Pierre De Meyts

Last updated

Pierre De Meyts
Pierre De Meyts (caricature by Jens Hage).jpg
Born1944 (age 79–80)
Verviers, Belgium
EducationUniversity of Liège
Known forDiabetogenes
Awards Christophe Plantin Prize, Belgium
Scientific career
FieldsHormone-receptor interaction of peptide hormones, physiopathogenesis of diabetes
InstitutionsHôpital de Bavière; Vrije Universiteit Brussel, Université catholique de Louvain; Beckman Research Institute, California; Hagedorn Research Institute, Copenhagen; University of Copenhagen

Pierre De Meyts (born 1944) is a Belgian physician and biochemist known for his research on fine chemical and kinetic aspects of ligand-receptor interaction, subunit assembly, and specific metabolic (as well as mitogenic) effects of hormones typically causing receptor tyrosine kinase activation such as insulin and insulin-like growth factors (IGFs). He has also studied receptor signalling for other peptide hormones such as growth hormone and relaxin, and key pathophysiological aspects of diabetes mellitus. De Meyts held professorial posts for over three decades at several European and United States institutions and currently is an emeritus professor in the Science Faculty at the Université catholique de Louvain. [1] [2] While living in Denmark (1990-2010) he occupied executive research positions at Novo Nordisk. [3] De Meyts (a.k.a. Chuck) is also known as a science cartoonist. [4] [5]

Contents

Biography

De Meyts was born in Verviers (Belgium) in 1944. [6] He attended high school at the Athénée Royal de Verviers, where he read "Humanités Anciennes" (Latin-Mathématiques). In 1969 De Meyts received his MD with honors ("Grande Distinction") from the University of Liège Medical School, and during the subsequent three years he specialized in internal medicine at the Hôpital de Bavière. Soon after he spent three years at NIH as a visiting scientist. During this NIH period De Meyts became a prominent member of the research group led by Jesse Roth, studying insulin receptors, and authoring a dozen original papers in duly indexed journals. [7] [8] In 1976, after NIH, he returned to Belgium where he occupied academic positions at universities including the Vrije Universiteit Brussel and the International Institute of Cellular and Molecular Pathology (now called "de Duve Institute", Université catholique de Louvain). De Meyts then moved to California (1984-1990), where he joined the Beckman Research Institute of City of Hope, (Duarte) and also taught at the University of Southern California for a short period. Immediately after, De Meyts was recruited by Novo Nordisk where he successively became the director of research of the Hagedorn Research Institute (1990-2000), scientific director of its Receptor Systems Biology Laboratory (2000-2010), and corporate vice-president of the company. During this period in Denmark until 2011 De Meyts simultaneously held academic posts as adjunct professor of experimental endocrinology (2000-2005) and guest lecturer (2007-2011) at the University of Copenhagen Faculty of Health Sciences. [9] Since then De Meyts returned to his home country and founded his own consulting company in Kraainem, where he remains professionally active. [10]

Research

De Meyts began his research career while a medical student at the University of Liège, collaborating with mentors such as Jean Lecomte and Annie Cession-Fossion in studies of the vascular actions of sympathomimetics. [11] [12] During a three-year visit to NIH starting in 1973, De Meyts got involved in what -by far- would become his major research fields: hormone-receptor interaction of peptide hormones and the study of the physiopathogenesis of diabetes. In the latter field his article with Steven G. Gray was the first to propose the possible etiological role of epigenetic factors in diabetes. [13] Also, De Meyts's articles first coined the term diabetogenes (1993), a new concept which has gained significant acceptance among independent peers in many countries (France, [14] US, [15] [16] [17] [18] Japan [19] and Denmark). [20] [21] Below is a list of De Meyts's most notable research topics and achievements:

Papers

De Meyt's most recent papers as a main author include:

Career

Editorial activity

De Meyts is chief specialty editor of Frontiers in Molecular and Structural Endocrinology , [46] associate editor of Frontiers in Systems Biology, [1] [47] and member of the editorial board of the Journal of Biological Chemistry . [48]

Awards

Cartoonist

Black-Box concept of insulin action, by Chuck Blackbox revisited by Pierre De Meyts, alias Chuck.jpg
Black-Box concept of insulin action, by Chuck

De Meyts's often iconoclastic cartoons first attained notoriety among francophone readers during the student upheavals occurring in 1968–69. [49] Many of his cartoons and posters from this period are archived and can be consulted at the Institut d’histoire ouvrière, économique et sociale in Seraing. [50] [51] [52] Once a scientist, he began drawing satirical science-cartoons. Many of these have been published in mainstream journals such as Nature , Trends in Biochemical Sciences , and Trends in Pharmacological Sciences . [5]

