Nature Search

A human osteosarcoma cell line secretes a growth factor structurally related to a homodimer of PDGF A-chains

Carl-Henrik Heldin
Ann Johnsson
Bengt Westermark
Research06 Feb 1986
Nature

Volume: 319, P: 511-514
cDNA sequence and chromosomal localization of human platelet-derived growth factor A-chain and its expression in tumour cell lines

Christer Betsholtz
Ann Johnsson
James Scott
Research24 Apr 1986
Nature

Volume: 320, P: 695-699
Possible positive autocrine feedback in the prereplicative phase of human fibroblasts

Ylva Paulsson
Annet Hammacher
Bengt Westermark
Research20 Aug 1987
Nature

Volume: 328, P: 715-717
Platelet-derived growth factor is structurally related to the putative transforming protein p28^sis of simian sarcoma virus

Michael D. Waterfield
Geoffrey T. Scrace
Thomas F. Deuel
Research01 Jul 1983
Nature

Volume: 304, P: 35-39
Stimulation of tyrosine-specific phosphorylation by platelet-derived growth factor

Bo Ek
Bengt Westermark
Carl-Henrik Heldin
Research04 Feb 1982
Nature

Volume: 295, P: 419-420
Antibodies against platelet-derived growth factor inhibit acute transformation by simian sarcoma virus

Ann Johnsson
Christer Betsholtz
Bengt Westermark
Research03 Oct 1985
Nature

Volume: 317, P: 438-440
Identification of Tyr-762 in the platelet-derived growth factor α-receptor as the binding site for Crk proteins

Koutaro Yokote
Ulf Hellman
Seijiro Mori
Research19 Mar 1998
Oncogene

Volume: 16, P: 1229-1239
Activation of Stat5 by platelet-derived growth factor (PDGF) is dependent on phosphorylation sites in PDGF β-receptor juxtamembrane and kinase insert domains

Sigrídur Valgeirsdóttir
Kirsi Paukku
Lena Claesson-Welsh
Research03 Feb 1998
Oncogene

Volume: 16, P: 505-515
Identification of angiogenic activity and the cloning and expression of platelet-derived endothelial cell growth factor

Fuyuki Ishikawa
Kohei Miyazono
Carl-Henrik Heldin
Research13 Apr 1989
Nature

Volume: 338, P: 557-562
Role for carbohydrate structures inTGF-β1 latency

Kohel Miyazono
Carl-Henrik Heldin
Research09 Mar 1989
Nature

Volume: 338, P: 158-160
The European Research Council — a new opportunity for European science

During recent decades, the lack of appropriate funding has made it difficult for European basic research to compete with research in North America and parts of Asia. The establishment of the European Research Council promises new opportunities to boost European science.

Carl-Henrik Heldin
Comments & Opinion01 May 2008
Nature Reviews Molecular Cell Biology

Volume: 9, P: 417-420
Tony Pawson 1952–2013

Carl-Henrik Heldin
John Scott
Comments & Opinion01 Oct 2013
Nature Cell Biology

Volume: 15, P: 1134
Identification of Smad7, a TGFβ-inducible antagonist of TGF-β signalling

Atsuhito Nakao
Mozhgan Afrakhte
Peter ten Dijke
Research09 Oct 1997
Nature

Volume: 389, P: 631-635
Increased mitogenicity of an αβ heterodimeric PDGF receptor complex correlates with lack of RasGAP binding

Simon Ekman
Eva Rupp Thuresson
Lars Rönnstrand
Research15 Apr 1999
Oncogene

Volume: 18, P: 2481-2488
SHP-2 is involved in heterodimer specific loss of phosphorylation of Tyr771 in the PDGF β-receptor

Simon Ekman
Anders Kallin
Lars Rönnstrand
Research13 Mar 2002
Oncogene

Volume: 21, P: 1870-1875
Characterization of the chronic myelomonocytic leukemia associated TEL-PDGFβR fusion protein

Tobias Sjöblom
Anthony Boureux
Arne Östman
Research30 Nov 1999
Oncogene

Volume: 18, P: 7055-7062
PDGF-D is a specific, protease-activated ligand for the PDGF β-receptor

Erika Bergsten
Marko Uutela
Ulf Eriksson
Research11 Apr 2001
Nature Cell Biology

Volume: 3, P: 512-516
Loss of SNAI1 induces cellular plasticity in invasive triple-negative breast cancer cells

Chrysoula Tsirigoti
Mohamad Moustafa Ali
Aristidis Moustakas
ResearchOpen Access28 Sept 2022
Cell Death & Disease

Volume: 13, P: 1-17
SMAD destruction turns off signalling

Carl-Henrik Heldin
Peter ten Dijke
News & Views01 Dec 1999
Nature Cell Biology

Volume: 1, P: E195-E197
An anchor for activation

The first step in signalling through the transforming growth factor (TGF)-β pathway involves phosphorylation of either Smad2 or Smad3 by an activated type-I receptor kinase. How do TGF-β, the receptor and the Smad manage to meet up? The answer is a newly discovered ‘anchor’ protein termed SARA, which recruits the Smads to the TGF-β receptor.

