Apoproteins

"Apoproteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).

Descriptor ID	D001059
MeSH Number(s)	D12.776.070
Concept/Terms	Apoproteins Apoproteins Apoprotein

Below are MeSH descriptors whose meaning is more general than "Apoproteins".

Chemicals and Drugs [D]
Amino Acids, Peptides, and Proteins [D12]
Proteins [D12.776]
Apoproteins [D12.776.070]

Below are MeSH descriptors whose meaning is related to "Apoproteins".

Below are MeSH descriptors whose meaning is more specific than "Apoproteins".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Apoproteins" by people in this website by year, and whether "Apoproteins" was a major or minor topic of these publications.

Bar chart showing 11 publications over 6 distinct years, with a maximum of 3 publications in 2008 and 2010

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
1998	1	0	1
2004	1	0	1
2007	1	1	2
2008	1	2	3
2010	0	3	3
2019	1	0	1

Below are the most recent publications written about "Apoproteins" by people in Profiles.

Cozzolino M, Pesce L, Pezzuoli D, Montali C, Brancaleon L, Cavanna L, Abbruzzetti S, Diaspro A, Bianchini P, Viappiani C. Apomyoglobin is an efficient carrier for zinc phthalocyanine in photodynamic therapy of tumors. Biophys Chem. 2019 10; 253:106228.

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Stefl M, James NG, Ross JA, Jameson DM. Applications of phasors to in vitro time-resolved fluorescence measurements. Anal Biochem. 2011 Mar 01; 410(1):62-9.

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Morleo A, Bonomi F, Iametti S, Huang VW, Kurtz DM. Iron-nucleated folding of a metalloprotein in high urea: resolution of metal binding and protein folding events. Biochemistry. 2010 Aug 10; 49(31):6627-34.

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James NG, Ross JA, Mason AB, Jameson DM. Excited-state lifetime studies of the three tryptophan residues in the N-lobe of human serum transferrin. Protein Sci. 2010 Jan; 19(1):99-110.

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Jiang Y, Trnka MJ, Medzihradszky KF, Ouellet H, Wang Y, Ortiz de Montellano PR. Covalent heme attachment to the protein in human heme oxygenase-1 with selenocysteine replacing the His25 proximal iron ligand. J Inorg Biochem. 2009 Mar; 103(3):316-25.

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Bonomi F, Iametti S, Ferranti P, Kurtz DM, Morleo A, Ragg EM. "Iron priming" guides folding of denatured aporubredoxins. J Biol Inorg Chem. 2008 Aug; 13(6):981-91.

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Hern?ndez R, Lamboy J, Gao LM, Matta J, Rom?n FR, Mel?ndez E. Structure-activity studies of Ti(IV) complexes: aqueous stability and cytotoxic properties in colon cancer HT-29 cells. J Biol Inorg Chem. 2008 Jun; 13(5):685-92.

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Du H, Xiang J, Zhang Y, Tang Y, Xu G. Binding of V(IV) to human transferrin: potential relevance to anticancer activity of vanadocene dichloride. J Inorg Biochem. 2008 Jan; 102(1):146-9.

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Gao LM, Hern?ndez R, Matta J, Mel?ndez E. Synthesis, Ti(IV) intake by apotransferrin and cytotoxic properties of functionalized titanocene dichlorides. J Biol Inorg Chem. 2007 Sep; 12(7):959-67.

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Griffith WP, Kaltashov IA. Protein conformational heterogeneity as a binding catalyst: ESI-MS study of hemoglobin H formation. Biochemistry. 2007 Feb 20; 46(7):2020-6.

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