Jamey Marth

Last updated
Jamey Marth
Born
Sarasota, Florida
NationalityAmerican and Canadian
Alma mater University of Washington
Scientific career
Fields Molecular biology
Cellular biology
Inflammatory diseases
Immunology
Glycobiology
Institutions SBP Medical Discovery Institute
UC Santa Barbara
Howard Hughes Medical Institute
UC San Diego
Doctoral advisors Roger M. Perlmutter and Edwin G. Krebs

Jamey Marth is a molecular and cellular biologist. He is currently on the faculty of the SBP Medical Discovery Institute in La Jolla, California where he is Director of the Immunity and Pathogenesis program. [1]

Contents

His research has largely focused on how protein glycosylation contributes to the origins of common diseases and syndromes including diabetes, sepsis, colitis, and autoimmunity. [2] [3] [4] [5]

Education

Marth earned a Ph.D. in Pharmacology from the University of Washington in 1987. [1] [6] During his time at Washington as a graduate student, he was mentored by Roger M. Perlmutter and Edwin G. Krebs. [1] Marth was Perlmutter's first graduate student. [7]

Career

Following his time as a staff scientist at Oncogen Corporation in Seattle, Marth was recruited to the founding faculty of the Biomedical Research Centre in Vancouver, British Columbia, Canada, where he was also appointed as a professor in the Department of Medical Genetics at the University of British Columbia. [1] In 1995, George Palade and Marilyn Farquhar (among others) recruited Marth to the University of California, San Diego (UCSD) in the Department of Cellular and Molecular Medicine. [6] Upon his arrival, he was appointed as an Investigator of the Howard Hughes Medical Institute. [6] Marth spent more than 14 years in this position at UCSD. His research at HHMI and UCSD helped bolster an already renowned glycobiology program that originated with Ajit Varki and later included Jeffrey Esko. [8] [9]

In 2009, he accepted a position at the University of California, Santa Barbara (UCSB) and the Sanford-Burnham Medical Research Institute as the Director of the Center for Nanomedicine. [6] He also then became the inaugural recipient of the Carbon Chair in Biochemistry and Molecular Biology and the recipient of the Mellichamp Chair of Systems Biology. [5] [10]

Research

Marth's research is credited with the development of methodologies applicable to investigating the origins of disease. His conception and co-development of Cre-Lox conditional mutagenesis has provided a means to further perceive the mechanistic underpinnings of disease, and continues to be used by scientists worldwide. [11] [12] [13] [14] [15] Prior to the development of conditional mutagenesis, the use of homologous recombination was limited to systemic gene targeting and mutation. [16] Marth's use of Cre-Lox conditional mutagenesis established the presence and functions of multiple and in some cases previously unknown enzymes participating in protein glycosylation, an area of research that has become a focus of exploration of the genetic and metabolic origins of disease. [17] [18] Marth also used Cre-Lox mutagenesis to establish a reproducible method for obtaining animal models of essential X chromosome-linked genes. [19]

Marth's early studies of glycosylation and glycan linkages revealed a profound effect on immunity and contributed to the genesis of the related sub-field termed glycoimmunology. [17] [20] [21] Marth's laboratory discovered connections between aberrant glycan linkages and autoimmune diseases including the fact that the exposure of cryptic immature glycan linkages in mammals could initiate chronic sterile inflammation leading to the development of autoimmunity. [5] [18] Those findings indicated that autoimmunity can be precipitated by the presence of abnormal glycan structures within the body. [20] [22]

Marth's laboratory has also taken a close look at the molecular and cellular bases of Type 2 diabetes and the role that protein glycosylation plays in the origin of the disease. [23] [24] Their research demonstrated that acquired pancreatic beta cell dysfunction was the major contributor of disease onset and corroborated views that genetic variation was unlikely to be the primary cause of obesity-associated Type 2 diabetes in humans. [23] [25] Instead, their findings revealed that altered pancreatic beta cell glycosylation resulting from elevated fatty acid levels in obesity disabled glucose sensing, resulting in hyperglycemia with glucose intolerance. [2] [26] Marth's research team further found that this pathway was induced in human patients with Type 2 diabetes and was responsible for a significant amount of the insulin resistance present in experimentally-induced obesity-associated diabetes. [2] [27]