Related Research Articles

<span class="mw-page-title-main">Insulin</span> Peptide hormone

Insulin is a peptide hormone produced by beta cells of the pancreatic islets encoded in humans by the insulin (INS) gene. It is the main anabolic hormone of the body. It regulates the metabolism of carbohydrates, fats, and protein by promoting the absorption of glucose from the blood into cells of the liver, fat, and skeletal muscles. In these tissues the absorbed glucose is converted into either glycogen, via glycogenesis, or fats (triglycerides), via lipogenesis; in the liver, glucose is converted into both. Glucose production and secretion by the liver are strongly inhibited by high concentrations of insulin in the blood. Circulating insulin also affects the synthesis of proteins in a wide variety of tissues. It is thus an anabolic hormone, promoting the conversion of small molecules in the blood into large molecules in the cells. Low insulin in the blood has the opposite effect, promoting widespread catabolism, especially of reserve body fat.

<span class="mw-page-title-main">Insulin-like growth factor</span> Proteins similar to insulin that stimulate cell proliferation

The insulin-like growth factors (IGFs) are proteins with high sequence similarity to insulin. IGFs are part of a complex system that cells use to communicate with their physiologic environment. This complex system consists of two cell-surface receptors, two ligands, a family of seven high-affinity IGF-binding proteins, as well as associated IGFBP degrading enzymes, referred to collectively as proteases.

Insulin resistance (IR) is a pathological condition in which cells in insulin-sensitive tissues in the body fail to respond normally to the hormone insulin or downregulate insulin receptors in response to hyperinsulinemia.

<span class="mw-page-title-main">Insulin receptor</span> Cell receptor found in humans

The insulin receptor (IR) is a transmembrane receptor that is activated by insulin, IGF-I, IGF-II and belongs to the large class of receptor tyrosine kinase. Metabolically, the insulin receptor plays a key role in the regulation of glucose homeostasis; a functional process that under degenerate conditions may result in a range of clinical manifestations including diabetes and cancer. Insulin signalling controls access to blood glucose in body cells. When insulin falls, especially in those with high insulin sensitivity, body cells begin only to have access to lipids that do not require transport across the membrane. So, in this way, insulin is the key regulator of fat metabolism as well. Biochemically, the insulin receptor is encoded by a single gene INSR, from which alternate splicing during transcription results in either IR-A or IR-B isoforms. Downstream post-translational events of either isoform result in the formation of a proteolytically cleaved α and β subunit, which upon combination are ultimately capable of homo or hetero-dimerisation to produce the ≈320 kDa disulfide-linked transmembrane insulin receptor.

<span class="mw-page-title-main">Insulin-like growth factor 1</span> Protein found in humans

Insulin-like growth factor 1 (IGF-1), also called somatomedin C, is a hormone similar in molecular structure to insulin which plays an important role in childhood growth, and has anabolic effects in adults. In the 1950s IGF-1 was called "sulfation factor" because it stimulated sulfation of cartilage in vitro, and in the 1970s due to its effects it was termed "nonsuppressible insulin-like activity" (NSILA).

<span class="mw-page-title-main">Adiponectin</span> Mammalian protein found in Homo sapiens

Adiponectin is a protein hormone and adipokine, which is involved in regulating glucose levels and fatty acid breakdown. In humans, it is encoded by the ADIPOQ gene and is produced primarily in adipose tissue, but also in muscle and even in the brain.

<span class="mw-page-title-main">Insulin-like growth factor 2</span> Protein hormone

Insulin-like growth factor 2 (IGF-2) is one of three protein hormones that share structural similarity to insulin. The MeSH definition reads: "A well-characterized neutral peptide believed to be secreted by the liver and to circulate in the blood. It has growth-regulating, insulin-like and mitogenic activities. The growth factor has a major, but not absolute, dependence on somatotropin. It is believed to be a major fetal growth factor in contrast to insulin-like growth factor 1 (IGF-1), which is a major growth factor in adults."

