Merilahti Johannes J

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Proteomics (4)

Organisms

Chlamydomonas reinhardtii (4)
Pseudomonas canadensis (4)
Human alphaherpesvirus 1 strain 17 (4)
Marchantia polymorpha subsp. ruderalis (4)
Methylocystis sp. (4)
Exiguobacterium sp. SH31 (4)
Porites pukoensis (4)
Porphyromonas gingivalis W83 (4)
Bothrops insularis (4)
Bothrops jararaca (4)
Bothrops jararacussu (4)
Bothrops cotiara (4)
Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841 (4)
Dinosauria (4)
Pseudomonas [fluorescens] SBW25 (4)
Trypanosoma vivax Y486 (4)
Streptomyces coelicolor (4)
Aves (4)
Pseudomonas taiwanensis (4)
Burkholderia ubonensis MSMB22 (4)
Pseudomonas aeruginosa PA103 (4)
Artibeus jamaicensis (4)
Morchella importuna (4)
Clostridium autoethanogenum (4)
Human alphaherpesvirus 1 strain KOS (4)
Human herpesvirus 2 strain 186 (4)
Microbacterium ginsengisoli (4)
Streptomyces sp. A494 Ydz-AH (4)
Strawberry leafy fruit phytoplasma (4)
Shewanella oneidensis MR-1 (4)

Repository

pride (4)

Tissue

Mammary gland tumor cell line (1)
Embryo (1)
Epithelial cell (1)

Disease

Adenocarcinoma (1)

Technology Type

Mass Spectrometry (4)
SRM/MRM (1)
Affinity purification coupled with mass spectrometry proteomics (1)
Data-independent acquisition (1)
Shotgun proteomics (1)

Publication Date

2023 (2)
2025 (1)
2020 (1)

Lab affiliation

Institute of Biomedicine, and Medicity Research Laboratories, University of Turku, Turku, Finland; Turku Bioscience Centre, University of Turku, and Åbo Akademi University, Turku, Finland (1)
Medicity Research Laboratories and Institute of Biomedicine, Faculty of Medicine, University of Turku, Finland Turku Bioscience Center, University of Turku and Åbo Akademi University, Finland (1)
Turku Bioscience Centre, University of Turku and Åbo Akademi University, Turku, Finland. (1)
Medicity Research Laboratories and Institute of Biomedicine, Faculty of Medicine, University of Turku, 20520 Turku, Finland. Turku Bioscience Centre, University of Turku and Åbo Akademi University, 20520 Turku, Finland. Department of Oncology, Turku University Hospital, 20521 Turku, Finland. (1)

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An extracellular receptor tyrosine kinase motif orchestrating intracellular STAT activation

The ErbB4 receptor isoforms JM-a and JM-b differ within their extracellular juxtamembrane (eJM) domains. Here, ErbB4 isoforms are used as a model to address the effect of structural variation in the eJM domain of receptor tyrosine kinases (RTK) on downstream signaling. A specific JM-a-like sequence ...

ORGANISM(S): Homo sapiens (Human)

2023-01-30 | PXD026546 | Pride

An extracellular receptor tyrosine kinase motif orchestrating intracellular STAT activation

ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) Cercopithecus aethiops (Green monkey) (Grivet)

2023-01-30 | PXD017783 | Pride

N-lectin Streptavidin pull down

Phosphoproteomic analysis reveals the diversity of signaling behind ErbB inhibitor-induced phenotypes

Effects of kinase inhibitors on the phosphoproteome have been rarely investigated at a whole organism level. Here we performed a phosphoproteomic analysis in embryonic zebrafish to identify the signaling pathways perturbed by the ErbB receptor tyrosine kinase inhibitors at the whole organism level. ...

ORGANISM(S): Danio rerio (Zebrafish) (Brachydanio rerio)

2025-12-29 | PXD050396 | Pride

Erbb inhibitor Signaling pathways Zebrafish embryos Phosphoproteome

VAV3 in ERBB4-mediated cancer cell migration

ERBB4 is a member of the epidermal growth factor receptor (EGFR)/ERBB subfamily of receptor tyrosine kinases that regulates cellular processes including proliferation, migration and survival. ERBB4 signaling is involved in embryogenesis and homeostasis of adult tissues, but also in human pathologies...