PTPN5

Last updated
PTPN5
Protein PTPN5 PDB 2bij.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases PTPN5 , PTPSTEP, STEP, STEP61, protein tyrosine phosphatase, non-receptor type 5, protein tyrosine phosphatase non-receptor type 5
External IDs OMIM: 176879 MGI: 97807 HomoloGene: 8423 GeneCards: PTPN5
Orthologs
SpeciesHumanMouse
Entrez

84867

19259

Ensembl

ENSG00000110786

ENSMUSG00000030854

UniProt

P54829

P54830

RefSeq (mRNA)

NM_001163565
NM_013643

RefSeq (protein)

NP_001157037
NP_038671

Location (UCSC) Chr 11: 18.73 – 18.79 Mb Chr 7: 46.73 – 46.78 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Protein tyrosine phosphatase non-receptor type 5 is an enzyme that in humans is encoded by the PTPN5 gene. [5] [6]

Contents

Protein tyrosine phosphatase (PTP), non-receptor type 5, also known as STEP (STriatal-Enriched protein tyrosine Phosphatase), was the first brain-specific PTP discovered. [5] The human STEP locus maps to chromosome 11p15.2-p15.1 and the murine STEP gene to chromosome 7B3-B5. [7] The single STEP gene is alternatively spliced to produce several isoforms, [8] [9] the best characterized of which are the cytosolic STEP46 protein and the membrane-associated STEP61 protein. [10] [11]

Substrates

Seven known targets of STEP have been identified as of 2015, including ERK1/2, [12] [13] p38, [12] Fyn, [14] Pyk2, [15] PTPα, [16] and the glutamate receptor subunits GluN2B and GluA2. [17] [18] [19] STEP dephosphorylation of the kinases (ERK1/2, p38, Fyn, and Pyk2) occurs at a regulatory tyrosine within the kinase activation loop and leads to their inactivation. Dephosphorylation of a regulatory tyrosine on PTPα prevents the translocation of PTPα from the cytosol to lipid rafts, where it normally activates Fyn. [16] STEP thereby directly inactivates Fyn and also prevents the translocation of PTPα to compartments where it activates Fyn. STEP dephosphorylation of GluN2B and GluA2 leads to the internalization of NMDARs (GluN1/GluN2B) and AMPARs (GluA1/GluA2). Thus, one function of STEP is to oppose synaptic strengthening by inactivating kinases and internalizing receptors that are critical for the development of synaptic strengthening.

Clinical significance

STEP levels are disrupted in several diseases. Alzheimer's disease (AD) was the first illness to be associated with elevated STEP expression both in human cortex and in several mouse models of AD. [17] [20] [19] [21] STEP is also increased in fragile X syndrome, [22] schizophrenia, [23] and Parkinson's disease. [24] In AD and FXS mouse models, genetic reduction of STEP expression reverses many of the cognitive and behavioral deficits. [22] [19] Other laboratories have now shown that STEP activity is also reduced in several additional disorders. Thus, STEP levels or activity is decreased in Huntington's disease, [25] [26] cerebral ischemia, [27] alcohol abuse, [28] [29] [30] and stress disorders. [31] [32] The emergent model suggests that an optimal level of STEP is required at synaptic sites, and that both high and low levels disrupt synaptic function. [33] [34]

Inhibition

Several STEP inhibitors have now been discovered. [15] [35] GlaxoSmithKline chose STEP as a new project for their Discovery Partnerships with Academia (DPAc) in 2014. This is a relatively new program in drug discovery and brings together the academic world with the drug discovery expertise of GSK to discover new inhibitors of validated targets.

Related Research Articles

<span class="mw-page-title-main">AMPA receptor</span> Transmembrane protein family

The α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (also known as AMPA receptor, AMPAR, or quisqualate receptor) is an ionotropic transmembrane receptor for glutamate (iGluR) and predominantly Na+ ion channel that mediates fast synaptic transmission in the central nervous system (CNS). It has been traditionally classified as a non-NMDA-type receptor, along with the kainate receptor. Its name is derived from its ability to be activated by the artificial glutamate analog AMPA. The receptor was first named the "quisqualate receptor" by Watkins and colleagues after a naturally occurring agonist quisqualate and was only later given the label "AMPA receptor" after the selective agonist developed by Tage Honore and colleagues at the Royal Danish School of Pharmacy in Copenhagen. The GRIA2-encoded AMPA receptor ligand binding core (GluA2 LBD) was the first glutamate receptor ion channel domain to be crystallized.