Peter ten Dijke
Carl-Henrik Heldin
News & Views14 Jan 1999
Nature

Volume: 397, P: 109-111
The nuts and bolts of IRF structure

The new crystal structure of the IRF-3 transactivation domain reveals an evolutionarily conserved protein domain whose activity is modulated by phosphorylation controlling oligomerization and protein-protein interactions.

Aristidis Moustakas
Carl-Henrik Heldin
News & Views01 Nov 2003
Nature Structural & Molecular Biology

Volume: 10, P: 874-876
High interstitial fluid pressure — an obstacle in cancer therapy

Carl-Henrik Heldin
Kristofer Rubin
Arne Östman
Reviews01 Oct 2004
Nature Reviews Cancer

Volume: 4, P: 806-813
TRAF6 ubiquitinates TGFβ type I receptor to promote its cleavage and nuclear translocation in cancer

TGFβ can function as both a tumour suppressor and tumour promoter under different cellular contexts. Here, the cleavage product of the TGFβ type I receptor is shown to be generated in a TGFβ-dependent manner, and can induce the expression of genes involved in tumour cell invasion.

Yabing Mu
Reshma Sundar
Marene Landström
ResearchOpen Access31 May 2011
Nature Communications

Volume: 2, P: 1-11
SHP-2 binds to Tyr763 and Tyr1009 in the PDGF β-receptor and mediates PDGF-induced activation of the Ras/MAP kinase pathway and chemotaxis

Lars Rönnstrand
Ann-Kristin Arvidsson
Carl-Henrik Heldin
Research14 Jul 1999
Oncogene

Volume: 18, P: 3696-3702
BMP signaling is a therapeutic target in ovarian cancer

Tomohiko Fukuda
Risa Fukuda
Carl-Henrik Heldin
ResearchOpen Access05 Dec 2020
Cell Death Discovery

Volume: 6, P: 1-15
The transcription factor LHX2 mediates and enhances oncogenic BMP signaling in medulloblastoma

Yae Ohata
Mohamad M. Ali
Aristidis Moustakas
ResearchOpen Access28 Mar 2025
Cell Death & Differentiation

Volume: 32, P: 1915-1929
PDGF-C is a new protease-activated ligand for the PDGF α-receptor

Xuri Li
Annica Pontén
Ulf Eriksson
Research07 Apr 2000
Nature Cell Biology

Volume: 2, P: 302-309
Chemical regulators of epithelial plasticity reveal a nuclear receptor pathway controlling myofibroblast differentiation

Jon M. Carthy
Martin Stöter
Aristidis Moustakas
ResearchOpen Access19 Jul 2016
Scientific Reports

Volume: 6, P: 1-17
A cis-acting regulatory mutation causes premature hair graying and susceptibility to melanoma in the horse

Gray horses are born colored but gradually lose hair pigmentation and become white, a trait that is transmitted in an autosomal dominant manner. Leif Andersson and colleagues report that the the mutation causing the Gray phenotype is a 4.6-kb duplication in intron 6 of STX17, which promotes overexpression of both STX17 and the neighboring gene NR4A3 in melanomas from Gray horses.

Gerli Rosengren Pielberg
Anna Golovko
Leif Andersson
Research20 Jul 2008
Nature Genetics

Volume: 40, P: 1004-1009
The type I TGF-β receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner

In response to TGFβ, and in contrast to canonical SMAD activation, TGFβ receptor kinase activity is dispensable for activating the TAK1 kinase, whereas the TRAF6 ubiquitin ligase is neccessary.

