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Article ; Online: Homogeneous Dual-Parametric-Coupled Assay for Simultaneous Nucleotide Exchange and KRAS/RAF-RBD Interaction Monitoring.

Kopra, Kari / Vuorinen, Emmiliisa / Abreu-Blanco, Maria / Wang, Qi / Eskonen, Ville / Gillette, William / Pulliainen, Arto T / Holderfield, Matthew / Härmä, Harri

Analytical chemistry

2020 Volume 92, Issue 7, Page(s) 4971–4979

Abstract: We have developed a rapid and sensitive single-well dual-parametric method introduced in linked RAS nucleotide exchange and RAS/RAF-RBD interaction assays. RAS mutations are frequent drivers of multiple different human cancers, but the development of ... ...

Abstract	We have developed a rapid and sensitive single-well dual-parametric method introduced in linked RAS nucleotide exchange and RAS/RAF-RBD interaction assays. RAS mutations are frequent drivers of multiple different human cancers, but the development of therapeutic strategies has been challenging. Traditionally, efforts to disrupt the RAS function have focused on nucleotide exchange inhibitors, GTP-RAS interaction inhibitors, and activators increasing GTPase activity of mutant RAS proteins. As the amount of biological knowledge grows, targeted biochemical assays enabling high-throughput screening have become increasingly interesting. We have previously introduced a homogeneous quenching resonance energy transfer (QRET) assay for nucleotide binding studies with RAS and heterotrimeric G proteins. Here, we introduce a novel homogeneous signaling technique called QTR-FRET, which combine QRET technology and time-resolved Förster resonance energy transfer (TR-FRET). The dual-parametric QTR-FRET technique enables the linking of guanine nucleotide exchange factor-induced Eu
MeSH term(s)	Fluorescence Resonance Energy Transfer ; Guanine Nucleotide Exchange Factors/chemistry ; Guanine Nucleotide Exchange Factors/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Proto-Oncogene Proteins c-raf/chemistry ; Proto-Oncogene Proteins c-raf/metabolism ; Proto-Oncogene Proteins p21(ras)/chemistry ; Proto-Oncogene Proteins p21(ras)/genetics ; Proto-Oncogene Proteins p21(ras)/metabolism
Chemical Substances	Guanine Nucleotide Exchange Factors ; KRAS protein, human ; Guanosine Triphosphate (86-01-1) ; Proto-Oncogene Proteins c-raf (EC 2.7.11.1) ; Proto-Oncogene Proteins p21(ras) (EC 3.6.5.2)
Language	English
Publishing date	2020-03-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.9b05126
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Article ; Online: Label-Free Time-Gated Luminescent Detection Method for the Nucleotides with Varying Phosphate Content.

Kopra, Kari / Seppälä, Tanja / Rabara, Dana / Abreu-Blanco, Maria / Kulmala, Sakari / Holderfield, Matthew / Härmä, Harri

Sensors (Basel, Switzerland)

2018 Volume 18, Issue 11

Abstract: A new label-free molecular probe for luminescent nucleotide detection in neutral aqueous solution is presented. Phosphate-containing molecules, such as nucleotides possess vital role in cell metabolism, energy economy, and various signaling processes. ... ...

Abstract	A new label-free molecular probe for luminescent nucleotide detection in neutral aqueous solution is presented. Phosphate-containing molecules, such as nucleotides possess vital role in cell metabolism, energy economy, and various signaling processes. Thus, the monitoring of nucleotide concentration and nucleotide related enzymatic reactions is of high importance. Two component lanthanide complex formed from Tb(III) ion carrier and light harvesting antenna, readily distinguishes nucleotides containing different number of phosphates and enable direct detection of enzymatic reactions converting nucleotide triphosphate (NTP) to nucleotide di/monophosphate or the opposite. Developed sensor enables the detection of enzymatic activity with a low nanomolar sensitivity, as highlighted with K-Ras and apyrase enzymes in their hydrolysis assays performed in a high throughput screening compatible 384-well plate format.
Language	English
Publishing date	2018-11-16
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2052857-7
ISSN	1424-8220 ; 1424-8220
ISSN (online)	1424-8220
ISSN	1424-8220
DOI	10.3390/s18113989
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Article ; Online: Crosstalk between vascular endothelial growth factor, notch, and transforming growth factor-beta in vascular morphogenesis.

