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Article ; Online: Correction to: VEGF

Boudria, Asma / Faycal, Cherine Abou / Jia, Tao / Gout, Stephanie / Keramidas, Michelle / Didier, Chloé / Lemaître, Nicolas / Manet, Sandra / Coll, Jean-Luc / Toffart, Anne-Claire / Moro-Sibilot, Denis / Albiges-Rizo, Corinne / Josserand, Véronique / Faurobert, Eva / Brambilla, Christian / Brambilla, Elisabeth / Gazzeri, Sylvie / Eymin, Beatrice

Oncogene

2023 Volume 42, Issue 32, Page(s) 2471–2472

Language	English
Publishing date	2023-07-07
Publishing country	England
Document type	Published Erratum
ZDB-ID	639046-8
ISSN	1476-5594 ; 0950-9232
ISSN (online)	1476-5594
ISSN	0950-9232
DOI	10.1038/s41388-023-02764-w
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Article ; Online: The first water-soluble bowl complex: molecular recognition of acetate by the biomimetic tris(imidazole) Zn(II) system at pH 7.4.

Rat, Stéphanie / Gout, Jérôme / Bistri, Olivia / Reinaud, Olivia

Organic & biomolecular chemistry

2015 Volume 13, Issue 11, Page(s) 3194–3197

Abstract: A supramolecular approach for modeling active sites of metallo-enzymes relies on the association of a metal ion bound to a tris(imidazole) core under the control of a cavity. One step further is the water-solubilization of the cavity-complex. Here, we ... ...

Abstract	A supramolecular approach for modeling active sites of metallo-enzymes relies on the association of a metal ion bound to a tris(imidazole) core under the control of a cavity. One step further is the water-solubilization of the cavity-complex. Here, we describe the synthesis of a water-soluble bowl-ligand that has been successively achieved through an 11-step strategy from resorcinol. First insights into its coordination properties in water show that it readily binds Zn(II) at physiological pH and acts as a molecular receptor for the hydrophilic acetate guest ligand.
MeSH term(s)	Acetates/analysis ; Biomimetic Materials/chemical synthesis ; Biomimetic Materials/chemistry ; Hydrogen-Ion Concentration ; Imidazoles/chemistry ; Molecular Conformation ; Organometallic Compounds/chemical synthesis ; Organometallic Compounds/chemistry ; Solubility ; Water/chemistry ; Zinc/chemistry
Chemical Substances	Acetates ; Imidazoles ; Organometallic Compounds ; Water (059QF0KO0R) ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2015-03-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2097583-1
ISSN	1477-0539 ; 1477-0520
ISSN (online)	1477-0539
ISSN	1477-0520
DOI	10.1039/c4ob02514h
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Article: Role of cancer microenvironment in metastasis: focus on colon cancer.

Gout, Stéphanie / Huot, Jacques

Cancer microenvironment : official journal of the International Cancer Microenvironment Society

2008 Volume 1, Issue 1, Page(s) 69–83

Abstract: One person on three will receive a diagnostic of cancer during his life. About one third of them will die of the disease. In most cases, death will result from the formation of distal secondary sites called metastases. Several events that lead to cancer ... ...

Abstract	One person on three will receive a diagnostic of cancer during his life. About one third of them will die of the disease. In most cases, death will result from the formation of distal secondary sites called metastases. Several events that lead to cancer are under genetic control. In particular, cancer initiation is tightly associated with specific mutations that affect proto-oncogenes and tumour suppressor genes. These mutations lead to unrestrained growth of the primary neoplasm and a propensity to detach and to progress through the subsequent steps of metastatic dissemination. This process depends tightly on the surrounding microenvironment. In fact, several studies support the point that tumour development relies on a continuous cross-talk between cancer cells and their cellular and extracellular microenvironments. This signaling cross-talk is mediated by transmembrane receptors expressed on cancer cells and stromal cells. The aim of this manuscript is to review how the cancer microenvironment influences the journey of a metastatic cell taking liver invasion by colorectal cancer cells as a model.
Language	English
Publishing date	2008-03-14
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2422345-1
ISSN	1875-2284 ; 1875-2292
ISSN (online)	1875-2284
ISSN	1875-2292
DOI	10.1007/s12307-008-0007-2
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Article ; Online: RINT1 Regulates SUMOylation and the DNA Damage Response to Preserve Cellular Homeostasis in Pancreatic Cancer.

