Advertisement
J. Lipid Res.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1194/jlr.E400002-JLR200 on August 1, 2004

This Article
Right arrow Abstract Freely available
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E400002-JLR200v1
45/10/1958    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mashek, D. G.
Right arrow Articles by Yamamoto, T. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mashek, D. G.
Right arrow Articles by Yamamoto, T. T.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Journal of Lipid Research, Vol. 45, 1958-1961, October 2004
Copyright © 2004 by American Society for Biochemistry and Molecular Biology


Report

Revised nomenclature for the mammalian long-chain acyl-CoA synthetase gene family

Douglas G. Mashek*, Karin E. Bornfeldt{dagger}, Rosalind A. Coleman1,*, Johannes Berger§, David A. Bernlohr**, Paul Black{dagger}{dagger}, Concetta C. DiRusso{dagger}{dagger}, Steven A. Farber§§, Wen Guo***, Naohiro Hashimoto{dagger}{dagger}{dagger}, Varsha Khodiyar§§§, Frans A. Kuypers****, Lois J. Maltais{dagger}{dagger}{dagger}{dagger}, Daniel W. Nebert§§§§, Alessandra Renieri*****, Jean E. Schaffer{dagger}{dagger}{dagger}{dagger}{dagger}, Andreas Stahl§§§§§, Paul A. Watkins******, Vasilis Vasiliou{dagger}{dagger}{dagger}{dagger}{dagger}{dagger} and Tokuo T. Yamamoto§§§§§§

* Departments of Nutrition and Pediatrics, University of North Carolina, Chapel Hill, NC 27599
{dagger} Department of Pathology, University of Washington, Seattle, WA 98195
§ Medical University of Vienna, Brain Research Institute, Neuroimmunology, A-1090 Vienna, Austria
** Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455
{dagger}{dagger} Ordway Research Institute, Inc., Albany, NY 12208
§§ Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA 19107
*** Department of Medicine, Boston University School of Medicine, Boston, MA 01228
{dagger}{dagger}{dagger} Tissue Stem Cell Research Team, Mitsubishi Kagaku Institute of Life Sciences, Machida, Tokyo 194-8511, Japan
§§§ The Human Genome Organization Gene Nomenclature Committee, Department of Biology, University College London, London NW1 2HE, UK
**** Children's Hospital Oakland Research Institute, Oakland, CA 94609
{dagger}{dagger}{dagger}{dagger} Mouse Genomic Nomenclature Committee, The Jackson Laboratory, Bar Harbor, ME 04609
§§§§ Department of Environmental Health and Center for Environmental Genetics, University of Cincinnati Medical Center, Cincinnati OH 45267-0056
***** Medical Genetics, University of Siena, Policlinico Le Scotte, 53100 Siena, Italy
{dagger}{dagger}{dagger}{dagger}{dagger} Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110
§§§§§ Research Institute, Palo Alto Medical Foundation, Palo Alto, CA 94301
****** Kennedy Krieger Institute, Baltimore, MD 21205
{dagger}{dagger}{dagger}{dagger}{dagger}{dagger} Molecular Toxicology and Environmental Health Sciences Program, Department of Pharmaceutical Sciences, University of Colorado Health Sciences Center, Denver, CO 809262
§§§§§§ Center for Advanced Genome Research, Institute of Development, Aging, and Cancer, Tohoku University, Sendai 981-8555, Japan

Published, JLR Papers in Press, August 1, 2004. DOI 10.1194/jlr.E400002-JLR200

1 To whom correspondence should be addressed. e-mail: rcoleman{at}unc.edu


ABSTRACT

By consensus, the acyl-CoA synthetase (ACS) community, with the advice of the human and mouse genome nomenclature committees, has revised the nomenclature for the mammalian long-chain acyl-CoA synthetases. ACS is the family root name, and the human and mouse genes for the long-chain ACSs are termed ACSL1,3–6 and Acsl1,3–6, respectively. Splice variants of ACSL3, -4, -5, and -6 are cataloged.

Suggestions for naming other family members and for the nonmammalian acyl-CoA synthetases are made.

