3). — P. 301—311. — doi:10.1023/A:1006317120460. — PMID 10598098.
Bellamacina C.R. The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins (англ.) // The FASEB Journal^[англ.] : journal. — Federation of American Societies for Experimental Biology^[англ.], 1996. — September (vol. 10, no. 11). — P. 1257—1269. — PMID 8836039. Архивировано 13 апреля 2020 года.
Rothermel B.A., Nelson T. Primary structure of the maize NADP-dependent malic enzyme (англ.) // The Journal of Biological Chemistry : journal. — 1989. — November (vol. 264, no. 33). — P. 19587—19592. — PMID 2584183.
Coleman, David E.; Rao, G. S. Jagannatha; Goldsmith, E. J.; Cook, Paul F.; Harris, Ben G. Crystal Structure of the Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide at 2.3 Å Resolution (англ.) // Biochemistry : journal. — 2002. — June (vol. 41, no. 22). — P. 6928—6938. — doi:10.1021/bi0255120. — PMID 12033925.
Edwards G.E., Franceschi V.R., Voznesenskaya E.V. Single-cell C(4) photosynthesis versus the dual-cell (Kranz) paradigm (англ.) // Annual Review of Plant Biology : journal. — 2004. — Vol. 55. — P. 173—196. — doi:10.1146/annurev.arplant.55.031903.141725. — PMID 15377218.

plantphysiol.org (Global: low place; Russian: low place)

Christopher J.T., Holtum J. Patterns of Carbon Partitioning in Leaves of Crassulacean Acid Metabolism Species during Deacidification (англ.) // Plant Physiology : journal. — American Society of Plant Biologists, 1996. — September (vol. 112, no. 1). — P. 393—399. — doi:10.1104/pp.112.1.393. — PMID 12226397. — PMC 157961.

web.archive.org (Global: 1^st place; Russian: 1^st place)

Bellamacina C.R. The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins (англ.) // The FASEB Journal^[англ.] : journal. — Federation of American Societies for Experimental Biology^[англ.], 1996. — September (vol. 10, no. 11). — P. 1257—1269. — PMID 8836039. Архивировано 13 апреля 2020 года.
Veronica G. Maurino, Martin J. Lercher, Maria F. Drincovich, Luitgard Nagel-Steger, Alejandro Buschiazzo. Molecular adaptations of NADP-malic enzyme for its function in C 4 photosynthesis in grasses (англ.) // Nature Plants. — 2019-06-24. — P. 1. — ISSN 2055-0278. — doi:10.1038/s41477-019-0451-7. Архивировано 20 июня 2022 года.

wikipedia.org (Global: low place; Russian: low place)

en.wikipedia.org

Bellamacina C.R. The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins (англ.) // The FASEB Journal^[англ.] : journal. — Federation of American Societies for Experimental Biology^[англ.], 1996. — September (vol. 10, no. 11). — P. 1257—1269. — PMID 8836039. Архивировано 13 апреля 2020 года.

worldcat.org (Global: 5^th place; Russian: 5^th place)

Veronica G. Maurino, Martin J. Lercher, Maria F. Drincovich, Luitgard Nagel-Steger, Alejandro Buschiazzo. Molecular adaptations of NADP-malic enzyme for its function in C 4 photosynthesis in grasses (англ.) // Nature Plants. — 2019-06-24. — P. 1. — ISSN 2055-0278. — doi:10.1038/s41477-019-0451-7. Архивировано 20 июня 2022 года.

НАДФ-зависимая декарбоксилирующая малатдегидрогеназа (Russian Wikipedia)

archive.org (Global: 6th place; Russian: 9th place)

books.google.com (Global: 3rd place; Russian: 10th place)

doi.org (Global: 2nd place; Russian: 3rd place)

dx.doi.org

fasebj.org (Global: low place; Russian: 9,960th place)

jbc.org (Global: 4,455th place; Russian: 4,527th place)

nature.com (Global: 234th place; Russian: 157th place)

nih.gov (Global: 4th place; Russian: 6th place)

ncbi.nlm.nih.gov

plantphysiol.org (Global: low place; Russian: low place)

web.archive.org (Global: 1st place; Russian: 1st place)

wikipedia.org (Global: low place; Russian: low place)

en.wikipedia.org

worldcat.org (Global: 5th place; Russian: 5th place)

archive.org (Global: 6^th place; Russian: 9^th place)

books.google.com (Global: 3^rd place; Russian: 10^th place)

doi.org (Global: 2^nd place; Russian: 3^rd place)

fasebj.org (Global: low place; Russian: 9,960^th place)

jbc.org (Global: 4,455^th place; Russian: 4,527^th place)

nature.com (Global: 234^th place; Russian: 157^th place)

nih.gov (Global: 4^th place; Russian: 6^th place)

web.archive.org (Global: 1^st place; Russian: 1^st place)

worldcat.org (Global: 5^th place; Russian: 5^th place)