Cancer research

2021 Volume 81, Issue 7, Page(s) 1758–1774

Abstract: Pancreatic ductal adenocarcinoma (PDAC) still presents with a dismal prognosis despite intense research. Better understanding of cellular homeostasis could identify druggable targets to improve therapy. Here we propose RAD50-interacting protein 1 (RINT1) ...

Abstract	Pancreatic ductal adenocarcinoma (PDAC) still presents with a dismal prognosis despite intense research. Better understanding of cellular homeostasis could identify druggable targets to improve therapy. Here we propose RAD50-interacting protein 1 (RINT1) as an essential mediator of cellular homeostasis in PDAC. In a cohort of resected PDAC, low RINT1 protein expression correlated significantly with better survival. Accordingly, RINT1 depletion caused severe growth defects
MeSH term(s)	Animals ; Carcinoma, Pancreatic Ductal/genetics ; Carcinoma, Pancreatic Ductal/metabolism ; Carcinoma, Pancreatic Ductal/pathology ; Cell Cycle Proteins/physiology ; Cell Line, Tumor ; Cohort Studies ; DNA Damage/genetics ; DNA Repair/genetics ; Female ; Homeostasis/genetics ; Humans ; Mice ; Mice, Nude ; Mice, Transgenic ; Pancreatic Neoplasms/genetics ; Pancreatic Neoplasms/metabolism ; Pancreatic Neoplasms/pathology ; Protein Processing, Post-Translational/genetics ; Sumoylation/genetics
Chemical Substances	Cell Cycle Proteins ; RINT1 protein, human
Language	English
Publishing date	2021-02-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-20-2633
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Article: Selectins and selectin ligands in extravasation of cancer cells and organ selectivity of metastasis.

Gout, Stéphanie / Tremblay, Pierre-Luc / Huot, Jacques

Clinical & experimental metastasis

2008 Volume 25, Issue 4, Page(s) 335–344

Abstract: Metastatic spreading is a dreadful complication of neoplastic diseases that is responsible for most deaths due to cancer. It consists in the formation of secondary neoplasms from cancer cells that have detached from the primary site. The formation of ... ...

Abstract	Metastatic spreading is a dreadful complication of neoplastic diseases that is responsible for most deaths due to cancer. It consists in the formation of secondary neoplasms from cancer cells that have detached from the primary site. The formation of these secondary sites is not random and several clinical observations indicate that the metastatic colonization exhibits organ selectivity. This organ tropism relies mostly on the complementary adhesive interactions between the cancer cells and their microenvironment. In particular, several lines of evidence suggest that the organ selectivity of colon cancer cells for the liver involves the binding of the circulating cancer cells to endothelial E-selectin. The aim of this review is to make an integrative up-date of the mechanisms that govern the organ selectivity of the metastatic process focusing more especially on the role of selectins and selectin ligands.
MeSH term(s)	Animals ; Cell Adhesion ; Humans ; Ligands ; Neoplasm Metastasis ; Neoplastic Cells, Circulating ; Oligosaccharides/metabolism ; Organ Specificity ; Selectins/physiology
Chemical Substances	Ligands ; Oligosaccharides ; Selectins
Language	English
Publishing date	2008
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	604952-7
ISSN	0262-0898
ISSN	0262-0898
DOI	10.1007/s10585-007-9096-4
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Article ; Online: A new function of the splicing factor SRSF2 in the control of E2F1-mediated cell cycle progression in neuroendocrine lung tumors.

Edmond, Valerie / Merdzhanova, Galina / Gout, Stephanie / Brambilla, Elisabeth / Gazzeri, Sylvie / Eymin, Beatrice

Cell cycle (Georgetown, Tex.)

