Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 13 entries
Sorted by: Best Match Show Resources per page
Genome-wide association analysis confirms and extends the association of SLC2A9 with serum uric acid levels to Mexican Americans.

Frontiers in genetics

Voruganti VS, Kent JW, Debnath S, Cole SA, Haack K, Göring HH, Carless MA, Curran JE, Johnson MP, Almasy L, Dyer TD, Maccluer JW, Moses EK, Abboud HE, Mahaney MC, Blangero J, Comuzzie AG.
PMID: 24379826
Front Genet. 2013 Dec 16;4:279. doi: 10.3389/fgene.2013.00279. eCollection 2013.

Increased serum uric acid (SUA) is a risk factor for gout and renal and cardiovascular disease (CVD). The purpose of this study was to identify genetic factors that affect the variation in SUA in 632 Mexican Americans participants of...

Cite
Voruganti VS, Kent JW, Debnath S, et al. Genome-wide association analysis confirms and extends the association of SLC2A9 with serum uric acid levels to Mexican Americans. Front Genet. 2013;4:279doi: 10.3389/fgene.2013.00279.
Voruganti, V. S., Kent, J. W., Debnath, S., Cole, S. A., Haack, K., Göring, H. H., Carless, M. A., Curran, J. E., Johnson, M. P., Almasy, L., Dyer, T. D., Maccluer, J. W., Moses, E. K., Abboud, H. E., Mahaney, M. C., Blangero, J., & Comuzzie, A. G. (2013). Genome-wide association analysis confirms and extends the association of SLC2A9 with serum uric acid levels to Mexican Americans. Frontiers in genetics, 4279. https://doi.org/10.3389/fgene.2013.00279
Voruganti, Venkata Saroja, et al. "Genome-wide association analysis confirms and extends the association of SLC2A9 with serum uric acid levels to Mexican Americans." Frontiers in genetics vol. 4 (2013): 279. doi: https://doi.org/10.3389/fgene.2013.00279
Voruganti VS, Kent JW, Debnath S, Cole SA, Haack K, Göring HH, Carless MA, Curran JE, Johnson MP, Almasy L, Dyer TD, Maccluer JW, Moses EK, Abboud HE, Mahaney MC, Blangero J, Comuzzie AG. Genome-wide association analysis confirms and extends the association of SLC2A9 with serum uric acid levels to Mexican Americans. Front Genet. 2013 Dec 16;4:279. doi: 10.3389/fgene.2013.00279. eCollection 2013. PMID: 24379826; PMCID: PMC3863993.
Copy Download .nbib Format: NLM
Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3.

Comparative biochemistry and physiology. Part D, Genomics & proteomics

Holmes RS, Cox LA, Vandeberg JL.
PMID: 20403742
Comp Biochem Physiol Part D Genomics Proteomics. 2009 Mar;4(1):54-65. doi: 10.1016/j.cbd.2008.10.004. Epub 2008 Nov 05.

Carboxylesterases (CES) are responsible for the detoxification of a wide range of drugs and xenobiotics, and may contribute to cholesterol, fatty acid and lung surfactant metabolism. In this study, in silico methods were used to predict the amino acid...

Cite
Holmes RS, Cox LA, Vandeberg JL. Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3. Comp Biochem Physiol Part D Genomics Proteomics. 2008;4(1):54-65doi: 10.1016/j.cbd.2008.10.004.
Holmes, R. S., Cox, L. A., & Vandeberg, J. L. (2009). Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3. Comparative biochemistry and physiology. Part D, Genomics & proteomics, 4(1), 54-65. https://doi.org/10.1016/j.cbd.2008.10.004
Holmes, Roger S, et al. "Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3." Comparative biochemistry and physiology. Part D, Genomics & proteomics vol. 4,1 (2009): 54-65. doi: https://doi.org/10.1016/j.cbd.2008.10.004
Holmes RS, Cox LA, Vandeberg JL. Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3. Comp Biochem Physiol Part D Genomics Proteomics. 2009 Mar;4(1):54-65. doi: 10.1016/j.cbd.2008.10.004. Epub 2008 Nov 05. PMID: 20403742; PMCID: PMC2916739.
Copy Download .nbib Format: NLM
Genomics and proteomics of vertebrate cholesterol ester lipase (LIPA) and cholesterol 25-hydroxylase (CH25H).