The pathological underpinnings of inflammatory diseases including sepsis have also been the subject of research by Marth's laboratory. [3] [5] [28] Marth and colleagues discovered the first physiological purpose of the Ashwell-Morell Receptor (AMR), a hepatocyte lectin discovered by Gilbert Ashwell and Anatol Morell. [18] [29] Marth's studies revealed the presence of an intrinsic mechanism of secreted protein aging and turnover first proposed by Ashwell and Morell in the 1960s, and which participates in controlling the half-lives and functions of secreted and cell surface glycoproteins. [18] [30] Their studies further identified how AMR function can be modulated for therapeutic purposes. [3]

In 2008, Marth published an initial enumeration of the building blocks of life, all of which fall under the four types of cellular macromolecules (glycans, lipids, nucleic acids, and proteins). [31] [32] This accounting has become an educational feature of cell biology texts. Marth and other colleagues have called attention to the fact that only half of these macromolecules are encoded by the genome, suggesting that a more holistic approach is needed in biomedical research to fully understand and intervene in the origins and progression of disease. [31] [33]

Selected publications

Related Research Articles

<span class="mw-page-title-main">Glycoprotein</span> Protein with oligosaccharide modifications

Glycoproteins are proteins which contain oligosaccharide chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated.

Defined in the narrowest sense, glycobiology is the study of the structure, biosynthesis, and biology of saccharides that are widely distributed in nature. Sugars or saccharides are essential components of all living things and aspects of the various roles they play in biology are researched in various medical, biochemical and biotechnological fields.

Glycosylation is the reaction in which a carbohydrate, i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule in order to form a glycoconjugate. In biology, glycosylation usually refers to an enzyme-catalysed reaction, whereas glycation may refer to a non-enzymatic reaction.

<span class="mw-page-title-main">Immunoglobulin D</span> Antibody isotype

Immunoglobulin D (IgD) is an antibody isotype that makes up about 1% of proteins in the plasma membranes of immature B-lymphocytes where it is usually co-expressed with another cell surface antibody called IgM. IgD is also produced in a secreted form that is found in very small amounts in blood serum, representing 0.25% of immunoglobulins in serum. The relative molecular mass and half-life of secreted IgD is 185 kDa and 2.8 days, respectively. Secreted IgD is produced as a monomeric antibody with two heavy chains of the delta (δ) class, and two Ig light chains.

<i>Vibrio vulnificus</i> Species of pathogenic bacterium found in water

Vibrio vulnificus is a species of Gram-negative, motile, curved rod-shaped (vibrio), pathogenic bacteria of the genus Vibrio. Present in marine environments such as estuaries, brackish ponds, or coastal areas, V. vulnificus is related to V. cholerae, the causative agent of cholera. At least one strain of V. vulnificus is bioluminescent. Increasing seasonal ocean temperatures and low-salt marine environments like estuaries favor a greater concentration of Vibrio within filter-feeding shellfish; V. vulnificus infections in the Eastern United States have increased eightfold from 1988–2018.

The terms glycans and polysaccharides are defined by IUPAC as synonyms meaning "compounds consisting of a large number of monosaccharides linked glycosidically". However, in practice the term glycan may also be used to refer to the carbohydrate portion of a glycoconjugate, such as a glycoprotein, glycolipid, or a proteoglycan, even if the carbohydrate is only an oligosaccharide. Glycans usually consist solely of O-glycosidic linkages of monosaccharides. For example, cellulose is a glycan composed of β-1,4-linked D-glucose, and chitin is a glycan composed of β-1,4-linked N-acetyl-D-glucosamine. Glycans can be homo- or heteropolymers of monosaccharide residues, and can be linear or branched.

Cre-Lox recombination is a site-specific recombinase technology, used to carry out deletions, insertions, translocations and inversions at specific sites in the DNA of cells. It allows the DNA modification to be targeted to a specific cell type or be triggered by a specific external stimulus. It is implemented both in eukaryotic and prokaryotic systems. The Cre-lox recombination system has been particularly useful to help neuroscientists to study the brain in which complex cell types and neural circuits come together to generate cognition and behaviors. NIH Blueprint for Neuroscience Research has created several hundreds of Cre driver mouse lines which are currently used by the worldwide neuroscience community.