Holderfield, Matthew T / Hughes, Christopher C W

Circulation research

2008 Volume 102, Issue 6, Page(s) 637–652

Abstract: Vascular morphogenesis encompasses a temporally regulated set of morphological changes that endothelial cells undergo to generate a network of interconnected tubules. Such a complex process inevitably involves multiple cell signaling pathways that must ... ...

Abstract	Vascular morphogenesis encompasses a temporally regulated set of morphological changes that endothelial cells undergo to generate a network of interconnected tubules. Such a complex process inevitably involves multiple cell signaling pathways that must be tightly coordinated in time and space. The formation of a new capillary involves endothelial cell activation, migration, alignment, proliferation, tube formation, branching, anastomosis, and maturation of intercellular junctions and the surrounding basement membrane. Each of these stages is either known or suspected to fall under the influence of the vascular endothelial growth factor, notch, and transforming growth factor-beta/bone morphogenetic protein signaling pathways. Vascular endothelial growth factor is essential for initiation of angiogenic sprouting, and also regulates migration of capillary tip cells, proliferation of trunk cells, and gene expression in both. Notch has been implicated in the regulation of cell fate decisions in the vasculature, especially the choice between arterial and venular endothelial cells, and between tip and trunk cell phenotype. Transforming growth factor-beta regulates cell migration and proliferation, as well as matrix synthesis. In this review, we emphasize how crosstalk between these pathways is essential for proper patterning of the vasculature and offer a transcriptional oscillator model to explain how these pathways might interact to generate new tip cells during retinal angiogenesis.
MeSH term(s)	Animals ; Capillaries/embryology ; Capillaries/metabolism ; Endothelial Cells/metabolism ; Feedback, Physiological ; Humans ; Morphogenesis ; Neovascularization, Physiologic ; Receptors, Notch/metabolism ; Retinal Vessels/embryology ; Retinal Vessels/metabolism ; Signal Transduction ; Time Factors ; Transforming Growth Factor beta/metabolism ; Vascular Endothelial Growth Factor A/metabolism
Chemical Substances	Receptors, Notch ; Transforming Growth Factor beta ; Vascular Endothelial Growth Factor A
Language	English
Publishing date	2008-03-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/CIRCRESAHA.107.167171
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Article ; Online: Inhibition of Ras/Raf/MEK/ERK Pathway Signaling by a Stress-Induced Phospho-Regulatory Circuit.

Ritt, Daniel A / Abreu-Blanco, María T / Bindu, Lakshman / Durrant, David E / Zhou, Ming / Specht, Suzanne I / Stephen, Andrew G / Holderfield, Matthew / Morrison, Deborah K

Molecular cell

2016 Volume 64, Issue 5, Page(s) 875–887

Abstract: Ras pathway signaling plays a critical role in cell growth control and is often upregulated in human cancer. The Raf kinases selectively interact with GTP-bound Ras and are important effectors of Ras signaling, functioning as the initiating kinases in ... ...