Supplementary key words acyl-coenzyme A synthetase • fatty acid-coenzyme A ligase • coenzyme A synthetase • bubblegum • fatty acid transport protein • very long chain-acyl-CoA synthetase • long-chain acyl-coenzyme A synthetase • lipidosin • scFat2p

In mammals, long-chain acyl-CoA synthetase (ACSL) catalyzes the initial step in cellular long-chain fatty acid metabolism. In this reaction, ACSL ligates fatty acids to CoA in a two-step reaction (1, 2): 1) fatty acid + ATP -> fatty acyl-AMP + pyrophosphate; 2) fatty acyl-AMP + CoA -> fatty acyl-CoA + AMP. Since the cDNA encoding ACSL was cloned in 1990 (3), five isoforms of ACSL differing in their substrate preferences, enzyme kinetics, cellular and organelle locations, and regulation have been identified and characterized in rodents and humans. Although our knowledge of the ACSL family has advanced greatly in recent years, inconsistencies regarding ACSL nomenclature have led to confusion in the scientific literature. To alleviate the confusion regarding ACSL naming and numbering, a group of researchers studying the ACSL genes, in coordination with the human and mouse genome nomenclature committees (HGNC and MGNC), have revised the previous nomenclature system. The purpose of this report is to present the revised and approved nomenclature for the ACSL gene family in humans and rodents and to encourage scientists referencing ACSL to adhere to the new nomenclature.


NOMENCLATURE

The HGNC and MGNC have chosen ACS as the family root name: synthetase, rather than ligase or synthase, was selected for the activity and acyl-CoA for the product. Synthetase refers to a reaction that uses ATP and forms an acyl-AMP intermediate. Despite the fact that the best known substrates are fatty acids, the entire spectrum of natural and xenobiotic substrates used by ACSL and other ACS subfamilies is not fully known, but it certainly encompasses substrates that are not fatty acids. For example, xenobiotic carboxylic acids (4) and bile acids (5) are substrates. Thus, the use of acyl-CoA is preferred because it does not limit ACS substrates to fatty acids.

The ACS family includes enzymes that prefer short-, medium-, long-, or very long-chain fatty acids as substrates. Although related family members exhibit considerable overlap in their use of fatty acids of similar chain lengths, differences in the amino acid sequences of the AMP/ATP and fatty acid binding motifs distinguish subfamilies previously designated as acetyl-CoA synthetase, medium-chain acyl-CoA synthetase, long-chain acyl-CoA synthetase, very long-chain acyl-CoA synthetase, bubblegum (lipidosin), and scFat2p (6). Earlier studies used the term LACS (long-chain ACS) to distinguish ACS isoforms that act on long-chain fatty acids; however, the revised nomenclature recommends a hierarchical approach with ACS as the root symbol followed by a letter to specify the length of fatty acid acted upon. The HGNC and MGNC have approved the ACSL mammalian gene nomenclature.

As standard guidelines for human and rodent gene nomenclature, the human symbols are entirely capitalized (e.g., ACSS, ACSM, ACSL) and the rodent symbols are lowercase with the exception of the first letter (e.g., Acss, Acsm, Acsl) (7). The HGNC recommends that gene and allele symbols be italicized and protein symbols be represented in nonitalicized fonts. Italics need not be used in gene catalogs. Proteins are shown in uppercase letters. To distinguish between mRNA, genomic DNA, and cDNA, the relevant prefix should be written in parentheses: (mRNA) ACSL1, (gDNA) ACSL1, (cDNA) ACSL1.


ORTHOLOGY

Improper designation of ACSL1, the first cloned human ACSL family member, has caused considerable confusion. Although two separate genes were originally reported to encode FACL1 (fatty acid-CoA ligase) and FACL2 (8, 9), it was subsequently discovered that FACL1 and FACL2 are the same gene. Therefore, the revised nomenclature system now identifies FACL1/FACL2 as human ACSL1. As a consequence of the original human nomenclature, the previously reported FACL2 was not orthologous to rodent ACS2. To correct this problem, the former rodent ACS2 has been redesignated as Acsl6 because it shares highest sequence identity with human ACSL6 [originally characterized as LACS5 (10)], as shown in Table 1. Hence, according to the revised nomenclature system, there is no ACSL2 in humans or in rodents.


View this table:
[in this window]
[in a new window]
 
TABLE 1. Revised nomenclature for the long-chain acyl-CoA synthetase gene family

 