<span class="mw-page-title-main">Fibroblast growth factor 1</span> Protein-coding gene in the species Homo sapiens

Fibroblast growth factor 1(FGF-1) also known as acidic fibroblast growth factor (aFGF), is a growth factor and signaling protein encoded by the FGF1 gene. It is synthesized as a 155 amino acid polypeptide, whose mature form is a non-glycosylated 17-18 kDa protein. Fibroblast growth factor protein was first purified in 1975, but soon afterwards others using different conditions isolated acidic FGF, Heparin-binding growth factor-1, and Endothelial cell growth factor-1. Gene sequencing revealed that this group was actually the same growth factor and that FGF1 was a member of a family of FGF proteins.

<span class="mw-page-title-main">Insulin-like growth factor 1 receptor</span> Cell receptor protein found in humans

The insulin-like growth factor 1 (IGF-1) receptor is a protein found on the surface of human cells. It is a transmembrane receptor that is activated by a hormone called insulin-like growth factor 1 (IGF-1) and by a related hormone called IGF-2. It belongs to the large class of tyrosine kinase receptors. This receptor mediates the effects of IGF-1, which is a polypeptide protein hormone similar in molecular structure to insulin. IGF-1 plays an important role in growth and continues to have anabolic effects in adults – meaning that it can induce hypertrophy of skeletal muscle and other target tissues. Mice lacking the IGF-1 receptor die late in development, and show a dramatic reduction in body mass. This testifies to the strong growth-promoting effect of this receptor.

<span class="mw-page-title-main">Glucagon receptor</span> Protein-coding gene in the species Homo sapiens

The glucagon receptor is a 62 kDa protein that is activated by glucagon and is a member of the class B G-protein coupled family of receptors, coupled to G alpha i, Gs and to a lesser extent G alpha q. Stimulation of the receptor results in the activation of adenylate cyclase and phospholipase C and in increased levels of the secondary messengers intracellular cAMP and calcium. In humans, the glucagon receptor is encoded by the GCGR gene.

<span class="mw-page-title-main">Hormone-sensitive lipase</span> Enzyme

Hormone-sensitive lipase (EC 3.1.1.79, HSL), also previously known as cholesteryl ester hydrolase (CEH), sometimes referred to as triacylglycerol lipase, is an enzyme that, in humans, is encoded by the LIPE gene, and catalyzes the following reaction:

<span class="mw-page-title-main">Laron syndrome</span> Medical condition

Laron syndrome (LS), also known as growth hormone insensitivity or growth hormone receptor deficiency (GHRD), is an autosomal recessive disorder characterized by a lack of insulin-like growth factor 1 production in response to growth hormone. It is usually caused by inherited growth hormone receptor (GHR) mutations.

<span class="mw-page-title-main">LYN</span> Mammalian protein found in Homo sapiens

Tyrosine-protein kinase Lyn is a protein that in humans is encoded by the LYN gene.

<span class="mw-page-title-main">Insulin receptor substrate 1</span> Protein found in humans

Insulin receptor substrate 1(IRS-1) is a signaling adapter protein that in humans is encoded by the IRS1 gene. It is a 180 kDa protein with amino acid sequence of 1242 residues. It contains a single pleckstrin homology (PH) domain at the N-terminus and a PTB domain ca. 40 residues downstream of this, followed by a poorly conserved C-terminus tail. Together with IRS2, IRS3 (pseudogene) and IRS4, it is homologous to the Drosophila protein chico, whose disruption extends the median lifespan of flies up to 48%. Similarly, Irs1 mutant mice experience moderate life extension and delayed age-related pathologies.

<span class="mw-page-title-main">IGFBP3</span> Protein-coding gene in the species Homo sapiens

Insulin-like growth factor-binding protein 3, also known as IGFBP-3, is a protein that in humans is encoded by the IGFBP3 gene. IGFBP-3 is one of six IGF binding proteins that have highly conserved structures and bind the insulin-like growth factors IGF-1 and IGF-2 with high affinity. IGFBP-7, sometimes included in this family, shares neither the conserved structural features nor the high IGF affinity. Instead, IGFBP-7 binds IGF1R, which blocks IGF-1 and IGF-2 binding, resulting in apoptosis.

<span class="mw-page-title-main">IRS2</span> Protein-coding gene in the species Homo sapiens

Insulin receptor substrate 2 is a protein that in humans is encoded by the IRS2 gene.

<span class="mw-page-title-main">SOCS2</span> Protein-coding gene in the species Homo sapiens

Suppressor of cytokine signaling 2 is a protein that in humans is encoded by the SOCS2 gene.

Breast development, also known as mammogenesis, is a complex biological process in primates that takes place throughout a female's life.