3 Biotech

Holmes RS, Vandeberg JL, Cox LA.
PMID: 22582164
3 Biotech. 2011 Sep;1(2):99-109. doi: 10.1007/s13205-011-0013-9. Epub 2011 Aug 03.

Cholesterol ester lipase (LIPA; EC 3.1.1.13) and cholesterol 25-hydroxylase (CH25H; EC 1.14.99.48) play essential role in cholesterol metabolism in the body by hydrolysing cholesteryl esters and triglycerides within lysosomes (LIPA) and catalysing the formation of 25-hydroxycholesterol from cholesterol (CH25H)...

Cite
Holmes RS, Vandeberg JL, Cox LA. Genomics and proteomics of vertebrate cholesterol ester lipase (LIPA) and cholesterol 25-hydroxylase (CH25H). 3 Biotech. 2011;1(2):99-109doi: 10.1007/s13205-011-0013-9.
Holmes, R. S., Vandeberg, J. L., & Cox, L. A. (2011). Genomics and proteomics of vertebrate cholesterol ester lipase (LIPA) and cholesterol 25-hydroxylase (CH25H). 3 Biotech, 1(2), 99-109. https://doi.org/10.1007/s13205-011-0013-9
Holmes, Roger S, et al. "Genomics and proteomics of vertebrate cholesterol ester lipase (LIPA) and cholesterol 25-hydroxylase (CH25H)." 3 Biotech vol. 1,2 (2011): 99-109. doi: https://doi.org/10.1007/s13205-011-0013-9
Holmes RS, Vandeberg JL, Cox LA. Genomics and proteomics of vertebrate cholesterol ester lipase (LIPA) and cholesterol 25-hydroxylase (CH25H). 3 Biotech. 2011 Sep;1(2):99-109. doi: 10.1007/s13205-011-0013-9. Epub 2011 Aug 03. PMID: 22582164; PMCID: PMC3324826.
Copy Download .nbib Format: NLM
A new class of mammalian carboxylesterase CES6.

Comparative biochemistry and physiology. Part D, Genomics & proteomics

Holmes RS, Cox LA, Vandeberg JL.
PMID: 20161041
Comp Biochem Physiol Part D Genomics Proteomics. 2009 Sep;4(3):209-17. doi: 10.1016/j.cbd.2009.03.002.

Mammalian carboxylesterases (CES) exhibit broad substrate specificities, catalyse hydrolytic and transesterification reactions with a wide range of drugs and xenobiotics and are widely distributed in the body. Four CES classes have been previously described, namely CES1 (major liver form);...

Cite
Holmes RS, Cox LA, Vandeberg JL. A new class of mammalian carboxylesterase CES6. Comp Biochem Physiol Part D Genomics Proteomics. 2009;4(3):209-17doi: 10.1016/j.cbd.2009.03.002.
Holmes, R. S., Cox, L. A., & Vandeberg, J. L. (2009). A new class of mammalian carboxylesterase CES6. Comparative biochemistry and physiology. Part D, Genomics & proteomics, 4(3), 209-17. https://doi.org/10.1016/j.cbd.2009.03.002
Holmes, Roger S, et al. "A new class of mammalian carboxylesterase CES6." Comparative biochemistry and physiology. Part D, Genomics & proteomics vol. 4,3 (2009): 209-17. doi: https://doi.org/10.1016/j.cbd.2009.03.002
Holmes RS, Cox LA, Vandeberg JL. A new class of mammalian carboxylesterase CES6. Comp Biochem Physiol Part D Genomics Proteomics. 2009 Sep;4(3):209-17. doi: 10.1016/j.cbd.2009.03.002. PMID: 20161041; PMCID: PMC2753981.
Copy Download .nbib Format: NLM
Mammalian Glutamyl Aminopeptidase Genes (ENPEP) and Proteins: Comparative Studies of a Major Contributor to Arterial Hypertension.

Journal of data mining in genomics & proteomics

Holmes RS, Spradling-Reeves KD, Cox LA.
PMID: 29900035
J Data Mining Genomics Proteomics. 2017;8(2). doi: 10.4172/2153-0602.1000211. Epub 2017 Jun 13.