Antigenic variation or antigenic alteration refers to the mechanism by which an infectious agent such as a protozoan, bacterium or virus alters the proteins or carbohydrates on its surface and thus avoids a host immune response, making it one of the mechanisms of antigenic escape. It is related to phase variation. Antigenic variation not only enables the pathogen to avoid the immune response in its current host, but also allows re-infection of previously infected hosts. Immunity to re-infection is based on recognition of the antigens carried by the pathogen, which are "remembered" by the acquired immune response. If the pathogen's dominant antigen can be altered, the pathogen can then evade the host's acquired immune system. Antigenic variation can occur by altering a variety of surface molecules including proteins and carbohydrates. Antigenic variation can result from gene conversion, site-specific DNA inversions, hypermutation, or recombination of sequence cassettes. The result is that even a clonal population of pathogens expresses a heterogeneous phenotype. Many of the proteins known to show antigenic or phase variation are related to virulence.

Siglecs(Sialic acid-binding immunoglobulin-type lectins) are cell surface proteins that bind sialic acid. They are found primarily on the surface of immune cells and are a subset of the I-type lectins. There are 14 different mammalian Siglecs, providing an array of different functions based on cell surface receptor-ligand interactions.

<span class="mw-page-title-main">Galectin</span> Protein family binding to β-galactoside sugars

Galectins are a class of proteins that bind specifically to β-galactoside sugars, such as N-acetyllactosamine, which can be bound to proteins by either N-linked or O-linked glycosylation. They are also termed S-type lectins due to their dependency on disulphide bonds for stability and carbohydrate binding. There have been about 15 galectins discovered in mammals, encoded by the LGALS genes, which are numbered in a consecutive manner. Only galectin-1, -2, -3, -4, -7, -7B, -8, -9, -9B, 9C, -10, -12, -13, -14, and -16 have been identified in humans. Galectin-5 and -6 are found in rodents, whereas galectin-11 and -15 are uniquely found in sheep and goats. Members of the galectin family have also been discovered in other mammals, birds, amphibians, fish, nematodes, sponges, and some fungi. Unlike the majority of lectins they are not membrane bound, but soluble proteins with both intra- and extracellular functions. They have distinct but overlapping distributions but found primarily in the cytosol, nucleus, extracellular matrix or in circulation. Although many galectins must be secreted, they do not have a typical signal peptide required for classical secretion. The mechanism and reason for this non-classical secretion pathway is unknown.

<span class="mw-page-title-main">Autoimmune disease</span> Disorders of adaptive immune system

An autoimmune disease is a condition that results from an anomalous response of the adaptive immune system, wherein it mistakenly targets and attacks healthy, functioning parts of the body as if they were foreign organisms. It is estimated that there are more than 80 recognized autoimmune diseases, with recent scientific evidence suggesting the existence of potentially more than 100 distinct conditions. Nearly any body part can be involved.

<i>N</i>-linked glycosylation Attachment of an oligosaccharide to a nitrogen atom

N-linked glycosylation, is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom, in a process called N-glycosylation, studied in biochemistry. The resulting protein is called an N-linked glycan, or simply an N-glycan.

O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O-glycosylation is a post-translational modification that occurs after the protein has been synthesised. In eukaryotes, it occurs in the endoplasmic reticulum, Golgi apparatus and occasionally in the cytoplasm; in prokaryotes, it occurs in the cytoplasm. Several different sugars can be added to the serine or threonine, and they affect the protein in different ways by changing protein stability and regulating protein activity. O-glycans, which are the sugars added to the serine or threonine, have numerous functions throughout the body, including trafficking of cells in the immune system, allowing recognition of foreign material, controlling cell metabolism and providing cartilage and tendon flexibility. Because of the many functions they have, changes in O-glycosylation are important in many diseases including cancer, diabetes and Alzheimer's. O-glycosylation occurs in all domains of life, including eukaryotes, archaea and a number of pathogenic bacteria including Burkholderia cenocepacia, Neisseria gonorrhoeae and Acinetobacter baumannii.