SPLICE VARIANTS

The ACSL3, ACSL4, ACSL5, and ACSL6 genes encode mRNAs and proteins that have splice variants. The human ACSL3 gene encodes two transcripts with varying 5' untranslated regions, ACSL3 variant 1 (ACSL3_v1) and ACSL3_v2 (Table 1). Both transcripts encode the same ACSL3 protein. Human ACSL3 is homologous to rat and mouse ACSL3. Likewise, human ACSL4 is homologous to rat and mouse ACSL4. In humans, two splice variants of ACSL4 have been demonstrated (11). Compared with ACSL4_v1, ACSL4_v2 contains an earlier in-frame start codon that encodes a hydrophobic N terminus that is 41 amino acids longer. Human ACSL5, which is homologous to rat and mouse ACSL5, has three splice variants. ACSL5_v1 encodes a protein with a 56 amino acid longer N terminus (ACSL5a) compared with the protein encoded by both ACSL5_v2 and ACSL5_v3, which encode the same shorter protein (ACSL5b). Splice variants of ACSL6 have been identified in humans and rodents (unpublished observations). The ACSL6_v1 and ACSL6_v2 transcripts of human ACSL6 differ in amino acid residues 306–331 because they are encoded by exon 14 and exon 13, respectively, as a result of alternative exon use.

The numerous examples of ACSL genes encoding multiple proteins having different N-terminal and/or internal regions suggest that additional splice variants will be identified. The HGNC recommends that new variants of ACSL1–6 or Acsl1–6 should be named splice variants of a gene (e.g., ACSL5_v4) if they use some of the same exons as an existing ACSL isoform (http://www.gene.ucl.ac.uk/nomenclature/guidelines.html). For genes with multiple promoters, the alternative promoters are designated by the addition of the lowercase letters "pr" (e.g., symbol: ACSL6_pr1; name: long-chain acyl-CoA synthetase 6, promoter 1). Proteins translated from mRNA splice variants may be distinguished by lowercase suffixes (e.g., ACSL5a and ACSL5b).


OTHER ACS FAMILY MEMBERS

It should be noted that proteins of the family previously named very long-chain ACS (VLCS) (6) are also known as fatty acid transport proteins (FATPs). These are included in the superfamily of proteins encoded by members of the solute carrier gene family, whose currently approved gene symbols are SLC27A1–6 (12). The VLCS/FATPs also have acyl-CoA synthetase enzymatic activity (1316). Thus, these proteins may play a dual role in the transport and esterification of their substrates.

Some amino acid sequences are shared between ACSL subfamily members and other enzymes, such as acetyl-CoA synthetase, bubblegum, and scFat2p, and related proteins (6). As yet, a standardized nomenclature has not been formulated for these other enzymes or for the yeast and bacterial ACS families. Each member of the extended ACS family has the ATP/AMP binding motif that is a hallmark of adenylate-forming enzymes as well as a fatty acid binding motif defined in the bacterial homolog FadD (17).


CONCLUSIONS

Previous publications have used a multitude of names for members of the ACSL family, which has led to confusion among investigators. Implementation of the revised nomenclature proposed here for the mammalian ACSL gene family will reduce disparities and render our literature more accessible to us as well as to those outside the field.

The use of ACSS and ACSM root symbols for the acetyl-CoA and medium-chain acyl-CoA synthetases, respectively, should also be considered. The VLCS/FATP/SLC27A1–6 and the bubblegum/lipidosin subfamily members use as substrates long-chain and very long-chain fatty acids and/or bile acids; thus, it is not yet clear what prefix should be used to designate these enzymes. Further consultation is needed among scientists who study these proteins. We propose that those working on ACS genes in other organisms also consider adopting a similar nomenclature.


ACKNOWLEDGMENTS

This project was supported in part by the Austrian Science Foundation FWF P14163-MOB (J.B.); the National Institutes of Health: DK-53189 (D.A.B.), HL-076719 (K.E.B.), GM-56850 (P.N.B), DK-59935 (R.A.C.), DK-60369 (S.A.F.), P30 HG-00330 (L.J.M.), P30 ES-06096 (D.W.N.), DK-066336 and DK-56339 (A.S.), EY-11490 (V.V.), and NS-37351 (P.A.W.); and the American Heart Association: North East Affiliate 0151215T (C.C.DR) and 0265311Y (A.S). The work of the Human Genome Nomenclature Committee is supported by National Institutes of Health contract N01-LM-9-3533, the UK Medical Research Council, and the Wellcome Trust.

Manuscript received June 25, 2004 and in revised form July 15, 2004.