2013 Volume 12, Issue 8, Page(s) 1267–1278

Abstract: The transcription factor E2F1 belongs to the E2F family and plays a crucial role during cell cycle progression and apoptosis. Ser/Arg-Rich (SR) proteins are a family of RNA-binding phosphoproteins that control both constitutive and alternative pre-mRNA ... ...

Abstract	The transcription factor E2F1 belongs to the E2F family and plays a crucial role during cell cycle progression and apoptosis. Ser/Arg-Rich (SR) proteins are a family of RNA-binding phosphoproteins that control both constitutive and alternative pre-mRNA splicing events. We previously identified the SR protein SRSF2 as a new transcriptional target of E2F1 and demonstrated that both proteins cooperate to induce apoptosis in non-small cell lung carcinoma. In this study, we postulated that SRSF2 is also involved in the proliferative functions of E2F1. Using IHC, we first demonstrate that SRSF2 and its phosphorylated form (P-SRSF2) are overexpressed in neuroendocrine lung tumors that are highly proliferative tumors expressing high levels of E2F1. Importantly, we show a direct correlation between cyclin E, an E2F1-target gene controlling S phase, and P-SRSF2 proteins levels (p = 0.0083), suggesting a role of SRSF2 in E2F1-mediated cellular proliferation. Accordingly, using neuroendocrine lung carcinoma cell lines, we demonstrate that SRSF2 is a cell cycle-regulated protein involved in entry and progression into S phase. We also provide evidence that SRSF2 interacts with E2F1 and stimulates its transcriptional control of cell cycle target genes such as cyclin E. Finally, we show that inhibition of AKT signaling pathway prevents SRSF2 phosphorylation and activity toward E2F1 transcriptional function. Taken together, these results identify a new role of SRSF2 in the control of cell cycle progression and reinforce the functional link between SRSF2 and E2F1 proteins.
MeSH term(s)	Blotting, Western ; Carcinoma, Neuroendocrine/metabolism ; Carcinoma, Neuroendocrine/physiopathology ; Cell Line, Tumor ; Cyclin E/metabolism ; DNA Primers/genetics ; E2F1 Transcription Factor/metabolism ; Flow Cytometry ; Gene Expression Regulation, Neoplastic/physiology ; Humans ; Immunohistochemistry ; Luciferases ; Lung Neoplasms/metabolism ; Lung Neoplasms/physiopathology ; Nuclear Proteins/metabolism ; Phosphorylation ; RNA, Small Interfering/genetics ; Real-Time Polymerase Chain Reaction ; Reverse Transcriptase Polymerase Chain Reaction ; Ribonucleoproteins/metabolism ; S Phase/physiology ; Serine-Arginine Splicing Factors ; Signal Transduction/physiology
Chemical Substances	Cyclin E ; DNA Primers ; E2F1 Transcription Factor ; E2F1 protein, human ; Nuclear Proteins ; RNA, Small Interfering ; Ribonucleoproteins ; SRSF2 protein, human (147153-65-9) ; Serine-Arginine Splicing Factors (170974-22-8) ; Luciferases (EC 1.13.12.-)
Language	English
Publishing date	2013-03-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2146183-1
ISSN	1551-4005 ; 1538-4101 ; 1554-8627
ISSN (online)	1551-4005
ISSN	1538-4101 ; 1554-8627
DOI	10.4161/cc.24363
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Article: Death receptor-3, a new E-Selectin counter-receptor that confers migration and survival advantages to colon carcinoma cells by triggering p38 and ERK MAPK activation.

Gout, Stéphanie / Morin, Chantale / Houle, François / Huot, Jacques

Cancer research

2006 Volume 66, Issue 18, Page(s) 9117–9124

Abstract: E-selectin-mediated adhesion of colon cancer cells to endothelial cells is a key event in metastasis. However, the signaling mechanisms that confer metastatic advantages to cancer cells adhering to E-selectin are ill defined. By using affinity column ... ...