Glutamyl aminopeptidase (ENPEP) is a member of the M1 family of endopeptidases which are mammalian type II integral membrane zinc-containing endopeptidases. ENPEP is involved in the catabolic pathway of the renin-angiotensin system forming angiotensin III, which participates in blood...

Cite
Holmes RS, Spradling-Reeves KD, Cox LA. Mammalian Glutamyl Aminopeptidase Genes (ENPEP) and Proteins: Comparative Studies of a Major Contributor to Arterial Hypertension. J Data Mining Genomics Proteomics. 2017;8(2)doi: 10.4172/2153-0602.1000211.
Holmes, R. S., Spradling-Reeves, K. D., & Cox, L. A. (2017). Mammalian Glutamyl Aminopeptidase Genes (ENPEP) and Proteins: Comparative Studies of a Major Contributor to Arterial Hypertension. Journal of data mining in genomics & proteomics, 8(2), . https://doi.org/10.4172/2153-0602.1000211
Holmes, Roger S, et al. "Mammalian Glutamyl Aminopeptidase Genes (ENPEP) and Proteins: Comparative Studies of a Major Contributor to Arterial Hypertension." Journal of data mining in genomics & proteomics vol. 8,2 (2017). doi: https://doi.org/10.4172/2153-0602.1000211
Holmes RS, Spradling-Reeves KD, Cox LA. Mammalian Glutamyl Aminopeptidase Genes (ENPEP) and Proteins: Comparative Studies of a Major Contributor to Arterial Hypertension. J Data Mining Genomics Proteomics. 2017;8(2). doi: 10.4172/2153-0602.1000211. Epub 2017 Jun 13. PMID: 29900035; PMCID: PMC5995572.
Copy Download .nbib Format: NLM
Bovine Carboxylesterases: Evidence for Two CES1 and Five Families of CES Genes on Chromosome 18.

Comparative biochemistry and physiology. Part D, Genomics & proteomics

Holmes RS, Cox LA, Vandeberg JL.
PMID: 20161341
Comp Biochem Physiol Part D Genomics Proteomics. 2009 Mar 01;4(1):11-20. doi: 10.1016/j.cbd.2008.09.002.

Predicted bovine carboxylesterase (CES) protein and gene sequences were derived from bovine (Bos taurus) genomic sequence data. Two bovine CES1 genes (CES1.1 and CES1.2) were located on chromosome 18 encoding amino acid sequences that were 81% identical. Two forms...

Cite
Holmes RS, Cox LA, Vandeberg JL. Bovine Carboxylesterases: Evidence for Two CES1 and Five Families of CES Genes on Chromosome 18. Comp Biochem Physiol Part D Genomics Proteomics. 2009;4(1):11-20doi: 10.1016/j.cbd.2008.09.002.
Holmes, R. S., Cox, L. A., & Vandeberg, J. L. (2009). Bovine Carboxylesterases: Evidence for Two CES1 and Five Families of CES Genes on Chromosome 18. Comparative biochemistry and physiology. Part D, Genomics & proteomics, 4(1), 11-20. https://doi.org/10.1016/j.cbd.2008.09.002
Holmes, Roger S, et al. "Bovine Carboxylesterases: Evidence for Two CES1 and Five Families of CES Genes on Chromosome 18." Comparative biochemistry and physiology. Part D, Genomics & proteomics vol. 4,1 (2009): 11-20. doi: https://doi.org/10.1016/j.cbd.2008.09.002
Holmes RS, Cox LA, Vandeberg JL. Bovine Carboxylesterases: Evidence for Two CES1 and Five Families of CES Genes on Chromosome 18. Comp Biochem Physiol Part D Genomics Proteomics. 2009 Mar 01;4(1):11-20. doi: 10.1016/j.cbd.2008.09.002. PMID: 20161341; PMCID: PMC2680296.
Copy Download .nbib Format: NLM
A quantitative trait locus on chromosome 5p influences d-dimer levels in the san antonio family heart study.

International journal of vascular medicine

Diego VP, Almasy L, Rainwater DL, Mahaney MC, Comuzzie AG, Cole SA, Tracy RP, Stern MP, Maccluer JW, Blangero J.
PMID: 21151504
Int J Vasc Med. 2010;2010:490241. doi: 10.1155/2010/490241. Epub 2010 Jun 27.