REFERENCES

  1. Cleland, W. W. 1963. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim. Biophys. Acta. 67: 104–137.[Medline]

  2. Bar-Tana, J., G. Rose, R. Brandes, and B. Shapiro. 1973. Palmitoyl-coenzyme A synthetase. Mechanism of reaction. Biochem. J. 131: 199–209.[Medline]

  3. Suzuki, H., Y. Kawarabayasi, J. Kondo, T. Abe, K. Nishikawa, S. Kimura, T. Hashimoto, and T. Yamamoto. 1990. Structure and regulation of rat long-chain acyl-CoA synthetase. J. Biol. Chem. 265: 8681–8685.[Abstract/Free Full Text]

  4. Brugger, R., C. Reichel, B. G. Alia, K. Brune, T. Yamamoto, I. Tegeder, and G. Geisslinger. 2001. Expression of rat liver long-chain acyl-CoA synthetase and characterization of its role in the metabolism of R-ibuprofen and other fatty acid-like xenobiotics. Biochem. Pharmacol. 61: 651–656.[CrossRef][Medline]

  5. Steinberg, S. J., S. J. Mihalik, D. G. Kim, D. A. Cuebas, and P. A. Watkins. 2000. The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase. J. Biol. Chem. 275: 15605–15608.[Abstract/Free Full Text]

  6. Steinberg, S. J., J. Morgenthaler, A. K. Heinzer, K. D. Smith, and P. A. Watkins. 2000. Very long-chain acyl-CoA synthetases: human "bubblegum" represents a new family of proteins capable of activating very long-chain fatty acids. J. Biol. Chem. 275: 35162–35169.[Abstract/Free Full Text]

  7. Wain, H. M., E. A. Bruford, R. C. Lovering, M. J. Lush, M. W. Wright, and S. Povey. 2002. Guidelines for human gene nomenclature. Genomics. 79: 464–470.[CrossRef][Medline]

  8. Abe, T., T. Fujino, R. Fukuyama, S. Minoshima, N. Shimzu, H. Toh, H. Suzuki, and T. Yamamoto. 1992. Human long-chain acyl-CoA synthetase: structure and chromosomal location. J. Biochem. 111: 123–128.[Abstract/Free Full Text]

  9. Ghosh, B., E. Barbosa, and I. Singh. 1995. Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression. Mol. Cell. Biochem. 151: 77–78.[CrossRef][Medline]

  10. Malhotra, K. T., K. Malhotra, B. H. Lubin, and F. A. Kuypers. 1999. Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem. J. 344: 135–143.

  11. Meloni, I., M. Muscettola, M. Raynaud, I. Longo, M. Bruttini, M. P. Moizard, M. Gomot, J. Chelly, V. des Portes, J. P. Fryns, H. H. Ropers, B. Magi, C. Bellan, N. Volpi, H. G. Yntema, S. E. Lewis, J. E. Schaffer, and A. Renieri. 2002. FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation. Nat. Genet. 30: 436–440.[CrossRef][Medline]

  12. Stahl, A. 2004. A current review of fatty acid transport proteins (SLC27). Pflugers Arch. 447: 722–727.[CrossRef][Medline]

  13. Herrmann, T., F. Buchkremer, I. Gosch, A. M. Hall, D. A. Bernlohr, and W. Stremmel. 2001. Mouse fatty acid transport protein 4 (FATP4): Characterization of the gene and functional assessment as a very long chain acyl-CoA synthetase. Gene. 270: 31–40.[CrossRef][Medline]

  14. Coe, N. R., A. J. Smith, B. I. Frohnert, P. A. Watkins, and D. A. Bernlohr. 1999. The fatty acid transport protein (FATP1) is a very long chain acyl-CoA synthetase. J. Biol. Chem. 274: 36300–36304.[Abstract/Free Full Text]

  15. Zou, Z., C. C. DiRusso, V. Ctrnacta, and P. N. Black. 2002. Fatty acid transport in Saccharomyces cerevisiae. Directed mutagenesis of FAT1 distinguishes the biochemical activities associated with Fat1p. J. Biol. Chem. 277: 31062–31071.[Abstract/Free Full Text]

  16. Hall, A. M., A. J. Smith, and D. A. Bernlohr. 2003. Characterization of the acyl CoA synthetase activity of purified murine fatty acid transport protein 1. J. Biol. Chem. 278: 43008–43013.[Abstract/Free Full Text]

  17. Black, P. N., Q. Zhang, J. D. Weimar, and C. C. DiRusso. 1997. Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity. J. Biol. Chem. 272: 4896–4903.[Abstract/Free Full Text]


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Exp. Biol. Med.Home page
E. Soupene and F. A. Kuypers
Mammalian Long-Chain Acyl-CoA Synthetases
Experimental Biology and Medicine, May 1, 2008; 233(5): 507 - 521.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
P. A. Watkins, D. Maiguel, Z. Jia, and J. Pevsner
Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome
J. Lipid Res., December 1, 2007; 48(12): 2736 - 2750.
[Abstract] [Full Text] [PDF]