Abstract	E-selectin-mediated adhesion of colon cancer cells to endothelial cells is a key event in metastasis. However, the signaling mechanisms that confer metastatic advantages to cancer cells adhering to E-selectin are ill defined. By using affinity column chromatography and pull-down assays on purified membrane extracts of HT29 and LoVo cells coupled to mass spectrometry analysis, we obtained the first evidence indicating that E-selectin binds to death receptor-3 (DR3) expressed by the cancer cells. Thereafter, we accumulated several results, suggesting that DR3 is an E-selectin receptor on colon cancer cells and that its activation by E-selectin triggers the activation of p38 and extracellular signal-regulated kinase (ERK) mitogen-activated protein kinase (MAPK) and confers migration and survival advantages. First, by Western blotting, we found that the E-selectin-binding protein, identified as DR3, is recognized by two anti-DR3 antibodies. Second, the neutralization of DR3 with an antibody and its knockdown by small interfering RNA decrease the adhesion of colon cancer cells to E-selectin and E-selectin-expressing human umbilical vein endothelial cells. Third, inhibiting DR3 and knocking down its expression impair transendothelial migration of HT29 cells and block the activation of p38 and ERK by E-selectin. Fourth, high molecular weight isoforms of DR3 are expressed in samples of primary human colon carcinoma but not in samples from normal colon tissue. Intriguingly, DR3 is a death receptor but its activation by E-selectin does not induce apoptosis in colon cancer cells, except when ERK is inhibited. Our findings identify novel signaling and functional roles of DR3 activated in response to E-selectin and highlight the potential link between DR3 and metastasis.
MeSH term(s)	Apoptosis/physiology ; Cell Movement/physiology ; Cell Survival/physiology ; Colonic Neoplasms/enzymology ; Colonic Neoplasms/metabolism ; Colonic Neoplasms/pathology ; E-Selectin/metabolism ; Endothelial Cells/cytology ; Endothelial Cells/enzymology ; Endothelial Cells/metabolism ; Enzyme Activation ; Extracellular Signal-Regulated MAP Kinases/metabolism ; HT29 Cells ; Humans ; Receptors, Tumor Necrosis Factor, Member 25/metabolism ; p38 Mitogen-Activated Protein Kinases/metabolism
Chemical Substances	E-Selectin ; Receptors, Tumor Necrosis Factor, Member 25 ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2006-09-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-05-4605
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Article ; Online: Supramolecular control of a mononuclear biomimetic copper(II) center: bowl complexes vs funnel complexes.

Gout, Jérôme / Višnjevac, Aleksandar / Rat, Stéphanie / Parrot, Arnaud / Hessani, Assia / Bistri, Olivia / Le Poul, Nicolas / Le Mest, Yves / Reinaud, Olivia

Inorganic chemistry

2014 Volume 53, Issue 12, Page(s) 6224–6234

Abstract: Modeling the mononuclear site of copper enzymes is important for a better understanding of the factors controlling the reactivity of the metal center. A major difficulty stems from the difficult control of the nuclearity while maintaining free sites open ...

