LIVIVO - Search results -

Search results

Result 1 - 10 of total 18

Search options

Article ; Online: Mass spectrometry-based Cellular Thermal Shift Assay (CETSA®) for target deconvolution in phenotypic drug discovery.

Friman, Tomas

2019 Volume 28, Issue 1, Page(s) 115174

Abstract: The recent renewed interest in phenotypic drug discovery has concomitantly put a focus on target deconvolution in order to achieve drug-target identification. Even though there are prescribed therapies whose mode of action is not fully understood, ... ...

Abstract	The recent renewed interest in phenotypic drug discovery has concomitantly put a focus on target deconvolution in order to achieve drug-target identification. Even though there are prescribed therapies whose mode of action is not fully understood, knowledge of the primary target will inevitably facilitate the discovery and translation of efficacy from bench to bedside. Elucidating targets and subsequent pathways engaged will also facilitate safety studies and overall development of novel drug candidates. Today, there are several techniques available for identifying the primary target, many of which rely on mass spectrometry (MS) to identify compound - target protein interactions. The Cellular Thermal Shift Assay (CETSA®) is well suited for identifying target engagement between ligands and their protein targets. Several studies have shown that CETSA combined with MS is a powerful technique that allows unlabeled target deconvolution in complex samples such as intact cells and tissues in addition to cell lysates and other protein suspensions. The applicability of CETSA MS for target deconvolution purposes will be discussed and exemplified in this mini review.
MeSH term(s)	Drug Discovery ; Humans ; Ligands ; Proteins/chemistry ; Proteomics ; Temperature
Chemical Substances	Ligands ; Proteins
Language	English
Publishing date	2019-10-31
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1161284-8
ISSN	1464-3391 ; 0968-0896
ISSN (online)	1464-3391
ISSN	0968-0896
DOI	10.1016/j.bmc.2019.115174
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3815: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: CETSA MS Profiling for a Comparative Assessment of FDA-Approved Antivirals Repurposed for COVID-19 Therapy Identifies TRIP13 as a Remdesivir Off-Target.

Friman, Tomas / Chernobrovkin, Alexey / Martinez Molina, Daniel / Arnold, Laurence

SLAS discovery : advancing life sciences R & D

2020 Volume 26, Issue 3, Page(s) 336–344

Abstract: The reuse of preexisting small molecules for a novel emerging disease threat is a rapid measure to discover unknown applications for previously validated therapies. A pertinent and recent example where such a strategy could be employed is in the fight ... ...

Abstract	The reuse of preexisting small molecules for a novel emerging disease threat is a rapid measure to discover unknown applications for previously validated therapies. A pertinent and recent example where such a strategy could be employed is in the fight against coronavirus disease 2019 (COVID-19). Therapies designed or discovered to target viral proteins also have off-target effects on the host proteome when employed in a complex physiological environment. This study aims to assess these host cell targets for a panel of FDA-approved antiviral compounds including remdesivir, using the cellular thermal shift assay (CETSA) coupled with mass spectrometry (CETSA MS) in noninfected cells. CETSA MS is a powerful method to delineate direct and indirect interactions between small molecules and protein targets in intact cells. Biologically active compounds can induce changes in thermal stability, in their primary binding partners, and in proteins that in turn interact with the direct targets. Such engagement of host targets by antiviral drugs may contribute to the clinical effect against the virus but can also constitute a liability. We present here a comparative study of CETSA molecular target engagement fingerprints of antiviral drugs to better understand the link between off-targets and efficacy.
MeSH term(s)	ATPases Associated with Diverse Cellular Activities/metabolism ; Adenosine/analogs & derivatives ; Adenosine Monophosphate/analogs & derivatives ; Adenosine Monophosphate/pharmacology ; Alanine/analogs & derivatives ; Alanine/pharmacology ; Antiviral Agents/pharmacology ; COVID-19/drug therapy ; Cell Cycle Proteins/metabolism ; Drug Evaluation, Preclinical/methods ; Drug Repositioning ; Furans/pharmacology ; Hep G2 Cells ; Humans ; Mass Spectrometry ; Proteomics/methods ; Pyrroles/pharmacology ; Triazines/pharmacology ; United States ; United States Food and Drug Administration
Chemical Substances	Antiviral Agents ; Cell Cycle Proteins ; Furans ; Pyrroles ; Triazines ; GS-441524 (1BQK176DT6) ; remdesivir (3QKI37EEHE) ; Adenosine Monophosphate (415SHH325A) ; ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-) ; TRIP13 protein, human (EC 3.6.4.-) ; Adenosine (K72T3FS567) ; Alanine (OF5P57N2ZX)
Keywords	covid19
Language	English
Publishing date	2020-11-18
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2885123-7
ISSN	2472-5560 ; 2472-5552
ISSN (online)	2472-5560
ISSN	2472-5552
DOI	10.1177/2472555220973597
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4911: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Vitamin D Analogues Tacalcitol and Calcipotriol Inhibit Proliferation and Migration of T98G Human Glioblastoma Cells.