Phosphoglycosyl transferase C (PglC) is an enzyme belonging to a class known as monotopic phosphoglycosyl transferases (PGT). PGTs are required for the synthesis of glycoconjugates on the membrane surface of bacteria. Glycoconjugates, such as glycoproteins, are imperative for bacterial communication as well as host cell interactions between prokaryotic and eukaryotic cells lending to bacteria's pathogenicity.

<span class="mw-page-title-main">Variant surface glycoprotein</span>

Variant surface glycoprotein (VSG) is a ~60kDa protein which densely packs the cell surface of protozoan parasites belonging to the genus Trypanosoma. This genus is notable for their cell surface proteins. They were first isolated from Trypanosoma brucei in 1975 by George Cross. VSG allows the trypanosomatid parasites to evade the mammalian host's immune system by extensive antigenic variation. They form a 12–15 nm surface coat. VSG dimers make up ~90% of all cell surface protein and ~10% of total cell protein. For this reason, these proteins are highly immunogenic and an immune response raised against a specific VSG coat will rapidly kill trypanosomes expressing this variant. However, with each cell division there is a possibility that the progeny will switch expression to change the VSG that is being expressed. VSG has no prescribed biochemical activity.

<span class="mw-page-title-main">Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A</span> Protein-coding gene in the species Homo sapiens

Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A is a type II membrane protein and an enzyme – particularly a glycosyltransferase – that, in addition to the related isoenzyme B (MGAT4B), takes part in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans in Golgi apparatus. Therefore, it is essential for the formation of tri- and tetra-antennary sugar chains. Furthermore, it is involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation with controlling cell-surface expression of SLC2A2 in pancreatic beta cells and, as it is suggested, in regulating the availability of serum glycoproteins, oncogenesis, and differentiation.

Translational glycobiology or applied glycobiology is the branch of glycobiology and glycochemistry that focuses on developing new pharmaceuticals through glycomics and glycoengineering. Although research in this field presents many difficulties, translational glycobiology presents applications with therapeutic glycoconjugates, with treating various bone diseases, and developing therapeutic cancer vaccines and other targeted therapies. Some mechanisms of action include using the glycan for drug targeting, engineering protein glycosylation for better efficacy, and glycans as drugs themselves.

<span class="mw-page-title-main">Paucimannosylation</span> Protein Paucimannosylation

In biochemistry, paucimannosylation is an enzymatic post-translational modification involving the attachment of relatively simple mannose (Man) and N-Acetylglucosamine (GlcNAc) containing carbohydrates (glycans) to proteins. The paucimannosidic glycans may also be modified with other types of monosaccharides including fucose (Fuc) and xylose (Xyl) depending on the species, tissue and cell origin.

<span class="mw-page-title-main">Harry Schachter</span>

Harry Schachter FRSC is a Canadian biochemist and glycobiologist, and professor emeritus at the University of Toronto and the Hospital For Sick Children in Toronto, Canada.

<span class="mw-page-title-main">Glycan-protein interactions</span> Class of biological intermolecular interactions

Glycan-Protein interactions represent a class of biomolecular interactions that occur between free or protein-bound glycans and their cognate binding partners. Intramolecular glycan-protein (protein-glycan) interactions occur between glycans and proteins that they are covalently attached to. Together with protein-protein interactions, they form a mechanistic basis for many essential cell processes, especially for cell-cell interactions and host-cell interactions. For instance, SARS-CoV-2, the causative agent of COVID-19, employs its extensively glycosylated spike (S) protein to bind to the ACE2 receptor, allowing it to enter host cells. The spike protein is a trimeric structure, with each subunit containing 22 N-glycosylation sites, making it an attractive target for vaccine search.