Abstract	Ras pathway signaling plays a critical role in cell growth control and is often upregulated in human cancer. The Raf kinases selectively interact with GTP-bound Ras and are important effectors of Ras signaling, functioning as the initiating kinases in the ERK cascade. Here, we identify a route for the phospho-inhibition of Ras/Raf/MEK/ERK pathway signaling that is mediated by the stress-activated JNK cascade. We find that key Ras pathway components, the RasGEF Sos1 and the Rafs, are phosphorylated on multiple S/TP sites in response to JNK activation and that the hyperphosphorylation of these sites renders the Rafs and Sos1 unresponsive to upstream signals. This phospho-regulatory circuit is engaged by cancer therapeutics, such as rigosertib and paclitaxel/Taxol, that activate JNK through mitotic and oxidative stress as well as by physiological regulators of the JNK cascade and may function as a signaling checkpoint to suppress the Ras pathway during conditions of cellular stress.
MeSH term(s)	Enzyme Activation/drug effects ; Glycine/analogs & derivatives ; Glycine/pharmacokinetics ; Glycine/pharmacology ; HeLa Cells ; Humans ; JNK Mitogen-Activated Protein Kinases/metabolism ; MAP Kinase Signaling System/drug effects ; Oxidative Stress ; Paclitaxel/pharmacokinetics ; Paclitaxel/pharmacology ; Phosphorylation ; Proto-Oncogene Proteins B-raf/metabolism ; Proto-Oncogene Proteins c-raf/metabolism ; Sulfones/pharmacokinetics ; Sulfones/pharmacology ; ras Proteins/metabolism
Chemical Substances	Sulfones ; ON 01910 (67DOW7F9GL) ; Proto-Oncogene Proteins B-raf (EC 2.7.11.1) ; Proto-Oncogene Proteins c-raf (EC 2.7.11.1) ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; ras Proteins (EC 3.6.5.2) ; Paclitaxel (P88XT4IS4D) ; Glycine (TE7660XO1C)
Language	English
Publishing date	2016-11-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, N.I.H., Extramural
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2016.10.029
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Article ; Online: Targeted mass spectrometry-based assays enable multiplex quantification of receptor tyrosine kinase, MAP Kinase, and AKT signaling.

Whiteaker, Jeffrey R / Sharma, Kanika / Hoffman, Melissa A / Kuhn, Eric / Zhao, Lei / Cocco, Alexandra R / Schoenherr, Regine M / Kennedy, Jacob J / Voytovich, Ulianna / Lin, Chenwei / Fang, Bin / Bowers, Kiah / Whiteley, Gordon / Colantonio, Simona / Bocik, William / Roberts, Rhonda / Hiltke, Tara / Boja, Emily / Rodriguez, Henry /

McCormick, Frank / Holderfield, Matthew / Carr, Steven A / Koomen, John M / Paulovich, Amanda G

Cell reports methods

2021 Volume 1, Issue 3

Abstract: Summary: A primary goal of the US National Cancer Institute's Ras initiative at the Frederick National Laboratory for Cancer Research is to develop methods to quantify RAS signaling to facilitate development of novel cancer therapeutics. We use targeted ...

Abstract	Summary: A primary goal of the US National Cancer Institute's Ras initiative at the Frederick National Laboratory for Cancer Research is to develop methods to quantify RAS signaling to facilitate development of novel cancer therapeutics. We use targeted proteomics technologies to develop a community resource consisting of 256 validated multiple reaction monitoring (MRM)-based, multiplexed assays for quantifying protein expression and phosphorylation through the receptor tyrosine kinase, MAPK, and AKT signaling networks. As proof of concept, we quantify the response of melanoma (A375 and SK-MEL-2) and colorectal cancer (HCT-116 and HT-29) cell lines to BRAF inhibition by PLX-4720. These assays replace over 60 Western blots with quantitative mass spectrometry-based assays of high molecular specificity and quantitative precision, showing the value of these methods for pharmacodynamic measurements and mechanism of action studies. Methods, fit-for-purpose validation, and results are publicly available as a resource for the community at assays.cancer.gov. Motivation: A lack of quantitative, multiplexable assays for phosphosignaling limits comprehensive investigation of aberrant signaling in cancer and evaluation of novel treatments. To alleviate this limitation, we sought to develop assays using targeted mass spectrometry for quantifying protein expression and phosphorylation through the receptor tyrosine kinase, MAPK, and AKT signaling networks. The resulting assays provide a resource for replacing over 60 Western blots in examining cancer signaling and tumor biology with high molecular specificity and quantitative rigor.
MeSH term(s)	Humans ; Proto-Oncogene Proteins c-akt/metabolism ; Mass Spectrometry/methods ; Receptor Protein-Tyrosine Kinases ; Melanoma ; Mitogen-Activated Protein Kinase Kinases ; Tyrosine
Chemical Substances	Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; Mitogen-Activated Protein Kinase Kinases (EC 2.7.12.2) ; Tyrosine (42HK56048U)
Language	English
Publishing date	2021-06-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ISSN	2667-2375
ISSN (online)	2667-2375
DOI	10.1016/j.crmeth.2021.100015
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Article ; Online: Tumor-selective activity of RAS-GTP inhibition in pancreatic cancer.