Home page
Arterioscler. Thromb. Vasc. Bio.Home page
Y. Zhou, P. Abidi, A. Kim, W. Chen, T.-T. Huang, F. B. Kraemer, and J. Liu
Transcriptional Activation of Hepatic ACSL3 and ACSL5 by Oncostatin M Reduces Hypertriglyceridemia Through Enhanced {beta}-Oxidation
Arterioscler. Thromb. Vasc. Biol., October 1, 2007; 27(10): 2198 - 2205.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
Y. Fujimoto, H. Itabe, T. Kinoshita, K. J. Homma, J. Onoduka, M. Mori, S. Yamaguchi, M. Makita, Y. Higashi, A. Yamashita, et al.
Involvement of ACSL in local synthesis of neutral lipids in cytoplasmic lipid droplets in human hepatocyte HuH7
J. Lipid Res., June 1, 2007; 48(6): 1280 - 1292.
[Abstract] [Full Text] [PDF]


Home page
DiabetesHome page
B. Askari, J. E. Kanter, A. M. Sherrid, D. L. Golej, A. T. Bender, J. Liu, W. A. Hsueh, J. A. Beavo, R. A. Coleman, and K. E. Bornfeldt
Rosiglitazone Inhibits Acyl-CoA Synthetase Activity and Fatty Acid Partitioning to Diacylglycerol and Triacylglycerol via a Peroxisome Proliferator-Activated Receptor-{gamma}-Independent Mechanism in Human Arterial Smooth Muscle Cells and Macrophages
Diabetes, April 1, 2007; 56(4): 1143 - 1152.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
L. O. Li, D. G. Mashek, J. An, S. D. Doughman, C. B. Newgard, and R. A. Coleman
Overexpression of Rat Long Chain Acyl-CoA Synthetase 1 Alters Fatty Acid Metabolism in Rat Primary Hepatocytes
J. Biol. Chem., December 1, 2006; 281(48): 37246 - 37255.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
D. G. Mashek, L. O. Li, and R. A. Coleman
Rat long-chain acyl-CoA synthetase mRNA, protein, and activity vary in tissue distribution and in response to diet
J. Lipid Res., September 1, 2006; 47(9): 2004 - 2010.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Z. Pei, Z. Jia, and P. A. Watkins
The Second Member of the Human and Murine "Bubblegum" Family Is a Testis- and Brainstem-specific Acyl-CoA Synthetase
J. Biol. Chem., March 10, 2006; 281(10): 6632 - 6641.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. G. Mashek, M. A. McKenzie, C. G. Van Horn, and R. A. Coleman
Rat Long Chain Acyl-CoA Synthetase 5 Increases Fatty Acid Uptake and Partitioning to Cellular Triacylglycerol in McArdle-RH7777 Cells
J. Biol. Chem., January 13, 2006; 281(2): 945 - 950.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
M. C. Hunt, J. Yamada, L. J. Maltais, M. W. Wright, E. J. Podesta, and S. E. H. Alexson
A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases
J. Lipid Res., September 1, 2005; 46(9): 2029 - 2032.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
T. Tonon, R. Qing, D. Harvey, Y. Li, T. R. Larson, and I. A. Graham
Identification of a Long-Chain Polyunsaturated Fatty Acid Acyl-Coenzyme A Synthetase from the Diatom Thalassiosira pseudonana
Plant Physiology, May 1, 2005; 138(1): 402 - 408.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
J. T. Eppig, C. J. Bult, J. A. Kadin, J. E. Richardson, J. A. Blake, and the Mouse Genome Database Group
The Mouse Genome Database (MGD): from genes to mice--a community resource for mouse biology
Nucleic Acids Res., January 1, 2005; 33(suppl_1): D471 - D475.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Z. Pei, P. Fraisl, J. Berger, Z. Jia, S. Forss-Petter, and P. A. Watkins
Mouse Very Long-chain Acyl-CoA Synthetase 3/Fatty Acid Transport Protein 3 Catalyzes Fatty Acid Activation but Not Fatty Acid Transport in MA-10 Cells
J. Biol. Chem., December 24, 2004; 279(52): 54454 - 54462.
[Abstract] [Full Text] [PDF]


This Article
Right arrow Abstract Freely available
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E400002-JLR200v1
45/10/1958    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mashek, D. G.
Right arrow Articles by Yamamoto, T. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mashek, D. G.
Right arrow Articles by Yamamoto, T. T.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Advertisement
spacer
Advertisement
Advertisement