Emanuelsson, Ida / Wikvall, Kjell / Friman, Tomas / Norlin, Maria

Basic & clinical pharmacology & toxicology

2018 Volume 123, Issue 2, Page(s) 130–136

Abstract: The active form of vitamin D (1α,25-dihydroxyvitamin D) acts as a steroid hormone and binds to the vitamin D receptor. This receptor is expressed in most cell types including cells in the central nervous system (CNS). Vitamin D has several functions in ... ...

Abstract	The active form of vitamin D (1α,25-dihydroxyvitamin D) acts as a steroid hormone and binds to the vitamin D receptor. This receptor is expressed in most cell types including cells in the central nervous system (CNS). Vitamin D has several functions in the body including effects on brain development, neuroprotection and immunological regulation. It has been shown that vitamin D has antiproliferative activities in different cancer cell lines. Tacalcitol and calcipotriol are synthetic analogues of 1α,25-dihydroxyvitamin D with reduced effect on calcium metabolism. The aim of this study was to analyse the effects of tacalcitol and calcipotriol on cell viability, proliferation and migration in the human glioblastoma cell line T98G. Glioblastoma is the most lethal type of primary tumours in the CNS. Both analogues decreased cell viability and/or growth, dose-dependently, in concentrations between 1 nM and 10 μM. Manual counting indicated suppressive effects by the vitamin D analogues on proliferation. Treatment with tacalcitol strongly suppressed thymidine incorporation, indicating that the vitamin D analogues mainly inhibit proliferation. Also, effects on cell migration were measured with wound-healing assay. Both calcipotriol and tacalcitol reduced the migration rate of T98G cells compared to vehicle-treated cells. However, they had no effect on caspase-3 and -7 activities, suggesting that their mechanism of action does not involve induction of apoptosis. The current results indicate that the vitamin D analogues tacalcitol and calcipotriol strongly reduce proliferation and migration of human glioblastoma T98G cells, suggesting a potential role for this type of compounds in treatment of brain cancer.
MeSH term(s)	Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Calcitriol/analogs & derivatives ; Calcitriol/pharmacology ; Calcitriol/therapeutic use ; Cell Line, Tumor ; Cell Movement/drug effects ; Cell Proliferation/drug effects ; Cell Survival/drug effects ; Dihydroxycholecalciferols/pharmacology ; Dihydroxycholecalciferols/therapeutic use ; Drug Evaluation, Preclinical ; Glioblastoma/drug therapy ; Glioblastoma/pathology ; Humans ; Receptors, Calcitriol/metabolism
Chemical Substances	Antineoplastic Agents ; Dihydroxycholecalciferols ; Receptors, Calcitriol ; VDR protein, human ; calcipotriene (143NQ3779B) ; 1 alpha,24-dihydroxyvitamin D3 (60965-80-2) ; Calcitriol (FXC9231JVH)
Language	English
Publishing date	2018-04-25
Publishing country	England
Document type	Journal Article
ZDB-ID	2134679-3
ISSN	1742-7843 ; 1742-7835
ISSN (online)	1742-7843
ISSN	1742-7835
DOI	10.1111/bcpt.13007
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Uf I Zs.144: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Modulation of E-Cadherin Function through the AmotL2 Isoforms Promotes Ameboid Cell Invasion.