Wasko, Urszula N / Jiang, Jingjing / Dalton, Tanner C / Curiel-Garcia, Alvaro / Edwards, A Cole / Wang, Yingyun / Lee, Bianca / Orlen, Margo / Tian, Sha / Stalnecker, Clint A / Drizyte-Miller, Kristina / Menard, Marie / Dilly, Julien / Sastra, Stephen A / Palermo, Carmine F / Hasselluhn, Marie C / Decker-Farrell, Amanda R / Chang, Stephanie / Jiang, Lingyan /

Wei, Xing / Yang, Yu C / Helland, Ciara / Courtney, Haley / Gindin, Yevgeniy / Muonio, Karl / Zhao, Ruiping / Kemp, Samantha B / Clendenin, Cynthia / Sor, Rina / Vostrejs, William P / Hibshman, Priya S / Amparo, Amber M / Hennessey, Connor / Rees, Matthew G / Ronan, Melissa M / Roth, Jennifer A / Brodbeck, Jens / Tomassoni, Lorenzo / Bakir, Basil / Socci, Nicholas D / Herring, Laura E / Barker, Natalie K / Wang, Junning / Cleary, James M / Wolpin, Brian M / Chabot, John A / Kluger, Michael D / Manji, Gulam A / Tsai, Kenneth Y / Sekulic, Miroslav / Lagana, Stephen M / Califano, Andrea / Quintana, Elsa / Wang, Zhengping / Smith, Jacqueline A M / Holderfield, Matthew / Wildes, David / Lowe, Scott W / Badgley, Michael A / Aguirre, Andrew J / Vonderheide, Robert H / Stanger, Ben Z / Baslan, Timour / Der, Channing J / Singh, Mallika / Olive, Kenneth P

Nature

2024

Abstract: Broad-spectrum RAS inhibition holds the potential to benefit roughly a quarter of human cancer patients whose tumors are driven by RAS ... ...

Abstract	Broad-spectrum RAS inhibition holds the potential to benefit roughly a quarter of human cancer patients whose tumors are driven by RAS mutations
Language	English
Publishing date	2024-04-08
Publishing country	England
Document type	Journal Article
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-024-07379-z
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Article: Tumor-selective effects of active RAS inhibition in pancreatic ductal adenocarcinoma.

Wasko, Urszula N / Jiang, Jingjing / Curiel-Garcia, Alvaro / Wang, Yingyun / Lee, Bianca / Orlen, Margo / Drizyte-Miller, Kristina / Menard, Marie / Dilly, Julien / Sastra, Stephen A / Palermo, Carmine F / Dalton, Tanner / Hasselluhn, Marie C / Decker-Farrell, Amanda R / Chang, Stephanie / Jiang, Lingyan / Wei, Xing / Yang, Yu C / Helland, Ciara /

Courtney, Haley / Gindin, Yevgeniy / Zhao, Ruiping / Kemp, Samantha B / Clendenin, Cynthia / Sor, Rina / Vostrejs, Will / Amparo, Amber A / Hibshman, Priya S / Rees, Matthew G / Ronan, Melissa M / Roth, Jennifer A / Bakir, Basil / Badgley, Michael A / Chabot, John A / Kluger, Michael D / Manji, Gulam A / Quintana, Elsa / Wang, Zhengping / Smith, Jacqueline A M / Holderfield, Matthew / Wildes, David / Aguirre, Andrew J / Der, Channing J / Vonderheide, Robert H / Stanger, Ben Z / Singh, Mallika / Olive, Kenneth P

bioRxiv : the preprint server for biology

2023

Abstract: Broad-spectrum RAS inhibition holds the potential to benefit roughly a quarter of human cancer patients whose tumors are driven by RAS mutations. However, the impact of inhibiting RAS functions in normal tissues is not known. RMC-7977 is a highly ... ...

