The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The human fatty acid-binding protein family: Evolutionary divergences and functions
Open accessAbstract
Fatty acid-binding proteins (FABPs) are members of the intracellular lipid-binding protein (iLBP) family and are involved in reversibly binding intracellular hydrophobic ligands and trafficking them throughout cellular compartments, including the peroxisomes, mitochondria, endoplasmic reticulum and nucleus. FABPs are small, structurally conserved cytosolic proteins consisting of a water-filled, interior-binding pocket surrounded by ten anti-parallel beta sheets, forming a beta barrel. At the superior surface, two alpha-helices cap the pocket and are thought to regulate binding. FABPs have broad specificity, including the ability to bind long-chain (C16-C20) fatty acids, eicosanoids, bile salts and peroxisome proliferators. FABPs demonstrate strong evolutionary conservation and are present in a spectrum of species including Drosophila melanogaster, Caenorhabditis elegans, mouse and human. The human genome consists of nine putatively functional protein-coding FABP genes. The most recently identified family member, FABP12, has been less studied.
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The lipocalin protein family: structure and function
FLOWER, D. R. (1996) · Biochemical Journal · doi:10.1042/bj3180001 · Cited by 1,679 · cited 1×
“Other members of the calycin superfamily include the avidins and the lipocalins.(23,30,31) Interestingly, the homology between these family members is relatively low ( 10 per cent amino acid identity), yet they still share the characteristic b-barrel tertiary structure.”
BackgroundCrystal Structure and Thermodynamic Analysis of Human Brain Fatty Acid-binding Protein
Balendiran, G. K., Schnütgen, F., Scapin, G., Börchers, T., Xhong, N., Lim, K., Godbout, R., Spener, F., & Sacchettini, J. C. (2000) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61478-x · Cited by 217
Altered emotional behavioral responses in mice lacking brain‐type fatty acid‐binding protein gene
Owada, Y., Abdelwahab, S. A., Kitanaka, N., Sakagami, H., Takano, H., Sugitani, Y., Sugawara, M., Kawashima, H., Kiso, Y., Mobarakeh, J. I., et al. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.04855.x · Cited by 154
Cited by
Triglyceride Metabolism in the Liver
Alves‐Bezerra, M., & Cohen, D. E. (2017) · Comprehensive Physiology · doi:10.1002/cphy.c170012 · Cited by 1,016
Bensaad, K., Favaro, E., Lewis, C. A., Peck, B., Lord, S., Collins, J. M., Pinnick, K. E., Wigfield, S., Buffa, F. M., Li, J.-L., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.08.056 · Cited by 665
Intestinal transport and metabolism of bile acids
Dawson, P. A., & Karpen, S. J. (2015) · Journal of Lipid Research · doi:10.1194/jlr.r054114 · Cited by 598
Molecular Targets of Cannabidiol in Neurological Disorders
Ibeas Bih, C., Chen, T., Nunn, A. V. W., Bazelot, M., Dallas, M., & Whalley, B. J. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0377-3 · Cited by 578
Acyl-CoA Metabolism and Partitioning
Grevengoed, T. J., Klett, E. L., & Coleman, R. A. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071813-105541 · Cited by 440
Metadata
- Authors
- Smathers, R. L., & Petersen, D. R.
- Venue
- Human Genomics
- Published
- 2011
- Volume
- 5
- Issue
- 3
- Pages
- 170
- ISSN
- 1473-9542 (ISSN-L)
- 1479-7364
- OpenAlex
- W1972168184
- Cited by
- 492
- References
- 3
- FWCI
- 7.29
- Type
- journal article
- Language
- en
- Open access
- gold
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