<span class="mw-page-title-main">NMDA receptor</span> Glutamate receptor and ion channel protein found in nerve cells

The N-methyl-D-aspartatereceptor (also known as the NMDA receptor or NMDAR), is a glutamate receptor and predominantly Ca2+ ion channel found in neurons. The NMDA receptor is one of three types of ionotropic glutamate receptors, the other two being AMPA and kainate receptors. Depending on its subunit composition, its ligands are glutamate and glycine (or D-serine). However, the binding of the ligands is typically not sufficient to open the channel as it may be blocked by Mg2+ ions which are only removed when the neuron is sufficiently depolarized. Thus, the channel acts as a “coincidence detector” and only once both of these conditions are met, the channel opens and it allows positively charged ions (cations) to flow through the cell membrane. The NMDA receptor is thought to be very important for controlling synaptic plasticity and mediating learning and memory functions.

<span class="mw-page-title-main">Brain-derived neurotrophic factor</span> Protein found in humans

Brain-derived neurotrophic factor (BDNF), or abrineurin, is a protein that, in humans, is encoded by the BDNF gene. BDNF is a member of the neurotrophin family of growth factors, which are related to the canonical nerve growth factor (NGF), a family which also includes NT-3 and NT-4/NT-5. Neurotrophic factors are found in the brain and the periphery. BDNF was first isolated from a pig brain in 1982 by Yves-Alain Barde and Hans Thoenen.

<span class="mw-page-title-main">Kainate receptor</span> Class of ionotropic glutamate receptors

Kainate receptors, or kainic acid receptors (KARs), are ionotropic receptors that respond to the neurotransmitter glutamate. They were first identified as a distinct receptor type through their selective activation by the agonist kainate, a drug first isolated from the algae Digenea simplex. They have been traditionally classified as a non-NMDA-type receptor, along with the AMPA receptor. KARs are less understood than AMPA and NMDA receptors, the other ionotropic glutamate receptors. Postsynaptic kainate receptors are involved in excitatory neurotransmission. Presynaptic kainate receptors have been implicated in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism.

<span class="mw-page-title-main">Protein tyrosine phosphatase</span> Class of enzymes

Protein tyrosine phosphatases (EC 3.1.3.48, systematic name protein-tyrosine-phosphate phosphohydrolase) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins:

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

The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of bacteria, yeast, plants, viruses and animals. Proteins containing PDZ domains play a key role in anchoring receptor proteins in the membrane to cytoskeletal components. Proteins with these domains help hold together and organize signaling complexes at cellular membranes. These domains play a key role in the formation and function of signal transduction complexes. PDZ domains also play a highly significant role in the anchoring of cell surface receptors to the actin cytoskeleton via mediators like NHERF and ezrin.

<span class="mw-page-title-main">DLG1</span> Protein-coding gene in the species Homo sapiens

Discs large homolog 1 (DLG1), also known as synapse-associated protein 97 or SAP97, is a scaffold protein that in humans is encoded by the SAP97 gene.

<span class="mw-page-title-main">GRIN2B</span> Protein-coding gene in the species Homo sapiens

Glutamate [NMDA] receptor subunit epsilon-2, also known as N-methyl D-aspartate receptor subtype 2B, is a protein that in humans is encoded by the GRIN2B gene.

<span class="mw-page-title-main">GRIN2A</span> Protein-coding gene in the species Homo sapiens

Glutamate [NMDA] receptor subunit epsilon-1 is a protein that in humans is encoded by the GRIN2A gene. With 1464 amino acids, the canonical GluN2A subunit isoform is large. GluN2A-short isoforms specific to primates can be produced by alternative splicing and contain 1281 amino acids.