Background. D-dimer is associated with increasing severity of atherosclerosis and with increased risk of a cardiovascular disease (CVD). Methods and Results. To better understand this risk factor, we performed a genome scan on 803 (301 males and 502 females)...

Cite
Diego VP, Almasy L, Rainwater DL, et al. A quantitative trait locus on chromosome 5p influences d-dimer levels in the san antonio family heart study. Int J Vasc Med. 2010;2010:490241doi: 10.1155/2010/490241.
Diego, V. P., Almasy, L., Rainwater, D. L., Mahaney, M. C., Comuzzie, A. G., Cole, S. A., Tracy, R. P., Stern, M. P., Maccluer, J. W., & Blangero, J. (2010). A quantitative trait locus on chromosome 5p influences d-dimer levels in the san antonio family heart study. International journal of vascular medicine, 2010490241. https://doi.org/10.1155/2010/490241
Diego, V P, et al. "A quantitative trait locus on chromosome 5p influences d-dimer levels in the san antonio family heart study." International journal of vascular medicine vol. 2010 (2010): 490241. doi: https://doi.org/10.1155/2010/490241
Diego VP, Almasy L, Rainwater DL, Mahaney MC, Comuzzie AG, Cole SA, Tracy RP, Stern MP, Maccluer JW, Blangero J. A quantitative trait locus on chromosome 5p influences d-dimer levels in the san antonio family heart study. Int J Vasc Med. 2010;2010:490241. doi: 10.1155/2010/490241. Epub 2010 Jun 27. PMID: 21151504; PMCID: PMC2989697.
Copy Download .nbib Format: NLM
Mammalian carboxylesterase 5: comparative biochemistry and genomics.

Comparative biochemistry and physiology. Part D, Genomics & proteomics

Holmes RS, Cox LA, Vandeberg JL.
PMID: 19727319
Comp Biochem Physiol Part D Genomics Proteomics. 2008 Sep;3(3):195-204. doi: 10.1016/j.cbd.2008.05.002.

Carboxylesterase 5 (CES5) (also called cauxin or CES7) is one of at least five mammalian CES gene families encoding enzymes of broad substrate specificity and catalysing hydrolytic and transesterification reactions. In silico methods were used to predict the amino...

Cite
Holmes RS, Cox LA, Vandeberg JL. Mammalian carboxylesterase 5: comparative biochemistry and genomics. Comp Biochem Physiol Part D Genomics Proteomics. 2008;3(3):195-204doi: 10.1016/j.cbd.2008.05.002.
Holmes, R. S., Cox, L. A., & Vandeberg, J. L. (2008). Mammalian carboxylesterase 5: comparative biochemistry and genomics. Comparative biochemistry and physiology. Part D, Genomics & proteomics, 3(3), 195-204. https://doi.org/10.1016/j.cbd.2008.05.002
Holmes, Roger S, et al. "Mammalian carboxylesterase 5: comparative biochemistry and genomics." Comparative biochemistry and physiology. Part D, Genomics & proteomics vol. 3,3 (2008): 195-204. doi: https://doi.org/10.1016/j.cbd.2008.05.002
Holmes RS, Cox LA, Vandeberg JL. Mammalian carboxylesterase 5: comparative biochemistry and genomics. Comp Biochem Physiol Part D Genomics Proteomics. 2008 Sep;3(3):195-204. doi: 10.1016/j.cbd.2008.05.002. PMID: 19727319; PMCID: PMC2583452.
Copy Download .nbib Format: NLM
Variants in CPT1A, FADS1, and FADS2 are Associated with Higher Levels of Estimated Plasma and Erythrocyte Delta-5 Desaturases in Alaskan Eskimos.

Frontiers in genetics

Voruganti VS, Higgins PB, Ebbesson SO, Kennish J, Göring HH, Haack K, Laston S, Drigalenko E, Wenger CR, Harris WS, Fabsitz RR, Devereux RB, Maccluer JW, Curran JE, Carless MA, Johnson MP, Moses EK, Blangero J, Umans JG, Howard BV, Cole SA, Comuzzie AG.
PMID: 22701466
Front Genet. 2012 Jun 11;3:86. doi: 10.3389/fgene.2012.00086. eCollection 2012.