Abstract	Broad-spectrum RAS inhibition holds the potential to benefit roughly a quarter of human cancer patients whose tumors are driven by RAS mutations. However, the impact of inhibiting RAS functions in normal tissues is not known. RMC-7977 is a highly selective inhibitor of the active (GTP-bound) forms of KRAS, HRAS, and NRAS, with affinity for both mutant and wild type (WT) variants. As >90% of human pancreatic ductal adenocarcinoma (PDAC) cases are driven by activating mutations in
Language	English
Publishing date	2023-12-04
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.12.03.569791
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Article: Inhibition of Ras/Raf/MEK/ERK Pathway Signaling by a Stress-Induced Phospho-Regulatory Circuit

Ritt, Daniel A / Andrew G. Stephen / David E. Durrant / Deborah K. Morrison / Lakshman Bindu / María T. Abreu-Blanco / Matthew Holderfield / Ming Zhou / Suzanne I. Specht

Molecular cell. 2016 Dec. 01, v. 64, no. 5

2016

Abstract	Ras pathway signaling plays a critical role in cell growth control and is often upregulated in human cancer. The Raf kinases selectively interact with GTP-bound Ras and are important effectors of Ras signaling, functioning as the initiating kinases in the ERK cascade. Here, we identify a route for the phospho-inhibition of Ras/Raf/MEK/ERK pathway signaling that is mediated by the stress-activated JNK cascade. We find that key Ras pathway components, the RasGEF Sos1 and the Rafs, are phosphorylated on multiple S/TP sites in response to JNK activation and that the hyperphosphorylation of these sites renders the Rafs and Sos1 unresponsive to upstream signals. This phospho-regulatory circuit is engaged by cancer therapeutics, such as rigosertib and paclitaxel/Taxol, that activate JNK through mitotic and oxidative stress as well as by physiological regulators of the JNK cascade and may function as a signaling checkpoint to suppress the Ras pathway during conditions of cellular stress.
Keywords	cell growth ; humans ; mitogen-activated protein kinase ; mitosis ; neoplasms ; oxidative stress ; paclitaxel ; signal transduction ; therapeutics
Language	English
Dates of publication	2016-1201
Size	p. 875-887.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2016.10.029
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Interferon-induced transmembrane protein 1 regulates endothelial lumen formation during angiogenesis.

Popson, Stephanie A / Ziegler, Mary E / Chen, Xiaofang / Holderfield, Matthew T / Shaaban, Cameron I / Fong, Ashley H / Welch-Reardon, Katrina M / Papkoff, Jackie / Hughes, Christopher C W

Arteriosclerosis, thrombosis, and vascular biology

2014 Volume 34, Issue 5, Page(s) 1011–1019

Abstract: Objective: It is well established that angiogenesis is a complex and coordinated multistep process. However, there remains a lack of information about the genes that regulate individual stages of vessel formation. Here, we aimed to define the role of ... ...