Abstract	Modeling the mononuclear site of copper enzymes is important for a better understanding of the factors controlling the reactivity of the metal center. A major difficulty stems from the difficult control of the nuclearity while maintaining free sites open to coordination of exogenous ligands. A supramolecular approach consists in associating a hydrophobic cavity to a tripodal ligand that will define the coordination spheres as well as access to the metal ion. Here, we describe the synthesis of a bowl Cu(II) complex based on the resorcinarene scaffold. This study supplements a previous work on Cu(I) coordination. It provides a complete picture of the cavity-copper system in its two oxidation states. The first XRD structure of such a bowl complex was obtained, evidencing a 5-coordinate Cu(II) ion with the three imidazole donors bound to the metal (two in the base of the pyramid, one in the apical position) and with an acetate anion, completing the base of the pyramid, and deeply included in the bowl. Solution studies conducted by EPR and UV-vis absorption spectroscopies as well as cyclic voltammetry highlighted interaction with coordinating solvents, various carboxylates that can sit either in the endo or in the exo position depending on their size as well as possible stabilization of hydroxo species in a mononuclear state. A comparison of the binding and redox properties of the bowl complex with funnel complexes based on the calix[6]arene core further highlights the importance of supramolecular features defining the first, second, and third coordination sphere for control of the metal ion.
MeSH term(s)	Biocatalysis ; Biomimetics ; Calixarenes/chemical synthesis ; Calixarenes/chemistry ; Coordination Complexes/chemical synthesis ; Coordination Complexes/chemistry ; Copper/chemistry ; Crystallography, X-Ray ; Models, Molecular ; Oxidation-Reduction ; Phenols/chemistry ; Phenylalanine/analogs & derivatives ; Phenylalanine/chemical synthesis ; Phenylalanine/chemistry
Chemical Substances	Coordination Complexes ; Phenols ; calix(6)arene ; resorcinarene ; Calixarenes (130036-26-9) ; Phenylalanine (47E5O17Y3R) ; Copper (789U1901C5)
Language	English
Publishing date	2014-06-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1484438-2
ISSN	1520-510X ; 0020-1669
ISSN (online)	1520-510X
ISSN	0020-1669
DOI	10.1021/ic500740r
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Article ; Online: Abnormal expression of the pre-mRNA splicing regulators SRSF1, SRSF2, SRPK1 and SRPK2 in non small cell lung carcinoma.

Gout, Stephanie / Brambilla, Elisabeth / Boudria, Asma / Drissi, Romain / Lantuejoul, Sylvie / Gazzeri, Sylvie / Eymin, Beatrice

PloS one

2012 Volume 7, Issue 10, Page(s) e46539

Abstract: Splicing abnormalities frequently occur in cancer. A key role as splice site choice regulator is played by the members of the SR (Ser/Arg-rich) family of proteins. We recently demonstrated that SRSF2 is involved in cisplatin-mediated apoptosis of human ... ...

Abstract	Splicing abnormalities frequently occur in cancer. A key role as splice site choice regulator is played by the members of the SR (Ser/Arg-rich) family of proteins. We recently demonstrated that SRSF2 is involved in cisplatin-mediated apoptosis of human lung carcinoma cell lines. In this study, by using immunohistochemistry, we demonstrate that the SR proteins SRSF1 and SRSF2 are overexpressed in 63% and 65% of lung adenocarcinoma (ADC) as well as in 68% and 91% of squamous cell lung carcinoma (SCC), respectively, compared to normal lung epithelial cells. In addition, we show that SRSF2 overexpression correlates with high level of phosphorylated SRSF2 in both ADC (p<0.0001) and SCC (p = 0.02), indicating that SRSF2 mostly accumulates under a phosphorylated form in lung tumors. Consistently, we further show that the SR-phosphorylating kinases SRPK1 and SRPK2 are upregulated in 92% and 94% of ADC as well as in 72% and 68% of SCC, respectively. P-SRSF2 and SRPK2 scores are correlated in ADC (p = 0.01). Using lung adenocarcinoma cell lines, we demonstrate that SRSF1 overexpression leads to a more invasive phenotype, evidenced by activation of PI3K/AKT and p42/44MAPK signaling pathways, increased growth capacity in soft agar, acquisition of mesenchymal markers such as E cadherin loss, vimentin and fibronectin gain, and increased resistance to chemotherapies. Finally, we provide evidence that high levels of SRSF1 and P-SRSF2 proteins are associated with extensive stage (III-IV) in ADC. Taken together, these results indicate that a global deregulation of pre-mRNA splicing regulators occurs during lung tumorigenesis and does not predict same outcome in both Non Small Cell Lung Carcinoma histological sub-types, likely contributing to a more aggressive phenotype in adenocarcinoma.
MeSH term(s)	Adenocarcinoma/metabolism ; Adenocarcinoma/pathology ; Aged ; Antineoplastic Agents/pharmacology ; Carboplatin/pharmacology ; Carcinoma, Non-Small-Cell Lung/metabolism ; Carcinoma, Non-Small-Cell Lung/pathology ; Carcinoma, Squamous Cell/metabolism ; Carcinoma, Squamous Cell/pathology ; Cell Line, Tumor ; Drug Resistance, Neoplasm ; Female ; Gene Expression ; Gene Expression Regulation, Neoplastic ; Humans ; Lung/metabolism ; Lung Neoplasms/metabolism ; Lung Neoplasms/pathology ; Male ; Middle Aged ; Neoplasm Staging ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Paclitaxel/pharmacology ; Phenotype ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Ribonucleoproteins/genetics ; Ribonucleoproteins/metabolism ; Serine-Arginine Splicing Factors ; Signal Transduction
Chemical Substances	Antineoplastic Agents ; Nuclear Proteins ; Phosphoproteins ; RNA-Binding Proteins ; Ribonucleoproteins ; SRSF2 protein, human (147153-65-9) ; Serine-Arginine Splicing Factors (170974-22-8) ; Carboplatin (BG3F62OND5) ; SRPK1 protein, human (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; SRPK2 protein, human (EC 2.7.11.1) ; Paclitaxel (P88XT4IS4D)
Language	English
Publishing date	2012-10-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0046539
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Article ; Online: VEGF