The delta-5 and delta-6 desaturases (D5D and D6D), encoded by fatty acid desaturase 1 (FADS1) and 2 (FADS2) genes, respectively, are rate-limiting enzymes in the metabolism of ω-3 and ω-6 fatty acids. The objective of this study was to...

Cite
Voruganti VS, Higgins PB, Ebbesson SO, et al. Variants in CPT1A, FADS1, and FADS2 are Associated with Higher Levels of Estimated Plasma and Erythrocyte Delta-5 Desaturases in Alaskan Eskimos. Front Genet. 2012;3:86doi: 10.3389/fgene.2012.00086.
Voruganti, V. S., Higgins, P. B., Ebbesson, S. O., Kennish, J., Göring, H. H., Haack, K., Laston, S., Drigalenko, E., Wenger, C. R., Harris, W. S., Fabsitz, R. R., Devereux, R. B., Maccluer, J. W., Curran, J. E., Carless, M. A., Johnson, M. P., Moses, E. K., Blangero, J., Umans, J. G., Howard, B. V., Cole, S. A., & Comuzzie, A. G. (2012). Variants in CPT1A, FADS1, and FADS2 are Associated with Higher Levels of Estimated Plasma and Erythrocyte Delta-5 Desaturases in Alaskan Eskimos. Frontiers in genetics, 386. https://doi.org/10.3389/fgene.2012.00086
Voruganti, V Saroja, et al. "Variants in CPT1A, FADS1, and FADS2 are Associated with Higher Levels of Estimated Plasma and Erythrocyte Delta-5 Desaturases in Alaskan Eskimos." Frontiers in genetics vol. 3 (2012): 86. doi: https://doi.org/10.3389/fgene.2012.00086
Voruganti VS, Higgins PB, Ebbesson SO, Kennish J, Göring HH, Haack K, Laston S, Drigalenko E, Wenger CR, Harris WS, Fabsitz RR, Devereux RB, Maccluer JW, Curran JE, Carless MA, Johnson MP, Moses EK, Blangero J, Umans JG, Howard BV, Cole SA, Comuzzie AG. Variants in CPT1A, FADS1, and FADS2 are Associated with Higher Levels of Estimated Plasma and Erythrocyte Delta-5 Desaturases in Alaskan Eskimos. Front Genet. 2012 Jun 11;3:86. doi: 10.3389/fgene.2012.00086. eCollection 2012. PMID: 22701466; PMCID: PMC3371589.
Copy Download .nbib Format: NLM
Novel associations of nonstructural Loci with paraoxonase activity.

Journal of lipids

Quillen EE, Rainwater DL, Dyer TD, Carless MA, Curran JE, Johnson MP, Göring HH, Cole SA, Rutherford S, Maccluer JW, Moses EK, Blangero J, Almasy L, Mahaney MC.
PMID: 22577559
J Lipids. 2012;2012:189681. doi: 10.1155/2012/189681. Epub 2012 Apr 17.

The high-density-lipoprotein-(HDL-) associated esterase paraoxonase 1 (PON1) is a likely contributor to the antioxidant and antiatherosclerotic capabilities of HDL. Two nonsynonymous mutations in the structural gene, PON1, have been associated with variation in activity levels, but substantial interindividual differences...

Cite
Quillen EE, Rainwater DL, Dyer TD, et al. Novel associations of nonstructural Loci with paraoxonase activity. J Lipids. 2012;2012:189681doi: 10.1155/2012/189681.
Quillen, E. E., Rainwater, D. L., Dyer, T. D., Carless, M. A., Curran, J. E., Johnson, M. P., Göring, H. H., Cole, S. A., Rutherford, S., Maccluer, J. W., Moses, E. K., Blangero, J., Almasy, L., & Mahaney, M. C. (2012). Novel associations of nonstructural Loci with paraoxonase activity. Journal of lipids, 2012189681. https://doi.org/10.1155/2012/189681
Quillen, Ellen E, et al. "Novel associations of nonstructural Loci with paraoxonase activity." Journal of lipids vol. 2012 (2012): 189681. doi: https://doi.org/10.1155/2012/189681
Quillen EE, Rainwater DL, Dyer TD, Carless MA, Curran JE, Johnson MP, Göring HH, Cole SA, Rutherford S, Maccluer JW, Moses EK, Blangero J, Almasy L, Mahaney MC. Novel associations of nonstructural Loci with paraoxonase activity. J Lipids. 2012;2012:189681. doi: 10.1155/2012/189681. Epub 2012 Apr 17. PMID: 22577559; PMCID: PMC3345224.
Copy Download .nbib Format: NLM
Comparative Structures and Evolution of Vertebrate Carboxyl Ester Lipase (CEL) Genes and Proteins with a Major Role in Reverse Cholesterol Transport.