Subramani, Aravindh / Cui, Weiyingqi / Zhang, Yuanyuan / Friman, Tomas / Zhao, Zhihai / Huang, Wenmao / Fonseca, Pedro / Lui, Weng-Onn / Narayanan, Vani / Bobrowska, Justyna / Lekka, Małgorzata / Yan, Jie / Conway, Daniel E / Holmgren, Lars

Cells

2023 Volume 12, Issue 13

Abstract: The spread of tumor cells and the formation of distant metastasis remain the main causes of mortality in cancer patients. However, the mechanisms governing the release of cells from micro-environmental constraints remain unclear. E-cadherin negatively ... ...

Abstract	The spread of tumor cells and the formation of distant metastasis remain the main causes of mortality in cancer patients. However, the mechanisms governing the release of cells from micro-environmental constraints remain unclear. E-cadherin negatively controls the invasion of epithelial cells by maintaining cell-cell contacts. Furthermore, the inactivation of E-cadherin triggers invasion in vitro. However, the role of E-cadherin is complex, as metastasizing cells maintain E-cadherin expression, which appears to have a positive role in the survival of tumor cells. In this report, we present a novel mechanism delineating how E-cadherin function is modulated to promote invasion. We have previously shown that E-cadherin is associated with p100AmotL2, which is required for radial actin formation and the transmission of mechanical force. Here, we present evidence that p60AmotL2, which is expressed in invading tumor cells, binds to the p100AmotL2 isoform and uncouples the mechanical constraint of radial actin filaments. We show for the first time that the coupling of E-cadherin to the actin cytoskeleton via p100AmotL2 is directly connected to the nuclear membrane. The expression of p60AmotL2 inactivates this connection and alters the properties of the nuclear lamina, potentiating the invasion of cells into micropores of the extracellular matrix. In summary, we propose that the balance of the two AmotL2 isoforms is important in the modulation of E-cadherin function and that an imbalance of this axis promotes ameboid cell invasion.
MeSH term(s)	Humans ; Amoeba/metabolism ; Cadherins/metabolism ; Actin Cytoskeleton/metabolism ; Actins/metabolism ; Epithelial Cells/metabolism
Chemical Substances	Cadherins ; Actins
Language	English
Publishing date	2023-06-21
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells12131682
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: A Tale of Two Tails: Efficient Profiling of Protein Degraders by Specific Functional and Target Engagement Readouts.

Chernobrovkin, Alexey L / Cázares-Körner, Cindy / Friman, Tomas / Caballero, Isabel Martin / Amadio, Daniele / Martinez Molina, Daniel

SLAS discovery : advancing life sciences R & D

2021 Volume 26, Issue 4, Page(s) 534–546

Abstract: Targeted protein degradation represents an area of great interest, potentially offering improvements with respect to dosing, side effects, drug resistance, and reaching "undruggable" proteins compared with traditional small-molecule therapeutics. A major ...