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

Receptor-type tyrosine-protein phosphatase F is an enzyme that, in humans, is encoded by the PTPRF gene.

<span class="mw-page-title-main">PPP1R1B</span> Protein

Protein phosphatase 1 regulatory subunit 1B (PPP1R1B), also known as dopamine- and cAMP-regulated neuronal phosphoprotein (DARPP-32), is a protein that in humans is encoded by the PPP1R1B gene.

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

Contactin 1, also known as CNTN1, is a protein which in humans is encoded by the CNTN1 gene.

<span class="mw-page-title-main">PTPN7</span> Protein-coding gene in the species Homo sapiens

Protein tyrosine phosphatase non-receptor type 7 is an enzyme that in humans is encoded by the PTPN7 gene.

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

Receptor-type tyrosine-protein phosphatase beta or VE-PTP is an enzyme specifically expressed in endothelial cells that in humans is encoded by the PTPRB gene.

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

Receptor-type tyrosine-protein phosphatase S, also known as R-PTP-S, R-PTP-sigma, or PTPσ, is an enzyme that in humans is encoded by the PTPRS gene.

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

Protein tyrosine phosphatase receptor-type R is an enzyme that in humans is encoded by the PTPRR gene.

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

Liprin-alpha-1 is a protein that in humans is encoded by the PPFIA1 gene.

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

Receptor-type tyrosine-protein phosphatase T is an enzyme that in humans is encoded by the PTPRT gene.

<span class="mw-page-title-main">GRID2</span> Protein-coding gene in the species Homo sapiens

Glutamate receptor, ionotropic, delta 2, also known as GluD2, GluRδ2, or δ2, is a protein that in humans is encoded by the GRID2 gene. This protein together with GluD1 belongs to the delta receptor subtype of ionotropic glutamate receptors. They possess 14–24% sequence homology with AMPA, kainate, and NMDA subunits, but, despite their name, do not actually bind glutamate or various other glutamate agonists.