Cholesterol

Holmes RS, Cox LA.
PMID: 22162806
Cholesterol. 2011;2011:781643. doi: 10.1155/2011/781643. Epub 2011 Nov 21.

Bile-salt activated carboxylic ester lipase (CEL) is a major triglyceride, cholesterol ester and vitamin ester hydrolytic enzyme contained within pancreatic and lactating mammary gland secretions. Bioinformatic methods were used to predict the amino acid sequences, secondary and tertiary structures...

Cite
Holmes RS, Cox LA. Comparative Structures and Evolution of Vertebrate Carboxyl Ester Lipase (CEL) Genes and Proteins with a Major Role in Reverse Cholesterol Transport. Cholesterol. 2011;2011:781643doi: 10.1155/2011/781643.
Holmes, R. S., & Cox, L. A. (2011). Comparative Structures and Evolution of Vertebrate Carboxyl Ester Lipase (CEL) Genes and Proteins with a Major Role in Reverse Cholesterol Transport. Cholesterol, 2011781643. https://doi.org/10.1155/2011/781643
Holmes, Roger S, and Cox, Laura A. "Comparative Structures and Evolution of Vertebrate Carboxyl Ester Lipase (CEL) Genes and Proteins with a Major Role in Reverse Cholesterol Transport." Cholesterol vol. 2011 (2011): 781643. doi: https://doi.org/10.1155/2011/781643
Holmes RS, Cox LA. Comparative Structures and Evolution of Vertebrate Carboxyl Ester Lipase (CEL) Genes and Proteins with a Major Role in Reverse Cholesterol Transport. Cholesterol. 2011;2011:781643. doi: 10.1155/2011/781643. Epub 2011 Nov 21. PMID: 22162806; PMCID: PMC3227413.
Copy Download .nbib Format: NLM
Comparative studies of glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1: evidence for a eutherian mammalian origin for the GPIHBP1 gene from an LY6-like gene.

3 Biotech

Holmes RS, Cox LA.
PMID: 22582156
3 Biotech. 2012 Mar;2(1):37-52. doi: 10.1007/s13205-011-0026-4. Epub 2011 Oct 18.

Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) functions as a platform and transport agent for lipoprotein lipase (LPL) which functions in the hydrolysis of chylomicrons, principally in heart, skeletal muscle and adipose tissue capillary endothelial cells. Previous reports of genetic...

Cite
Holmes RS, Cox LA. Comparative studies of glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1: evidence for a eutherian mammalian origin for the GPIHBP1 gene from an LY6-like gene. 3 Biotech. 2011;2(1):37-52doi: 10.1007/s13205-011-0026-4.
Holmes, R. S., & Cox, L. A. (2012). Comparative studies of glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1: evidence for a eutherian mammalian origin for the GPIHBP1 gene from an LY6-like gene. 3 Biotech, 2(1), 37-52. https://doi.org/10.1007/s13205-011-0026-4
Holmes, Roger S, and Cox, Laura A. "Comparative studies of glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1: evidence for a eutherian mammalian origin for the GPIHBP1 gene from an LY6-like gene." 3 Biotech vol. 2,1 (2012): 37-52. doi: https://doi.org/10.1007/s13205-011-0026-4
Holmes RS, Cox LA. Comparative studies of glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1: evidence for a eutherian mammalian origin for the GPIHBP1 gene from an LY6-like gene. 3 Biotech. 2012 Mar;2(1):37-52. doi: 10.1007/s13205-011-0026-4. Epub 2011 Oct 18. PMID: 22582156; PMCID: PMC3339605.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 13 entries