Boudria, Asma / Abou Faycal, Cherine / Jia, Tao / Gout, Stephanie / Keramidas, Michelle / Didier, Chloé / Lemaître, Nicolas / Manet, Sandra / Coll, Jean-Luc / Toffart, Anne-Claire / Moro-Sibilot, Denis / Albiges-Rizo, Corinne / Josserand, Véronique / Faurobert, Eva / Brambilla, Christian / Brambilla, Elisabeth / Gazzeri, Sylvie / Eymin, Beatrice

Oncogene

2018 Volume 38, Issue 7, Page(s) 1050–1066

Abstract: Vascular endothelial growth factor-A (VEGF-A) is highly subjected to alternative pre-mRNA splicing that generates several splice variants. The ... ...

Abstract	Vascular endothelial growth factor-A (VEGF-A) is highly subjected to alternative pre-mRNA splicing that generates several splice variants. The VEGF
MeSH term(s)	Alternative Splicing ; Angiogenesis Inhibitors/pharmacology ; Autocrine Communication/drug effects ; Bevacizumab/pharmacology ; Carcinoma, Non-Small-Cell Lung/drug therapy ; Carcinoma, Non-Small-Cell Lung/genetics ; Carcinoma, Non-Small-Cell Lung/metabolism ; Carcinoma, Non-Small-Cell Lung/pathology ; Female ; Humans ; Integrin beta1/genetics ; Integrin beta1/metabolism ; Lung Neoplasms/drug therapy ; Lung Neoplasms/genetics ; Lung Neoplasms/metabolism ; Lung Neoplasms/pathology ; Male ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Neovascularization, Pathologic/drug therapy ; Neovascularization, Pathologic/genetics ; Neovascularization, Pathologic/metabolism ; Neovascularization, Pathologic/pathology ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Receptors, Vascular Endothelial Growth Factor/genetics ; Receptors, Vascular Endothelial Growth Factor/metabolism ; Signal Transduction/drug effects ; Vascular Endothelial Growth Factor A/genetics ; Vascular Endothelial Growth Factor A/metabolism
Chemical Substances	Angiogenesis Inhibitors ; Integrin beta1 ; Neoplasm Proteins ; Protein Isoforms ; VEGFA protein, human ; Vascular Endothelial Growth Factor A ; Bevacizumab (2S9ZZM9Q9V) ; Receptors, Vascular Endothelial Growth Factor (EC 2.7.10.1)
Language	English
Publishing date	2018-09-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639046-8
ISSN	1476-5594 ; 0950-9232
ISSN (online)	1476-5594
ISSN	0950-9232
DOI	10.1038/s41388-018-0486-7
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