R. Suzanne Zukin is an American neuroscientist and a professor of neuroscience who directs a research lab as a F. M. Kirby Chair in Neural Repair and Protection and director of the Neuropsychopharmacology Center at Albert Einstein College of Medicine. Zukin's areas of research include neurodegenerative disorders, Ischemia, Epigenetics and Autism and uses molecular biology approaches to research these disorders. Zukin has made seminal contributions to the understanding of NMDA and AMPA receptor function and activity.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000110786 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030854 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 Lombroso PJ, Murdoch G, Lerner M (Aug 1991). "Molecular characterization of a protein-tyrosine-phosphatase enriched in striatum". Proceedings of the National Academy of Sciences of the United States of America. 88 (16): 7242–6. Bibcode:1991PNAS...88.7242L. doi: 10.1073/pnas.88.16.7242 . PMC   52270 . PMID   1714595.
  6. ↑ "Entrez Gene: PTPN5 protein tyrosine phosphatase, non-receptor type 5 (striatum-enriched)".
  7. ↑ Li X, Luna J, Lombroso PJ, Francke U (Aug 1995). "Molecular cloning of the human homolog of a striatum-enriched phosphatase (STEP) gene and chromosomal mapping of the human and murine loci". Genomics. 28 (3): 442–9. doi: 10.1006/geno.1995.1173 . PMID   7490079.
  8. ↑ Sharma E, Zhao F, Bult A, Lombroso PJ (Aug 1995). "Identification of two alternatively spliced transcripts of STEP: a subfamily of brain-enriched protein tyrosine phosphatases". Brain Research. Molecular Brain Research. 32 (1): 87–93. doi: 10.1016/0169-328x(95)00066-2 . PMID   7494467.
  9. ↑ Bult A, Zhao F, Dirkx R, Sharma E, Lukacsi E, Solimena M, Naegele JR, Lombroso PJ (Dec 1996). "STEP61: a member of a family of brain-enriched PTPs is localized to the endoplasmic reticulum". The Journal of Neuroscience. 16 (24): 7821–31. doi: 10.1523/JNEUROSCI.16-24-07821.1996 . PMC   6579237 . PMID   8987810.
  10. ↑ Lombroso PJ, Naegele JR, Sharma E, Lerner M (Jul 1993). "A protein tyrosine phosphatase expressed within dopaminoceptive neurons of the basal ganglia and related structures". The Journal of Neuroscience. 13 (7): 3064–74. doi: 10.1523/JNEUROSCI.13-07-03064.1993 . PMC   6576687 . PMID   8331384.
  11. ↑ Boulanger LM, Lombroso PJ, Raghunathan A, During MJ, Wahle P, Naegele JR (Feb 1995). "Cellular and molecular characterization of a brain-enriched protein tyrosine phosphatase". The Journal of Neuroscience. 15 (2): 1532–44. doi: 10.1523/JNEUROSCI.15-02-01532.1995 . PMC   6577844 . PMID   7869116.
  12. 1 2 Muñoz JJ, Tárrega C, Blanco-Aparicio C, Pulido R (May 2003). "Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38alpha is determined by a kinase specificity sequence and influenced by reducing agents". The Biochemical Journal. 372 (Pt 1): 193–201. doi:10.1042/BJ20021941. PMC   1223371 . PMID   12583813.
  13. ↑ Paul S, Nairn AC, Wang P, Lombroso PJ (Jan 2003). "NMDA-mediated activation of the tyrosine phosphatase STEP regulates the duration of ERK signaling". Nature Neuroscience. 6 (1): 34–42. doi:10.1038/nn989. PMID   12483215. S2CID   32980653.
  14. ↑ Nguyen TH, Liu J, Lombroso PJ (Jul 2002). "Striatal enriched phosphatase 61 dephosphorylates Fyn at phosphotyrosine 420". The Journal of Biological Chemistry. 277 (27): 24274–9. doi: 10.1074/jbc.M111683200 . PMID   11983687.
  15. 1 2 Xu J, Chatterjee M, Baguley TD, Brouillette J, Kurup P, Ghosh D, Kanyo J, Zhang Y, Seyb K, Ononenyi C, Foscue E, Anderson GM, Gresack J, Cuny GD, Glicksman MA, Greengard P, Lam TT, Tautz L, Nairn AC, Ellman JA, Lombroso PJ (Aug 2014). "Inhibitor of the tyrosine phosphatase STEP reverses cognitive deficits in a mouse model of Alzheimer's disease". PLOS Biology. 12 (8): e1001923. doi: 10.1371/journal.pbio.1001923 . PMC   4122355 . PMID   25093460.