References

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  2. 1 2 3 "Fatty diet triggers diabetes onslaught". Futurity. 2011-08-16. Retrieved 2021-07-14.
  3. 1 2 3 "Biomedical scientist discovers method to increase survival in sepsis". ScienceDaily. Retrieved 2021-07-14.
  4. ↑ Marth, Jamey David (2020). "Glycosylation in a Common Mechanism of Colitis and Sepsis". The FASEB Journal. 34 (S1): 1. doi: 10.1096/fasebj.2020.34.s1.00176 . ISSN   1530-6860. S2CID   218775798.
  5. 1 2 3 4 "Jamey Marth Honored for Research Linking Glycans to Diabetes, Lupus, Sepsis". www.newswise.com. Retrieved 2021-07-14.
  6. 1 2 3 4 "Jamey Marth - MCDB - UC Santa Barbara". 2021-04-18. Archived from the original on 2021-04-18. Retrieved 2021-07-14.
  7. ↑ "Notable Members" (PDF). 2016-01-02. Archived from the original (PDF) on 2016-01-02. Retrieved 2021-07-14.
  8. ↑ Haltiwanger, Robert S. (2000-12-01). "Essentials of Glycobiology. Ajit Varki , Richard Cummings , Jeffrey Esko , Hudson Freeze , Gerald Hart , Jamey Marth , Maarten Chrispeels , Ole Hindsgaul , James C. Paulson , John Lowe , Adriana Manzi , Leland Powell , Herman van Halbeek". The Quarterly Review of Biology. 75 (4): 451–452. doi:10.1086/393647. ISSN   0033-5770.
  9. ↑ "History - Glycobiology Research and Training Center, UC San Diego". UC San Diego Health Sciences. Retrieved 2021-07-14.
  10. ↑ "Faculty - Division of Mathematical Life and Physical Sciences - UC Santa Barbara". science.ucsb.edu. Retrieved 2021-07-14.
  11. ↑ "Floxed Mice - Cre-lox Recombination and Gene Targeting". www.genetargeting.com. 12 June 2019. Retrieved 2021-07-14.
  12. ↑ Marth, J. D. (1996-05-01). "Recent advances in gene mutagenesis by site-directed recombination". The Journal of Clinical Investigation. 97 (9): 1999–2002. doi:10.1172/JCI118634. PMC   507272 . PMID   8621787 . Retrieved 2021-07-14.
  13. ↑ Orban, P. C.; Chui, D.; Marth, J. D. (1992-08-01). "Tissue- and site-specific DNA recombination in transgenic mice". Proceedings of the National Academy of Sciences of the United States of America. 89 (15): 6861–6865. Bibcode:1992PNAS...89.6861O. doi: 10.1073/pnas.89.15.6861 . ISSN   0027-8424. PMC   49604 . PMID   1495975.
  14. ↑ Gu, H.; Marth, J. D.; Orban, P. C.; Mossmann, H.; Rajewsky, K. (1994-07-01). "Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting". Science. 265 (5168): 103–106. Bibcode:1994Sci...265..103G. doi:10.1126/science.8016642. ISSN   0036-8075. PMID   8016642.
  15. ↑ Hennet, T.; Hagen, F. K.; Tabak, L. A.; Marth, J. D. (1995-12-19). "T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl-transferase gene by site-directed recombination". Proceedings of the National Academy of Sciences of the United States of America. 92 (26): 12070–12074. Bibcode:1995PNAS...9212070H. doi: 10.1073/pnas.92.26.12070 . ISSN   0027-8424. PMC   40298 . PMID   8618846.
  16. ↑ Wadman, M. (1998-08-27). "DuPont opens up access to genetics tool". Nature. 394 (6696): 819. Bibcode:1998Natur.394..819W. doi: 10.1038/29607 . ISSN   0028-0836. PMID   9732857. S2CID   4431441.
  17. 1 2 News, Chemical & Engineering. "Chemical & Engineering News: Cover Story - Sugar Medicine". pubsapp.acs.org. Retrieved 2021-07-14.{{cite web}}: |last= has generic name (help)
  18. 1 2 3 4 Ohtsubo, Kazuaki; Marth, Jamey D. (2006-09-08). "Glycosylation in Cellular Mechanisms of Health and Disease". Cell. 126 (5): 855–867. doi: 10.1016/j.cell.2006.08.019 . ISSN   0092-8674. PMID   16959566. S2CID   9474696.