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

Adipogenesis is the formation of adipocytes from stem cells. It involves 2 phases, determination, and terminal differentiation. Determination is mesenchymal stem cells committing to the adipocyte precursor cells, also known as lipoblasts or preadipocytes which lose the potential to differentiate to other types of cells such as chondrocytes, myocytes, and osteoblasts. Terminal differentiation is that preadipocytes differentiate into mature adipocytes. Adipocytes can arise either from preadipocytes resident in adipose tissue, or from bone-marrow derived progenitor cells that migrate to adipose tissue.

Derek LeRoith is a South African endocrinologist and Professor of Medicine and the current Chief of the Hilda and J. Lester Gabrilove, M.D. Division of Endocrinology, Diabetes and Bone Disease and Director of the Metabolism Institute of the Mount Sinai Medical Center in New York City. He is an international expert in insulin-like growth factor-1 (IGF-1).

References

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  2. ↑ "Speaker Biographies". ectsoc.org. Archived from the original on 5 October 2010. Retrieved 17 September 2014.
  3. ↑ "Pierre de Meyts". excellence-in-diabetes.eu. Retrieved 17 September 2014.
  4. ↑ "Featured Cartoons by Pierre De Meyts". sarahgreene.net. Archived from the original on 6 October 2014. Retrieved 17 September 2014.
  5. 1 2 De Meyts, Pierre (2005). "A Scientist and a Cartoonist: how Chuck came to be". IUBMB Life. 57 (4–5): 251–252. doi: 10.1080/152165405000943134 . S2CID   221830282.
  6. ↑ "1944, the liberation of Brussels". brussels.be. Archived from the original on 7 March 2015. Retrieved 17 September 2014.
  7. ↑ "C U R R I C U L U M V I T A E, PDM" (PDF). demeytsconsulting.com. Archived from the original (PDF) on 6 October 2014. Retrieved 22 September 2014.
  8. ↑ "JESSE ROTH, MD, FACP". 2.kenes.com. Retrieved 22 September 2014.
  9. 1 2 3 4 5 "PDM biographical sketch" (PDF). 3.niddk.nih.gov. Retrieved 2 October 2014.
  10. ↑ "De Meyts R&D Consulting SPRLU". demeytsconsulting.com. Retrieved 22 September 2014.
  11. ↑ De Meyts, P; Lecomte, J (20 July 1967). "[Pseudo-ephedrine as sympathomimetic amine with indirect action in the rat]". Comptes Rendus des Séances de la Société de Biologie et de Ses Filiales. 161 (2): 487–8. PMID   4229166.
  12. ↑ De Meyts, P; Cession-Fossion, A (1966). "[Ephedrine as a sympathicomimetic amine with indirect action in the rat]". Comptes Rendus des Séances de la Société de Biologie et de Ses Filiales. 160 (11): 2224–7. PMID   4228170.
  13. ↑ Gray, SG; De Meyts, P (September–October 2005). "Role of histone and transcription factor acetylation in diabetes pathogenesis". Diabetes/Metabolism Research and Reviews. 21 (5): 416–33. doi:10.1002/dmrr.559. PMID   15906405. S2CID   35952558.
  14. ↑ Baudry, A; Leroux, L; Jackerott, M; Joshi, RL (April 2002). "Genetic manipulation of insulin signaling, action and secretion in mice. Insights into glucose homeostasis and pathogenesis of type 2 diabetes". EMBO Reports. 3 (4): 323–8. doi:10.1093/embo-reports/kvf078. PMC   1084066 . PMID   11943762.
  15. ↑ Redondo, MJ; Fain, PR; Eisenbarth, GS (2001). "Genetics of type 1A diabetes". Recent Progress in Hormone Research. 56: 69–89. doi: 10.1210/rp.56.1.69 . PMID   11237226.
  16. ↑ Sacks, DB; McDonald, JM (February 1996). "The pathogenesis of type II diabetes mellitus. A polygenic disease". American Journal of Clinical Pathology. 105 (2): 149–56. doi: 10.1093/ajcp/105.2.149 . PMID   8607437.
  17. ↑ Kahn, CR; Vicent, D; Doria, A (1996). "Genetics of non-insulin-dependent (type-II) diabetes mellitus". Annual Review of Medicine. 47: 509–31. doi:10.1146/annurev.med.47.1.509. PMID   8712800.