Abstract	Targeted protein degradation represents an area of great interest, potentially offering improvements with respect to dosing, side effects, drug resistance, and reaching "undruggable" proteins compared with traditional small-molecule therapeutics. A major challenge in the design and characterization of degraders acting as molecular glues is that binding of the molecule to the protein of interest (PoI) is not needed for efficient and selective protein degradation; instead, one needs to understand the interaction with the responsible ligase. Similarly, for proteasome targeting chimeras (PROTACs), understanding the binding characteristics of the PoI alone is not sufficient. Therefore, simultaneously assessing the binding to both PoI and the E3 ligase as well as the resulting degradation profile is of great value. The cellular thermal shift assay (CETSA) is an unbiased cell-based method, designed to investigate the interaction of compounds with their cellular protein targets by measuring compound-induced changes in protein thermal stability. In combination with mass spectrometry (MS), CETSA can simultaneously evaluate compound-induced changes in the stability of thousands of proteins. We have used CETSA MS to profile a number of protein degraders, including molecular glues (e.g., immunomodulatory drugs) and PROTACs, to understand mode of action and to deconvolute off-target effects in intact cells. Within the same experiment, we were able to monitor both target engagement by observing changes in protein thermal stability as well as efficacy by simultaneous assessment of protein abundances. This allowed us to correlate target engagement (i.e., binding to the PoI and ligases) and functional readout (i.e., degrader induced protein degradation).
MeSH term(s)	Drug Discovery/methods ; Eukaryotic Cells/cytology ; Eukaryotic Cells/drug effects ; Eukaryotic Cells/immunology ; Eukaryotic Cells/metabolism ; High-Throughput Screening Assays ; Humans ; Immunomodulating Agents/chemistry ; Immunomodulating Agents/pharmacology ; Ligands ; Mass Spectrometry/methods ; Molecular Targeted Therapy/methods ; Proteasome Endopeptidase Complex/metabolism ; Protein Binding ; Protein Processing, Post-Translational ; Protein Stability ; Proteolysis/drug effects ; Proteomics/methods ; Proteostasis/genetics ; Temperature ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination/drug effects
Chemical Substances	Immunomodulating Agents ; Ligands ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2021-01-15
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2885123-7
ISSN	2472-5560 ; 2472-5552
ISSN (online)	2472-5560
ISSN	2472-5552
DOI	10.1177/2472555220984372
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4911: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: CETSA® MS profiling for a comparative assessment of FDA approved antivirals repurposed for COVID-19 therapy identifies Trip13 as a Remdesivir off-target

Friman, Tomas / Chernobrovkin, Alexey / Molina, Daniel Martinez / Arnold, Laurence

bioRxiv

Abstract: The reuse of pre-existing small molecules for a novel emerging disease threat is a rapid measure to discover unknown applications for previously validated therapies. A pertinent and recent example where such strategy could be employed is in the fight ... ...

Abstract	The reuse of pre-existing small molecules for a novel emerging disease threat is a rapid measure to discover unknown applications for previously validated therapies. A pertinent and recent example where such strategy could be employed is in the fight against COVID-19. Therapies designed or discovered to target viral proteins also have off-target effects on the host proteome when employed in a complex physiological environment. This study aims to assess these host cell targets for a panel of FDA approved antiviral compounds including Remdesivir, using the cellular thermal shift assay (CETSA®) coupled to mass spectrometry (CETSA MS) in non-infected cells. CETSA MS is a powerful method to delineate direct and indirect interactions between small molecules and protein targets in intact cells. Biologically active compounds can induce changes in thermal stability, in their primary binding partners as well as in proteins that in turn interact with the direct targets. Such engagement of host targets by antiviral drugs may contribute to the clinical effect against the virus but can also constitute a liability. We present here a comparative study of CETSA molecular target engagement fingerprints of antiviral drugs to better understand the link between off-targets and efficacy.
Keywords	covid19
Publisher	BioRxiv; WHO
Document type	Article ; Online
DOI	10.1101/2020.07.19.210492
Database	COVID19

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article ; Online: CETSA MS profiling for a comparative assessment of FDA approved antivirals repurposed for COVID-19 therapy identifies Trip13 as a Remdesivir off-target

Friman, Tomas / Chernobrovkin, Alexey / Martinez Molina, Daniel / Arnold, Laurence H

bioRxiv

Abstract	The reuse of pre-existing small molecules for a novel emerging disease threat is a rapid measure to discover unknown applications for previously validated therapies. A pertinent and recent example where such strategy could be employed is in the fight against COVID-19. Therapies designed or discovered to target viral proteins also have off-target effects on the host proteome when employed in a complex physiological environment. This study aims to assess these host-cell targets for a panel of FDA approved antiviral compounds including Remdesivir, using the cellular thermal shift assay (CETSA®) coupled to mass spectrometry (CETSA MS) in non-infected cells. CETSA MS is a powerful method to delineate direct and indirect interactions between small molecules and protein targets in intact cells. Biologically active compounds can induce changes in thermal stability, in their primary binding partners as well as in proteins that in turn interact with the direct targets. Such engagement of host targets by antiviral drugs may contribute to the clinical effect against the virus but can also constitute a liability. We present here a comparative study of CETSA molecular target engagement fingerprints of antiviral drugs to better understand the link between off-targets and efficacy.
Keywords	covid19
Language	English
Publishing date	2020-07-20
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2020.07.19.210492
Database	COVID19

Full text online

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Mechanistic Insights into a CDK9 Inhibitor Via Orthogonal Proteomics Methods.