  19. ↑ Shafi, Raheel; Iyer, Sai Prasad N.; Ellies, Lesley G.; O'Donnell, Niall; Marek, Kurt W.; Chui, Daniel; Hart, Gerald W.; Marth, Jamey D. (2000-05-23). "The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny". Proceedings of the National Academy of Sciences of the United States of America. 97 (11): 5735–5739. Bibcode:2000PNAS...97.5735S. doi: 10.1073/pnas.100471497 . ISSN   0027-8424. PMC   18502 . PMID   10801981.
  20. 1 2 Marth, Jamey D.; Grewal, Prabhjit K. (2008). "Mammalian glycosylation in immunity". Nature Reviews Immunology. 8 (11): 874–887. doi:10.1038/nri2417. ISSN   1474-1741. PMC   2768770 . PMID   18846099.
  21. ↑ Baum, Linda G.; Crocker, Paul R. (2009). "Glycoimmunology: ignore at your peril". Immunological Reviews. 230 (1): 5–8. doi:10.1111/j.1600-065X.2009.00800.x. ISSN   1600-065X. PMID   19594625. S2CID   38067762.
  22. ↑ Green, Ryan S.; Stone, Erica L.; Tenno, Mari; Lehtonen, Eero; Farquhar, Marilyn G.; Marth, Jamey D. (2007-08-01). "Mammalian N-glycan branching protects against innate immune self-recognition and inflammation in autoimmune disease pathogenesis". Immunity. 27 (2): 308–320. doi: 10.1016/j.immuni.2007.06.008 . ISSN   1074-7613. PMID   17681821.
  23. 1 2 Ohtsubo, Kazuaki; Chen, Mark Z; Olefsky, Jerrold M; Marth, Jamey D (2011-08-14). "Pathway to diabetes through attenuation of pancreatic beta cell glycosylation and glucose transport". Nature Medicine. 17 (9): 1067–1075. doi:10.1038/nm.2414. ISSN   1078-8956. PMC   3888087 . PMID   21841783.
  24. ↑ "UCSD Team Discovers Diabetes Trigger in Fatty Diet". UC Health - UC San Diego. Retrieved 2021-07-14.
  25. ↑ "How Fat and Obesity Cause Diabetes". The UCSB Current. Retrieved 2021-07-14.
  26. ↑ "Pioneering research on type 2 diabetes - UC Health". 2019-03-02. Archived from the original on 2019-03-02. Retrieved 2021-07-14.
  27. ↑ "Fat 'disrupts sugar sensors causing type 2 diabetes'". BBC News. 2011-08-14. Retrieved 2021-07-14.
  28. ↑ Yang, Won Ho; Heithoff, Douglas M.; Aziz, Peter V.; Sperandio, Markus; Nizet, Victor; Mahan, Michael J.; Marth, Jamey D. (2017-12-22). "Recurrent Infection Progressively Disables Host Protection Against Intestinal Inflammation". Science. 358 (6370): eaao5610. doi:10.1126/science.aao5610. ISSN   0036-8075. PMC   5824721 . PMID   29269445.
  29. ↑ Grewal, Prabhjit K; Uchiyama, Satoshi; Ditto, David; Varki, Nissi; Le, Dzung T; Nizet, Victor; Marth, Jamey D (2008). "The Ashwell receptor mitigates the lethal coagulopathy of sepsis". Nature Medicine. 14 (6): 648–655. doi:10.1038/nm1760. ISSN   1078-8956. PMC   2853759 . PMID   18488037.
  30. ↑ Yang, Won Ho; Aziz, Peter V.; Heithoff, Douglas M.; Mahan, Michael J.; Smith, Jeffrey W.; Marth, Jamey D. (2015-11-03). "An intrinsic mechanism of secreted protein aging and turnover". Proceedings of the National Academy of Sciences of the United States of America. 112 (44): 13657–13662. Bibcode:2015PNAS..11213657Y. doi: 10.1073/pnas.1515464112 . ISSN   1091-6490. PMC   4640737 . PMID   26489654.
  31. 1 2 Marth, Jamey D. (2008). "A unified vision of the building blocks of life". Nature Cell Biology. 10 (9): 1015–1016. doi:10.1038/ncb0908-1015. ISSN   1476-4679. PMC   2892900 . PMID   18758488.
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