  18. ↑ Kahn, CR (August 1994). "Banting Lecture. Insulin action, diabetogenes, and the cause of type II diabetes". Diabetes. 43 (8): 1066–84. doi:10.2337/diab.43.8.1066. PMID   8039601. S2CID   2536019.
  19. ↑ Murakami, T; Shima, K (August 1995). "[Diabetogenes; which cause type II diabetes mellitus]". Rinsho Byori. 43 (8): 781–5. PMID   7474436.
  20. ↑ Hansen, L (November 2003). "Candidate genes and late-onset type 2 diabetes mellitus. Susceptibility genes or common polymorphisms?". Danish Medical Bulletin. 50 (4): 320–46. PMID   14694850.
  21. ↑ Kahn, C. R. (1994). "Pubmed search: (diabetogenes[Title/Abstract]) NOT De Meyts[Author]". Diabetes. 43 (8): 1066–84. doi:10.2337/diab.43.8.1066. PMID   8039601. S2CID   2536019.
  22. ↑ Smal, J; Closset, J; Hennen, G; de Meyts, P (15 January 1985). "Receptor-binding and down-regulatory properties of 22000-Mr human growth hormone and its natural 20000-Mr variant on IM-9 human lymphocytes". The Biochemical Journal. 225 (2): 283–9. doi:10.1042/bj2250283. PMC   1144588 . PMID   2983666.
  23. ↑ Ilondo, MM; Damholt, AB; Cunningham, BA; Wells, JA; De Meyts, P; Shymko, RM (June 1994). "Receptor dimerization determines the effects of growth hormone in primary rat adipocytes and cultured human IM-9 lymphocytes". Endocrinology. 134 (6): 2397–403. doi:10.1210/endo.134.6.8194466. PMID   8194466.
  24. ↑ Wabitsch, M; Heinze, E; Hauner, H; Shymko, RM; Teller, WM; De Meyts, P; Ilondo, MM (January 1996). "Biological effects of human growth hormone in rat adipocyte precursor cells and newly differentiated adipocytes in primary culture". Metabolism: Clinical and Experimental. 45 (1): 34–42. doi:10.1016/s0026-0495(96)90197-3. PMID   8544774.
  25. ↑ Wabitsch, M; Braun, S; Hauner, H; Heinze, E; Ilondo, MM; Shymko, R; De Meyts, P; Teller, WM (September 1996). "Mitogenic and antiadipogenic properties of human growth hormone in differentiating human adipocyte precursor cells in primary culture". Pediatric Research. 40 (3): 450–6. doi: 10.1203/00006450-199609000-00014 . PMID   8865283.
  26. ↑ de Meyts, P; Roth, J; Neville DM, Jr; Gavin JR, 3rd; Lesniak, MA (1 November 1973). "Insulin interactions with its receptors: experimental evidence for negative cooperativity". Biochemical and Biophysical Research Communications. 55 (1): 154–61. doi:10.1016/s0006-291x(73)80072-5. PMID   4361269.{{cite journal}}: CS1 maint: numeric names: authors list (link)
  27. ↑ De Meyts, P (1976). "Cooperative properties of hormone receptors in cell membranes". Journal of Supramolecular Structure. 4 (2): 241–58. doi:10.1002/jss.400040211. PMID   177816.
  28. ↑ DeMeyts, P; Bainco, AR; Roth, J (10 April 1976). "Site-site interactions among insulin receptors. Characterization of the negative cooperativity". The Journal of Biological Chemistry. 251 (7): 1877–88. doi: 10.1016/S0021-9258(17)33630-X . PMID   5434.
  29. ↑ De Meyts, P (August 2008). "The insulin receptor: a prototype for dimeric, allosteric membrane receptors?". Trends in Biochemical Sciences. 33 (8): 376–84. doi:10.1016/j.tibs.2008.06.003. PMID   18640841.
  30. ↑ De Meyts, P; Gauguin, L; Svendsen, AM; Sarhan, M; Knudsen, L; Nøhr, J; Kiselyov, VV (April 2009). "Structural basis of allosteric ligand-receptor interactions in the insulin/relaxin peptide family: implications for other receptor tyrosine kinases and G-protein-coupled receptors". Annals of the New York Academy of Sciences. 1160: 45–53. doi: 10.1111/j.1749-6632.2009.03837.x . PMID   19416158. S2CID   12579339.
  31. ↑ De Meyts, P (September 1994). "The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling". Diabetologia. 37 (Suppl 2): S135–48. doi: 10.1007/bf00400837 . PMID   7821729.
  32. ↑ Gauguin, L; Klaproth, B; Sajid, W; Andersen, AS; McNeil, KA; Forbes, BE; De Meyts, P (1 February 2008). "Structural basis for the lower affinity of the insulin-like growth factors for the insulin receptor". The Journal of Biological Chemistry. 283 (5): 2604–13. doi: 10.1074/jbc.m709220200 . PMID   18048361.
  33. ↑ Gauguin, L; Delaine, C; Alvino, CL; McNeil, KA; Wallace, JC; Forbes, BE; De Meyts, P (25 July 2008). "Alanine scanning of a putative receptor binding surface of insulin-like growth factor-I". The Journal of Biological Chemistry. 283 (30): 20821–9. doi: 10.1074/jbc.m802620200 . PMC   3258947 . PMID   18502759.
  34. ↑ Shymko, RM; De Meyts, P; Thomas, R (1 September 1997). "Logical analysis of timing-dependent receptor signalling specificity: application to the insulin receptor metabolic and mitogenic signalling pathways". The Biochemical Journal. 326 (2): 463–9. doi:10.1042/bj3260463. PMC   1218692 . PMID   9291119.
  35. ↑ Svendsen, AM; Winge, SB; Zimmermann, M; Lindvig, AB; Warzecha, CB; Sajid, W; Horne, MC; De Meyts, P (1 January 2014). "Down-regulation of cyclin G2 by insulin, IGF-I (insulin-like growth factor 1) and X10 (AspB10 insulin): role in mitogenesis". The Biochemical Journal. 457 (1): 69–77. doi:10.1042/bj20130490. PMID   24059861.
  36. ↑ Kiselyov, VV; Versteyhe, S; Gauguin, L; De Meyts, P (2009). "Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation". Molecular Systems Biology. 5: 243. doi:10.1038/msb.2008.78. PMC   2657531 . PMID   19225456.
  37. ↑ "Vladislav V Kiselyov". researchgate.net. Retrieved 26 September 2014.
  38. ↑ De Meyts, P (1993). "The Diabetogenes Concept of NIDDM". New Concepts in the Pathogenesis of NIDDM. Advances in Experimental Medicine and Biology. Vol. 334. pp. 89–100. doi:10.1007/978-1-4615-2910-1_7. ISBN   978-1-4613-6262-3. PMID   8249698.
  39. ↑ Lamothe, B; Baudry, A; Desbois, P; Lamotte, L; Bucchini, D; De Meyts, P; Joshi, RL (15 October 1998). "Genetic engineering in mice: impact on insulin signalling and action". The Biochemical Journal. 335 (2): 193–204. doi:10.1042/bj3350193. PMC   1219769 . PMID   9761714.
  40. ↑ De Meyts, P; Whittaker, J (October 2002). "Structural biology of insulin and IGF1 receptors: implications for drug design". Nature Reviews. Drug Discovery. 1 (10): 769–83. doi:10.1038/nrd917. PMID   12360255. S2CID   31103926.
  41. ↑ De Meyts, Pierre (2015). "Insulin/receptor binding: the last piece of the puzzle? What recent progress on the structure of the insulin/receptor complex tells us (or not) about negative cooperativity and activation". News and Reviews in Molecular, Cellular and Developmental Biology. 37 (4): 389–397. doi:10.1002/bies.201400190. ISSN   1521-1878. PMID   25630923.
  42. ↑ De Meyts, Pierre (2000), Feingold, Kenneth R.; Anawalt, Bradley; Boyce, Alison; Chrousos, George (eds.), "The Insulin Receptor and Its Signal Transduction Network", Endotext, South Dartmouth (MA): MDText.com, Inc., PMID   27512793 , retrieved 30 January 2022
  43. ↑ De Meyts, Pierre (5 October 2016). "Structural basis for the poisonous activity of a predator's venom insulin". Nature Structural & Molecular Biology. 23 (10): 872–874. doi:10.1038/nsmb.3304. ISSN   1545-9985. PMID   27706132. S2CID   195675703.
  44. ↑ Rostène, William; De Meyts, Pierre (28 September 2021). "Insulin: A 100-Year-Old Discovery With a Fascinating History". Endocrine Reviews. 42 (5): 503–527. doi: 10.1210/endrev/bnab020 . ISSN   1945-7189. PMID   34273145. S2CID   236034586.
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  47. ↑ "Editorial Board". frontiersin.org. Retrieved 29 September 2014.
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  51. ↑ "IHOES Aperçu général des fonds et collections 2013" (PDF). ihoes.be. Retrieved 29 September 2014.
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