Abstract	Objective: It is well established that angiogenesis is a complex and coordinated multistep process. However, there remains a lack of information about the genes that regulate individual stages of vessel formation. Here, we aimed to define the role of human interferon-induced transmembrane protein 1 (IFITM1) during blood vessel formation. Approach and results: We identified IFITM1 in a microarray screen for genes differentially regulated by endothelial cells (ECs) during an in vitro angiogenesis assay and found that IFITM1 expression was strongly induced as ECs sprouted and formed lumens. We showed by immunohistochemistry that human IFITM1 was expressed by stable blood vessels in multiple organs. siRNA-mediated knockdown of IFITM1 expression spared EC sprouting but completely disrupted lumen formation, in both in vitro and in an in vivo xeno-transplant model. ECs lacking IFITM1 underwent early stages of lumenogenesis (ie, intracellular vacuole formation) but failed to mature or expand lumens. Coimmunoprecipitation studies confirmed occludin as an IFITM1 binding partner in ECs, and immunocytochemistry showed a lack of occludin at endothelial tight junctions in the absence of IFITM1. Finally, time-lapse video microscopy revealed that IFITM1 is required for the formation of stable cell-cell contacts during endothelial lumen formation. Conclusions: IFITM1 is essential for the formation of functional blood vessels and stabilizes EC-EC interactions during endothelial lumen formation by regulating tight junction assembly.
MeSH term(s)	Animals ; Antigens, Differentiation/genetics ; Antigens, Differentiation/metabolism ; Cells, Cultured ; Gene Expression Profiling/methods ; Human Umbilical Vein Endothelial Cells/metabolism ; Human Umbilical Vein Endothelial Cells/transplantation ; Humans ; Immunoprecipitation ; Mice ; Mice, Inbred ICR ; Mice, SCID ; Microscopy, Video ; Neovascularization, Physiologic ; Occludin/metabolism ; Oligonucleotide Array Sequence Analysis ; Protein Binding ; RNA Interference ; Signal Transduction ; Tight Junctions/metabolism ; Time Factors ; Time-Lapse Imaging ; Transfection
Chemical Substances	Antigens, Differentiation ; OCLN protein, human ; Occludin ; leu-13 antigen
Language	English
Publishing date	2014-03-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ZDB-ID	1221433-4
ISSN	1524-4636 ; 1079-5642
ISSN (online)	1524-4636
ISSN	1079-5642
DOI	10.1161/ATVBAHA.114.303352
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Article: HESR1/CHF2 suppresses VEGFR2 transcription independent of binding to E-boxes.

Holderfield, Matthew T / Henderson Anderson, April M / Kokubo, Hiroki / Chin, Michael T / Johnson, Randy L / Hughes, Christopher C W

Biochemical and biophysical research communications

2006 Volume 346, Issue 3, Page(s) 637–648

Abstract: The bHLH transcription factor HESR1 (CHF2) acts downstream of notch to regulate cardiovascular development and angiogenesis, at least in part through down-regulation of the VEGF receptor, VEGFR2. Surprisingly, we find that HESR1 interacts with the ... ...

Abstract	The bHLH transcription factor HESR1 (CHF2) acts downstream of notch to regulate cardiovascular development and angiogenesis, at least in part through down-regulation of the VEGF receptor, VEGFR2. Surprisingly, we find that HESR1 interacts with the promoter in endothelial cells (EC) not through direct binding to the E-boxes, but through intermediary interactions with GC-box-binding proteins. The bHLH and orange domains of HESR1 are sufficient for repression in EC, likely through recruitment of co-repressors, however, the C-terminal YRPW motif is not required. The VEGFR2 promoter contains a functional initiator element but no TATA box, however, addition of a TATA sequence renders the promoter resistant to inhibition by HESR1. In agreement with this finding, the NrCAM, TK, and CMV promoters, which have TATA boxes, cannot be repressed. Thus, HESR1 represses VEGFR2 through interactions with SP-1-like factors and requires an Inr element in the absence of a TATA box. Our findings illuminate an important mechanism for notch/HESR1 regulation of VEGF-induced angiogenesis.
MeSH term(s)	Base Sequence ; Basic Helix-Loop-Helix Transcription Factors/genetics ; Basic Helix-Loop-Helix Transcription Factors/metabolism ; Cells, Cultured ; Endothelial Cells/metabolism ; Humans ; Mutation/genetics ; Promoter Regions, Genetic/genetics ; Protein Binding ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Transcription, Genetic/genetics ; Vascular Endothelial Growth Factor Receptor-2/genetics ; Vascular Endothelial Growth Factor Receptor-2/metabolism
Chemical Substances	Basic Helix-Loop-Helix Transcription Factors ; Hairy, HRT1 protein ; Repressor Proteins ; Vascular Endothelial Growth Factor Receptor-2 (EC 2.7.10.1)
Language	English
Publishing date	2006-08-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2006.05.177
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