ACS chemical biology

2021 Volume 17, Issue 1, Page(s) 54–67

Abstract: Cyclin-dependent-kinases (CDKs) are members of the serine/threonine kinase family and are highly regulated by cyclins, a family of regulatory subunits that bind to CDKs. CDK9 represents one of the most studied examples of these transcriptional CDKs. CDK9 ...

Abstract	Cyclin-dependent-kinases (CDKs) are members of the serine/threonine kinase family and are highly regulated by cyclins, a family of regulatory subunits that bind to CDKs. CDK9 represents one of the most studied examples of these transcriptional CDKs. CDK9 forms a heterodimeric complex with its regulatory subunit cyclins T1, T2 and K to form the positive transcription elongation factor b (P-TEFb). This complex regulates transcription via the phosphorylation of RNA polymerase II (RNAPolII) on Ser-2, facilitating promoter clearance and transcription elongation and thus remains an attractive therapeutic target. Herein, we have utilized classical affinity purification chemical proteomics, kinobeads assay, compressed CEllular Thermal Shift Assay (CETSA)-MS and Limited Proteolysis (LiP) to study the selectivity, target engagement and downstream mechanistic insights of a CDK9 tool compound. The above experiments highlight the value of quantitative mass spectrometry approaches to drug discovery, specifically proteome wide target identification and selectivity profiling. The approaches utilized in this study unanimously indicated that the CDK family of kinases are the main target of the compound of interest, with CDK9, showing the highest target affinity with remarkable consistency across approaches. We aim to provide guidance to the scientific community on the available chemical biology/proteomic tools to study advanced lead molecules and to highlight pros and cons of each technology while describing our findings in the context of the CDKs biology.
MeSH term(s)	Cell Line, Tumor ; Chemical Fractionation ; Cyclin-Dependent Kinase 9/antagonists & inhibitors ; Cyclin-Dependent Kinase 9/genetics ; Cyclin-Dependent Kinase 9/metabolism ; Gene Expression Regulation, Enzymologic/drug effects ; Humans ; Mass Spectrometry ; Proteomics
Chemical Substances	CDK9 protein, human (EC 2.7.11.22) ; Cyclin-Dependent Kinase 9 (EC 2.7.11.22)
Language	English
Publishing date	2021-12-25
Publishing country	United States
Document type	Journal Article
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.1c00488
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Phenotypical differences in connective tissue cells emerging from microvascular pericytes in response to overexpression of PDGF-B and TGF-β1 in normal skin in vivo.

Rodriguez, Alejandro / Friman, Tomas / Kowanetz, Marcin / van Wieringen, Tijs / Gustafsson, Renata / Sundberg, Christian

The American journal of pathology

2013 Volume 182, Issue 6, Page(s) 2132–2146

Abstract: Fibrosis is a deleterious consequence of chronic inflammation in a number of human pathologies ultimately leading to organ dysfunction and failure. Two growth factors that are important in blood vessel physiology and tissue fibrosis, platelet-derived ... ...