  16. 1 2 Xu J, Kurup P, Foscue E, Lombroso PJ (May 2015). "STriatal-Enriched protein tyrosine Phosphatase (STEP) Regulates the PTPα/Fyn Signaling Pathway". Journal of Neurochemistry. 134 (4): 629–41. doi:10.1111/jnc.13160. PMC   4516628 . PMID   25951993.
  17. 1 2 Snyder EM, Nong Y, Almeida CG, Paul S, Moran T, Choi EY, Nairn AC, Salter MW, Lombroso PJ, Gouras GK, Greengard P (Aug 2005). "Regulation of NMDA receptor trafficking by amyloid-beta". Nature Neuroscience. 8 (8): 1051–8. doi:10.1038/nn1503. PMID   16025111. S2CID   25182223.
  18. ↑ Xu J, Kurup P, Zhang Y, Goebel-Goody SM, Wu PH, Hawasli AH, Baum ML, Bibb JA, Lombroso PJ (Jul 2009). "Extrasynaptic NMDA receptors couple preferentially to excitotoxicity via calpain-mediated cleavage of STEP". The Journal of Neuroscience. 29 (29): 9330–43. doi:10.1523/JNEUROSCI.2212-09.2009. PMC   2737362 . PMID   19625523.
  19. 1 2 3 Zhang Y, Kurup P, Xu J, Carty N, Fernandez SM, Nygaard HB, Pittenger C, Greengard P, Strittmatter SM, Nairn AC, Lombroso PJ (Nov 2010). "Genetic reduction of striatal-enriched tyrosine phosphatase (STEP) reverses cognitive and cellular deficits in an Alzheimer's disease mouse model". Proceedings of the National Academy of Sciences of the United States of America. 107 (44): 19014–9. Bibcode:2010PNAS..10719014Z. doi: 10.1073/pnas.1013543107 . PMC   2973892 . PMID   20956308.
  20. ↑ Kurup P, Zhang Y, Xu J, Venkitaramani DV, Haroutunian V, Greengard P, Nairn AC, Lombroso PJ (Apr 2010). "Abeta-mediated NMDA receptor endocytosis in Alzheimer's disease involves ubiquitination of the tyrosine phosphatase STEP61". The Journal of Neuroscience. 30 (17): 5948–57. doi:10.1523/JNEUROSCI.0157-10.2010. PMC   2868326 . PMID   20427654.
  21. ↑ Zhang Y, Kurup P, Xu J, Anderson GM, Greengard P, Nairn AC, Lombroso PJ (Nov 2011). "Reduced levels of the tyrosine phosphatase STEP block β amyloid-mediated GluA1/GluA2 receptor internalization". Journal of Neurochemistry. 119 (3): 664–72. doi:10.1111/j.1471-4159.2011.07450.x. PMC   3192910 . PMID   21883219.
  22. 1 2 Goebel-Goody SM, Wilson-Wallis ED, Royston S, Tagliatela SM, Naegele JR, Lombroso PJ (Jul 2012). "Genetic manipulation of STEP reverses behavioral abnormalities in a fragile X syndrome mouse model". Genes, Brain and Behavior. 11 (5): 586–600. doi:10.1111/j.1601-183X.2012.00781.x. PMC   3922131 . PMID   22405502.
  23. ↑ Carty NC, Xu J, Kurup P, Brouillette J, Goebel-Goody SM, Austin DR, Yuan P, Chen G, Correa PR, Haroutunian V, Pittenger C, Lombroso PJ (2012). "The tyrosine phosphatase STEP: implications in schizophrenia and the molecular mechanism underlying antipsychotic medications". Translational Psychiatry. 2 (7): e137. doi:10.1038/tp.2012.63. PMC   3410627 . PMID   22781170.
  24. ↑ Kurup PK, Xu J, Videira RA, Ononenyi C, Baltazar G, Lombroso PJ, Nairn AC (Jan 2015). "STEP61 is a substrate of the E3 ligase parkin and is upregulated in Parkinson's disease". Proceedings of the National Academy of Sciences of the United States of America. 112 (4): 1202–7. Bibcode:2015PNAS..112.1202K. doi: 10.1073/pnas.1417423112 . PMC   4313846 . PMID   25583483.
  25. ↑ Saavedra A, Giralt A, Rué L, Xifró X, Xu J, Ortega Z, Lucas JJ, Lombroso PJ, Alberch J, Pérez-Navarro E (Jun 2011). "Striatal-enriched protein tyrosine phosphatase expression and activity in Huntington's disease: a STEP in the resistance to excitotoxicity". The Journal of Neuroscience. 31 (22): 8150–62. doi:10.1523/JNEUROSCI.3446-10.2011. PMC   3472648 . PMID   21632937.
  26. ↑ Gladding CM, Sepers MD, Xu J, Zhang LY, Milnerwood AJ, Lombroso PJ, Raymond LA (Sep 2012). "Calpain and STriatal-Enriched protein tyrosine phosphatase (STEP) activation contribute to extrasynaptic NMDA receptor localization in a Huntington's disease mouse model". Human Molecular Genetics. 21 (17): 3739–52. doi:10.1093/hmg/dds154. PMC   3412376 . PMID   22523092.
  27. ↑ Deb I, Manhas N, Poddar R, Rajagopal S, Allan AM, Lombroso PJ, Rosenberg GA, Candelario-Jalil E, Paul S (Nov 2013). "Neuroprotective role of a brain-enriched tyrosine phosphatase, STEP, in focal cerebral ischemia". The Journal of Neuroscience. 33 (45): 17814–26. doi:10.1523/JNEUROSCI.2346-12.2013. PMC   3818554 . PMID   24198371.
  28. ↑ Hicklin TR, Wu PH, Radcliffe RA, Freund RK, Goebel-Goody SM, Correa PR, Proctor WR, Lombroso PJ, Browning MD (Apr 2011). "Alcohol inhibition of the NMDA receptor function, long-term potentiation, and fear learning requires striatal-enriched protein tyrosine phosphatase". Proceedings of the National Academy of Sciences of the United States of America. 108 (16): 6650–5. Bibcode:2011PNAS..108.6650H. doi: 10.1073/pnas.1017856108 . PMC   3081035 . PMID   21464302.
  29. ↑ Darcq E, Hamida SB, Wu S, Phamluong K, Kharazia V, Xu J, Lombroso P, Ron D (Jun 2014). "Inhibition of striatal-enriched tyrosine phosphatase 61 in the dorsomedial striatum is sufficient to increased ethanol consumption". Journal of Neurochemistry. 129 (6): 1024–34. doi:10.1111/jnc.12701. PMC   4055745 . PMID   24588427.
  30. ↑ Legastelois, R; Darcq, E; Wegner, S. A.; Lombroso, P. J.; Ron, D (2015). "Striatal-Enriched Protein Tyrosine Phosphatase Controls Responses to Aversive Stimuli: Implication for Ethanol Drinking". PLOS ONE. 10 (5): e0127408. Bibcode:2015PLoSO..1027408L. doi: 10.1371/journal.pone.0127408 . PMC   4438985 . PMID   25992601.
  31. ↑ Yang CH, Huang CC, Hsu KS (May 2012). "A critical role for protein tyrosine phosphatase nonreceptor type 5 in determining individual susceptibility to develop stress-related cognitive and morphological changes". The Journal of Neuroscience. 32 (22): 7550–62. doi: 10.1523/JNEUROSCI.5902-11.2012 . PMC   6703597 . PMID   22649233.
  32. ↑ Dabrowska J, Hazra R, Guo JD, Li C, Dewitt S, Xu J, Lombroso PJ, Rainnie DG (Dec 2013). "Striatal-enriched protein tyrosine phosphatase-STEPs toward understanding chronic stress-induced activation of corticotrophin releasing factor neurons in the rat bed nucleus of the stria terminalis". Biological Psychiatry. 74 (11): 817–26. doi:10.1016/j.biopsych.2013.07.032. PMC   3818357 . PMID   24012328.
  33. ↑ Goebel-Goody SM, Baum M, Paspalas CD, Fernandez SM, Carty NC, Kurup P, Lombroso PJ (Jan 2012). "Therapeutic implications for striatal-enriched protein tyrosine phosphatase (STEP) in neuropsychiatric disorders". Pharmacological Reviews. 64 (1): 65–87. doi:10.1124/pr.110.003053. PMC   3250079 . PMID   22090472.
  34. ↑ Karasawa T, Lombroso PJ (Dec 2014). "Disruption of striatal-enriched protein tyrosine phosphatase (STEP) function in neuropsychiatric disorders". Neuroscience Research. 89: 1–9. doi:10.1016/j.neures.2014.08.018. PMC   4259835 . PMID   25218562.
  35. ↑ Baguley TD, Xu HC, Chatterjee M, Nairn AC, Lombroso PJ, Ellman JA (Oct 2013). "Substrate-based fragment identification for the development of selective, nonpeptidic inhibitors of striatal-enriched protein tyrosine phosphatase". Journal of Medicinal Chemistry. 56 (19): 7636–50. doi:10.1021/jm401037h. PMC   3875168 . PMID   24083656.
  36. ↑ Baguley TD, Nairn AC, Lombroso PJ, Ellman JA (March 2015). "Synthesis of benzopentathiepin analogs and their evaluation as inhibitors of the phosphatase STEP". Bioorg. Med. Chem. Lett. 25 (5): 1044–6. doi:10.1016/j.bmcl.2015.01.020. PMC   4334692 . PMID   25666825.

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