Alessandro Sorrentino
Noopur Thakur
Maréne Landström
Research31 Aug 2008
Nature Cell Biology

Volume: 10, P: 1199-1207
TGFβ1/Smad3 counteracts BRCA1-dependent repair of DNA damage

Anna Dubrovska
Takashi Kanamoto
Serhiy Souchelnytskyi
Research14 Feb 2005
Oncogene

Volume: 24, P: 2289-2297
BRCA2 and Smad3 synergize in regulation of gene transcription

Olena Preobrazhenska
Mariya Yakymovych
Serhiy Souchelnytskyi
Research15 Aug 2002
Oncogene

Volume: 21, P: 5660-5664
Functional consequences of tumorigenic missense mutations in the amino-terminal domain of Smad4

Anita Morén
Susumu Itoh
Carl-Henrik Heldin
Research07 Sept 2000
Oncogene

Volume: 19, P: 4396-4404
TGF-β signalling from cell membrane to nucleus through SMAD proteins

Carl-Henrik Heldin
Kohei Miyazono
Peter ten Dijke
Reviews04 Dec 1997
Nature

Volume: 390, P: 465-471
The noncoding MIR100HG RNA enhances the autocrine function of transforming growth factor β signaling

Panagiotis Papoutsoglou
Dorival Mendes Rodrigues-Junior
Aristidis Moustakas
ResearchOpen Access04 May 2021
Oncogene

Volume: 40, P: 3748-3765
The polarity protein Par3 coordinates positively self-renewal and negatively invasiveness in glioblastoma

Mahsa Shahidi Dadras
Laia Caja
Aristidis Moustakas
ResearchOpen Access12 Oct 2021
Cell Death & Disease

Volume: 12, P: 1-17
Feedback Control: The role of negative feedback in signal transduction control

Carl-Henrik Heldin
Johan Lennartsson
Carina Hellberg
News09 Apr 2008
European Journal of Human Genetics

Volume: 16, P: 769-770
TUFT1 interacts with RABGAP1 and regulates mTORC1 signaling

Natsumi Kawasaki
Kazunobu Isogaya
Daizo Koinuma
ResearchOpen Access09 Jan 2018
Cell Discovery

Volume: 4, P: 1-16
Snail regulates BMP and TGFβ pathways to control the differentiation status of glioma-initiating cells

Laia Caja
Kalliopi Tzavlaki
Aristidis Moustakas
ResearchOpen Access16 Feb 2018
Oncogene

Volume: 37, P: 2515-2531
LXRα limits TGFβ-dependent hepatocellular carcinoma associated fibroblast differentiation

Anita Morén
Claudia Bellomo
Aristidis Moustakas
ResearchOpen Access16 May 2019
Oncogenesis

Volume: 8, P: 1-14
TGFβ and EGF signaling orchestrates the AP-1- and p63 transcriptional regulation of breast cancer invasiveness

Anders Sundqvist
Eleftheria Vasilaki
Hans van Dam
ResearchOpen Access29 Apr 2020
Oncogene

Volume: 39, P: 4436-4449
Snail mediates crosstalk between TGFβ and LXRα in hepatocellular carcinoma

Claudia Bellomo
Laia Caja
Aristidis Moustakas
ResearchOpen Access11 Dec 2017
Cell Death & Differentiation

P: 1-19
VEGF receptor signalling ? in control of vascular function

Vascular endothelial growth factors (VEGFs) regulate vascular development during embryogenesis and angiogenesis in the adult. The recently developed cancer treatments that target VEGF receptor activation highlight the clinical relevance of inhibiting VEGF pathways that are exaggerated in pathological angiogenesis.

Anna-Karin Olsson
Anna Dimberg
Lena Claesson-Welsh
Reviews01 May 2006
Nature Reviews Molecular Cell Biology

Volume: 7, P: 359-371
Mechanisms and regulation of endothelial VEGF receptor signalling

Vascular endothelial growth factors (VEGFs) and their receptors (VEGFRs) are crucial for the formation and remodelling of blood vessels. VEGFR2, which is the main endothelial VEGFR, is regulated by receptor-interacting proteins, endocytosis and trafficking. Recent insights have been gained into these layers of regulation and the crosstalk between VEGFR2 signalling and other endothelial signalling cascades.

Michael Simons
Emma Gordon
Lena Claesson-Welsh
Reviews27 Jul 2016
Nature Reviews Molecular Cell Biology

Volume: 17, P: 611-625
Extracellular control of TGFβ signalling in vascular development and disease

Recent studies of human genetic syndromes and transgenic mouse models with vascular pathology have exposed a crucial function of extracellular control in the regulation of TGFβ bioavailability in the vascular system. This Review discusses such regulation and the implications of defects in this process with regards to human health.

Peter ten Dijke
Helen M. Arthur
Reviews01 Nov 2007
Nature Reviews Molecular Cell Biology

Volume: 8, P: 857-869
A gain-of-function mutation in the PDGFR-β alters the kinetics of injury response in liver and skin

Monika Krampert
Carl-Henrik Heldin
Rainer L Heuchel
Research01 Sept 2008
Laboratory Investigation

Volume: 88, P: 1204-1214

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