Abstract	Fibrosis is a deleterious consequence of chronic inflammation in a number of human pathologies ultimately leading to organ dysfunction and failure. Two growth factors that are important in blood vessel physiology and tissue fibrosis, platelet-derived growth factor (PDGF)-B and transforming growth factor (TGF)-β1, were investigated. Adenoviral vectors were used to induce transient overexpression of these growth factors in mouse skin. Changes in tissue structure and protein and mRNA expressions were investigated. Both PDGF-B and TGF-β1 could initiate but neither could sustain angiogenesis. Instead, vascular regression was observed. Overexpression of both TGF-β1 and PDGF-B led to a marked macrophage influx and an expansion of the connective tissue cell population. Over time, this effect was sustained in mice treated with TGF-β1, whereas it was partially reversible in mice treated with PDGF-B. On the basis of structure and expression of phenotypical markers, the emerging connective tissue cell population may originate from microvascular pericytes. TGF-β1 induced expansion of connective tissue cells with a myofibroblast phenotype, whereas PDGF-B induced a fibroblast phenotype negative for α-smooth muscle actin. TGF-β1 and PDGF-B overexpressions mediated distinct effects on mRNA transcript levels of fibrillar procollagens, their modifying enzymes, small leucin-rich repeat proteoglycans, and matricellular proteins affecting both the composition and the quantity of the extracellular matrix. This study offers new insight into the effects of PDGF-B and TGF-β1 on the vasculature and connective tissue in vivo.
MeSH term(s)	Adenoviridae/genetics ; Animals ; Connective Tissue Cells/cytology ; Endothelium, Vascular/cytology ; Extracellular Matrix/physiology ; Extracellular Matrix Proteins/metabolism ; Fibromodulin ; Gene Expression Regulation/physiology ; Genetic Vectors ; Macrophages/physiology ; Mice ; Mice, Nude ; Microvessels/cytology ; Neovascularization, Physiologic/physiology ; Pericytes/cytology ; Pericytes/metabolism ; Phenotype ; Proteoglycans/metabolism ; Proto-Oncogene Proteins c-sis/physiology ; RNA, Messenger/genetics ; Skin/blood supply ; Skin/cytology ; Skin/metabolism ; Transforming Growth Factor beta1/physiology
Chemical Substances	Extracellular Matrix Proteins ; FMOD protein, human ; Fmod protein, mouse ; Proteoglycans ; Proto-Oncogene Proteins c-sis ; RNA, Messenger ; Transforming Growth Factor beta1 ; Fibromodulin (126468-95-9)
Language	English
Publishing date	2013-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2943-9
ISSN	1525-2191 ; 0002-9440
ISSN (online)	1525-2191
ISSN	0002-9440
DOI	10.1016/j.ajpath.2013.01.054
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Ud II Zs.76: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Inhibition of integrin α

Olof Olsson, P / Gustafsson, Renata / Salnikov, Alexei V / Göthe, Maria / Zeller, Kathrin S / Friman, Tomas / Baldetorp, Bo / Koopman, Louise A / Weinreb, Paul H / Violette, Shelia M / Kalamajski, Sebastian / Heldin, Nils-Erik / Rubin, Kristofer

Cell communication and signaling : CCS

2018 Volume 16, Issue 1, Page(s) 36

Abstract: Background: Chemotherapeutic efficacy can be improved by targeting the structure and function of the extracellular matrix (ECM) in the carcinomal stroma. This can be accomplished by e.g. inhibiting TGF-β1 and -β3 or treating with Imatinib, which results ...

Abstract	Background: Chemotherapeutic efficacy can be improved by targeting the structure and function of the extracellular matrix (ECM) in the carcinomal stroma. This can be accomplished by e.g. inhibiting TGF-β1 and -β3 or treating with Imatinib, which results in scarcer collagen fibril structure in xenografted human KAT-4/HT29 (KAT-4) colon adenocarcinoma. Methods: The potential role of α Results: Both KAT-4 and Capan-2 cells expressed the α Conclusion: Our data demonstrate that the α
MeSH term(s)	Animals ; Antibodies, Monoclonal/immunology ; Antigens, Neoplasm/immunology ; Antigens, Neoplasm/metabolism ; Cell Line, Tumor ; Cell Transformation, Neoplastic ; Collagen/chemistry ; Collagen/metabolism ; Extracellular Fluid/metabolism ; Female ; Gene Expression Profiling ; Humans ; Integrins/immunology ; Integrins/metabolism ; Mice ; Pressure ; Transforming Growth Factor beta/metabolism
Chemical Substances	Antibodies, Monoclonal ; Antigens, Neoplasm ; Integrins ; Transforming Growth Factor beta ; integrin alphavbeta6 ; Collagen (9007-34-5)
Language	English
Publishing date	2018-07-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1478-811X
ISSN (online)	1478-811X
DOI	10.1186/s12964-018-0249-7
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Kategorien

Inter-library loan at ZB MED

Full text online

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED