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Article ; Online: Fluorescence-Based Peptidolytic Assay for High-Throughput Screening of MMP14 Inhibitors.

Lee, Hyun / Ibrahimi, Lucas / Han, Kyu-Yeon

Methods in molecular biology (Clifton, N.J.)

2023 Volume 2747, Page(s) 229–242

Abstract: The membrane-bound matrix metalloproteinase 14 (MMP14, also known as MT1-MMP) plays important roles in the remodeling of the extracellular matrix during various cellular processes such as cancer metastasis, angiogenesis, and wound healing through its ... ...

Abstract	The membrane-bound matrix metalloproteinase 14 (MMP14, also known as MT1-MMP) plays important roles in the remodeling of the extracellular matrix during various cellular processes such as cancer metastasis, angiogenesis, and wound healing through its proteolytic activity. There are no known MMP14-specific inhibitors to date, and hence identification of MMP14-specific inhibitors will be beneficial for finding potential therapeutics for various diseases, including cancer and inflammation. High-throughput screening (HTS) assays have become a common way to search for new small compounds, peptides, and natural products. Enzymatic assays are highly amenable to HTS because most enzyme activities are quantifiable with the effect of many small molecules of interest on a specific target enzyme. Here, we describe a fluorescence-based enzymatic assay that can be applied as a large-scale HTS and a follow-up enzyme kinetics assay to find MMP14-specific inhibitors.
MeSH term(s)	Humans ; Matrix Metalloproteinase 14/chemistry ; High-Throughput Screening Assays ; Peptides ; Neoplasms ; Wound Healing
Chemical Substances	Matrix Metalloproteinase 14 (EC 3.4.24.80) ; Peptides ; MMP14 protein, human (EC 3.4.24.80)
Language	English
Publishing date	2023-12-01
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-3589-6_18
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Chlorine-Induced Toxicity on Murine Cornea: Exploring the Potential Therapeutic Role of Antioxidants.

An, Seungwon / Anwar, Khandaker / Ashraf, Mohammadjavad / Han, Kyu-Yeon / Djalilian, Ali R

Cells

2024 Volume 13, Issue 5

Abstract: Chlorine ( ... ...

Abstract	Chlorine (Cl
MeSH term(s)	Humans ; Animals ; Mice ; Antioxidants/metabolism ; Chlorine/toxicity ; Reactive Oxygen Species/metabolism ; Cornea/metabolism ; Corneal Injuries ; Fluorescein/pharmacology
Chemical Substances	Antioxidants ; Chlorine (4R7X1O2820) ; Reactive Oxygen Species ; Fluorescein (TPY09G7XIR)
Language	English
Publishing date	2024-03-05
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells13050458
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Article ; Online: The Role of Membrane-Type 1 Matrix Metalloproteinase-Substrate Interactions in Pathogenesis.

Lee, Hyun / Ibrahimi, Lucas / Azar, Dimitri T / Han, Kyu-Yeon

International journal of molecular sciences

2023 Volume 24, Issue 3

Abstract: A protease is an enzyme with a proteolytic activity that facilitates the digestion of its substrates. Membrane-type I matrix metalloproteinase (MT1-MMP), a member of the broader matrix metalloproteinases (MMP) family, is involved in the regulation of ... ...

Abstract	A protease is an enzyme with a proteolytic activity that facilitates the digestion of its substrates. Membrane-type I matrix metalloproteinase (MT1-MMP), a member of the broader matrix metalloproteinases (MMP) family, is involved in the regulation of diverse cellular activities. MT1-MMP is a very well-known enzyme as an activator of pro-MMP-2 and two collagenases, MMP-8 and MMP-13, all of which are essential for cell migration. As an anchored membrane enzyme, MT1-MMP has the ability to interact with a diverse group of molecules, including proteins that are not part of the extracellular matrix (ECM). Therefore, MT1-MMP can regulate various cellular activities not only by changing the extra-cellular environment but also by regulating cell signaling. The presence of both intracellular and extra-cellular portions of MT1-MMP can allow it to interact with proteins on both sides of the cell membrane. Here, we reviewed the MT1-MMP substrates involved in disease pathogenesis.
MeSH term(s)	Collagenases ; Matrix Metalloproteinase 14 ; Matrix Metalloproteinases ; Matrix Metalloproteinases, Membrane-Associated ; Metalloendopeptidases/metabolism ; Proteins ; Substrate Specificity
Chemical Substances	Collagenases (EC 3.4.24.-) ; Matrix Metalloproteinase 14 (EC 3.4.24.80) ; Matrix Metalloproteinases (EC 3.4.24.-) ; Matrix Metalloproteinases, Membrane-Associated (EC 3.4.24.-) ; Metalloendopeptidases (EC 3.4.24.-) ; Proteins
Language	English
Publishing date	2023-01-22
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24032183
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Article: Chemical constituents of Entandrophragma angolense and their anti-inflammatory activity

Youn, Isoo / Han, Kyu-Yeon / Gurgul, Aleksandra / Wu, Zhenlong / Lee, Hyun / Che, Chun-Tao

Phytochemistry. 2022 Sept., v. 201

2022

Abstract: From the stem bark of Entandrophragma angolense, six undescribed compounds were isolated, including seco-tirucallane type triterpenoids, limonoids, and a catechin glucoside, along with nineteen known structures. All structures were determined by ... ...

Abstract	From the stem bark of Entandrophragma angolense, six undescribed compounds were isolated, including seco-tirucallane type triterpenoids, limonoids, and a catechin glucoside, along with nineteen known structures. All structures were determined by interpretation of spectroscopic and HRMS data, and absolute configuration was confirmed with the aid of electronic circular dichroism. The isolated compounds were tested for LPS-induced NO inhibition in RAW 264.7 macrophages and EC₅₀ values for moluccensin O and (−)-catechin were 81 μM and 137 μM, respectively.
Keywords	Entandrophragma angolense ; anti-inflammatory activity ; bark ; catechin ; circular dichroism spectroscopy ; glucosides ; limonoids ; macrophages
Language	English
Dates of publication	2022-09
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	208884-8
ISSN	1873-3700 ; 0031-9422
ISSN (online)	1873-3700
ISSN	0031-9422
DOI	10.1016/j.phytochem.2022.113276
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Proteomics-Based Characterization of the Effects of MMP14 on the Protein Content of Exosomes from Corneal Fibroblasts.

Han, Kyu-Yeon / Chang, Jin-Hong / Azar, Dimitri T

Protein and peptide letters

2020 Volume 27, Issue 10, Page(s) 979–988

Abstract: Background: Exosomes secreted by corneal fibroblasts contain matrix metalloproteinase (MMP) 14, which is known to influence pro-MMP2 accumulation on exosomes. Accordingly, we hypothesized that the enzymatic activity of MMP14 may alter the protein ... ...

Abstract	Background: Exosomes secreted by corneal fibroblasts contain matrix metalloproteinase (MMP) 14, which is known to influence pro-MMP2 accumulation on exosomes. Accordingly, we hypothesized that the enzymatic activity of MMP14 may alter the protein content of corneal fibroblast- secreted exosomes. Objective: The aim of this study was to investigate the effects of MMP14 on the composition and biological activity of corneal fibroblast-derived exosomes. Methods: Knock out of the catalytic domain (ΔExon4) of MMP14 in corneal fibroblasts was used to determine the effect of MMP14 expression on the characteristics of fibroblast-secreted exosomes. The amount of secreted proteins and their size distribution were measured using Nano Tracking Analysis. Proteins within exosomes from wild-type (WT) and ΔExon4-deficient fibroblasts were identified by liquid chromatography-tandem mass spectrometry (MS/MS) proteomics analysis. The proteolytic effects of MMP14 were evaluated in vitro via MS identification of eliminated proteins. The biological functions of MMP14-carrying exosomes were investigated via fusion to endothelial cells and flow cytometric assays. Results: Exosomes isolated from WT and ΔExon4-deficient fibroblasts exhibited similar size distributions and morphologies, although WT fibroblasts secreted a greater amount of exosomes. The protein content, however, was higher in ΔExon4-deficient fibroblast-derived exosomes than in WT fibroblast-derived exosomes. Proteomics analysis revealed that WT-derived exosomes included proteins that regulated cell migration, and ΔExon4 fibroblast-derived exosomes contained additional proteins that were cleaved by MMP14. Conclusion: Our findings suggest that MMP14 expression influences the protein composition of exosomes secreted by corneal fibroblasts, and through those biological components, MMP14 in corneal fibroblasts derived-exosomes may regulate corneal angiogenesis.
MeSH term(s)	Animals ; Cornea/metabolism ; Exosomes/metabolism ; Fibroblasts/metabolism ; Matrix Metalloproteinase 14/metabolism ; Mice ; Protein Domains ; Proteomics
Chemical Substances	Mmp14 protein, mouse ; Matrix Metalloproteinase 14 (EC 3.4.24.80)
Language	English
Publishing date	2020-04-08
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1280776-x
ISSN	1875-5305 ; 0929-8665
ISSN (online)	1875-5305
ISSN	0929-8665
DOI	10.2174/0929866527666200408142827
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Article ; Online: Chemical constituents of Entandrophragma angolense and their anti-inflammatory activity.

Youn, Isoo / Han, Kyu-Yeon / Gurgul, Aleksandra / Wu, Zhenlong / Lee, Hyun / Che, Chun-Tao

Phytochemistry

2022 Volume 201, Page(s) 113276

Abstract	From the stem bark of Entandrophragma angolense, six undescribed compounds were isolated, including seco-tirucallane type triterpenoids, limonoids, and a catechin glucoside, along with nineteen known structures. All structures were determined by interpretation of spectroscopic and HRMS data, and absolute configuration was confirmed with the aid of electronic circular dichroism. The isolated compounds were tested for LPS-induced NO inhibition in RAW 264.7 macrophages and EC
MeSH term(s)	Anti-Inflammatory Agents/pharmacology ; Catechin ; Limonins/chemistry ; Limonins/pharmacology ; Meliaceae/chemistry ; Molecular Structure
Chemical Substances	Anti-Inflammatory Agents ; Limonins ; Catechin (8R1V1STN48)
Language	English
Publishing date	2022-06-15
Publishing country	England
Document type	Journal Article
ZDB-ID	208884-8
ISSN	1873-3700 ; 0031-9422
ISSN (online)	1873-3700
ISSN	0031-9422
DOI	10.1016/j.phytochem.2022.113276
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Article ; Online: Polyoxygenated cyclohexene derivatives and other constituents of Uvaria rufa stem.

Gurgul, Aleksandra / Wu, Zhenlong / Han, Kyu-Yeon / Shetye, Gauri / Sydara, Kongmany / Souliya, Onevilay / Johnson, Jeremy J / Che, Chun-Tao

Phytochemistry

2023 Volume 216, Page(s) 113884

Abstract: Six undescribed compounds, uvarirufols D and E, (+)-uvarigranol B, (-)-uvarigranol E, 6-acetoxy-5-hydroxy-7-methoxyflavanone and cherrevenaphthalene D, along with twelve known compounds, including polyoxygenated cyclohexenes, flavonoids, and lignans, ... ...

Abstract	Six undescribed compounds, uvarirufols D and E, (+)-uvarigranol B, (-)-uvarigranol E, 6-acetoxy-5-hydroxy-7-methoxyflavanone and cherrevenaphthalene D, along with twelve known compounds, including polyoxygenated cyclohexenes, flavonoids, and lignans, were isolated from the methanol extract of Uvaria rufa stems. Their structures were elucidated by spectroscopic analyses and the absolute configurations were determined using electronic circular dichroism. Several isolates were evaluated for cytotoxic, antitubercular and anti-inflammatory potentials. (-)-6-Acetylzeylenol showed moderate inhibitory activity against Mycobacterium tuberculosis, with MIC value of 47.10 μg/mL. Cherrevenaphthalene D exhibited weak antimycobacterial activity and potent inhibitory effect on lipopolysaccharide-induced nitric oxide (NO) production in RAW 264.7 cells (EC
MeSH term(s)	Uvaria/chemistry ; Molecular Structure ; Cyclohexenes/pharmacology ; Cyclohexenes/chemistry ; Lignans/pharmacology
Chemical Substances	cyclohexene (12L0P8F7GN) ; Cyclohexenes ; Lignans
Language	English
Publishing date	2023-10-07
Publishing country	England
Document type	Journal Article
ZDB-ID	208884-8
ISSN	1873-3700 ; 0031-9422
ISSN (online)	1873-3700
ISSN	0031-9422
DOI	10.1016/j.phytochem.2023.113884
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Article ; Online: Identification of small molecule inhibitors against MMP-14 via High-Throughput screening.

Lee, Hyun / Youn, Isoo / Demissie, Robel / Vaid, Tasneem M / Che, Chun-Tao / Azar, Dimitri T / Han, Kyu-Yeon

Bioorganic & medicinal chemistry

2023 Volume 85, Page(s) 117289

Abstract: Matrix metalloproteinases (MMPs) are involved in various cellular events in physiology and pathophysiology through endopeptidases activity. The expression levels and activities of most MMPs remain minimal in the normal conditions, whereas some MMPs are ... ...

Abstract	Matrix metalloproteinases (MMPs) are involved in various cellular events in physiology and pathophysiology through endopeptidases activity. The expression levels and activities of most MMPs remain minimal in the normal conditions, whereas some MMPs are significantly activated in pathological conditions such as cancer and neovascularization. Hence, MMPs are considered as both diagnostic markers and potential targets for therapeutic agents. Twenty-three known human MMPs share a similar active site structure with a zinc-binding motif, resulting in lack of specificity. Therefore, the enhancement of target specificity is a primary goal for the development of specific MMP inhibitors. MMP-14 regulates VEGFA/VEGFR2-system through cleavage of the non-functional VEGFR1 in vascular angiogenesis. In this study, we developed a fluorescence-based enzymatic assay using a specific MMP-14 substrate generated from VEGFR1 cleavage site. This well optimized assay was used as a primary screen method to identify MMP-14 specific inhibitors from 1,200 Prestwick FDA-approved drug library. Of ten initial hits, two compounds showed IC
MeSH term(s)	Humans ; High-Throughput Screening Assays ; Matrix Metalloproteinase 14 ; Clioquinol ; Matrix Metalloproteinase Inhibitors/chemistry ; Matrix Metalloproteinases/metabolism
Chemical Substances	Matrix Metalloproteinase 14 (EC 3.4.24.80) ; Clioquinol (7BHQ856EJ5) ; Matrix Metalloproteinase Inhibitors ; Matrix Metalloproteinases (EC 3.4.24.-)
Language	English
Publishing date	2023-04-17
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1161284-8
ISSN	1464-3391 ; 0968-0896
ISSN (online)	1464-3391
ISSN	0968-0896
DOI	10.1016/j.bmc.2023.117289
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Article ; Online: MMP14-Containing Exosomes Cleave VEGFR1 and Promote VEGFA-Induced Migration and Proliferation of Vascular Endothelial Cells.

Han, Kyu-Yeon / Chang, Jin-Hong / Azar, Dimitri T

Investigative ophthalmology & visual science

2019 Volume 60, Issue 6, Page(s) 2321–2329

Abstract: Purpose: Investigate the impact matrix metalloproteinase 14 (MMP14) delivered via exosomes produced by corneal fibroblasts on vascular endothelial growth factor receptor 1 (VEGFR1) cleavage on endothelial cells, and other key processes of angiogenesis.!# ...

Abstract	Purpose: Investigate the impact matrix metalloproteinase 14 (MMP14) delivered via exosomes produced by corneal fibroblasts on vascular endothelial growth factor receptor 1 (VEGFR1) cleavage on endothelial cells, and other key processes of angiogenesis. Methods: Proteolysis of VEGFR1 and R2 by the catalytic domain of MMP14 was investigated via immunocytochemistry with anti-VEGFR1, anti-VEGFR2, and anti-MMP14 antibodies. Exosomes were isolated via precipitation and serial ultracentrifugation from wild-type (WT) and MMP14 exon4-deficient corneal fibroblasts. Transmission electron microscopy and nanotracking analysis were used to characterize the isolated exosomes. The presence of MMP14 in exosomes from WT fibroblasts was confirmed by Western blotting. VEGFR1 cleavage upon treatment with WT-derived exosomes, Δexon4-derived exosomes, or the pan-MMP inhibitor GM60001 was examined via in vitro proteolysis analysis using recombinant mouse (rm) VEGFR1/R2. Endothelial cell migration and proliferation were investigated using a Boyden chamber assay and BrdU incorporation, respectively. Results: WT-derived exosomes specifically cleaved rmVEGFR1 in vitro, whereas Δexon4-derived exosomes did not. Treatment with the pan-MMP inhibitor GM6001 effectively inhibited VEGFR1 cleavage by WT-derived exosomes, confirming the role of MMP14 in this cleavage. WT-derived exosomes induced greater endothelial cell migration (P < 0.01) and proliferation (P < 0.5) compared to Δexon4-derived exosomes. Conclusions: MMP14-containing exosomes may be involved in the regulation of corneal neovascularization through degradation of VEGFR1 and VEGFA-induced endothelial cell proliferation and migration.
MeSH term(s)	Cell Movement/drug effects ; Cell Proliferation/drug effects ; Cornea/cytology ; Endothelial Cells/metabolism ; Exosomes/physiology ; Humans ; Immunohistochemistry ; Matrix Metalloproteinase 14/pharmacology ; Vascular Endothelial Growth Factor A/metabolism ; Vascular Endothelial Growth Factor Receptor-1/metabolism
Chemical Substances	Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factor Receptor-1 (EC 2.7.10.1) ; MMP14 protein, human (EC 3.4.24.80) ; Matrix Metalloproteinase 14 (EC 3.4.24.80)
Language	English
Publishing date	2019-05-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	391794-0
ISSN	1552-5783 ; 0146-0404
ISSN (online)	1552-5783
ISSN	0146-0404
DOI	10.1167/iovs.18-26277
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Article ; Online: MMP14 Regulates VEGFR3 Expression on Corneal Epithelial Cells.

Han, Kyu-Yeon / Chang, Jin-Hong / Azar, Dimitri T

Protein and peptide letters

2016 Volume 23, Issue 12, Page(s) 1095–1102

Abstract: Vascular endothelial growth factor receptor 3 (VEGFR3) regulates the growth and differentiation of blood and lymphatic vessels. To determine whether matrix metalloproteinase 14 (MMP14) modulates VEGFR3 expression in the corneal epithelium to influence ... ...

Abstract	Vascular endothelial growth factor receptor 3 (VEGFR3) regulates the growth and differentiation of blood and lymphatic vessels. To determine whether matrix metalloproteinase 14 (MMP14) modulates VEGFR3 expression in the corneal epithelium to influence the avascularity of the cornea, VEGFR3 expression was compared between wild-type and MMP14-deficient (MMP14 Δexon4) corneal epithelial cells. Western blot analysis showed that VEGFR3 protein expression was higher on MMP14 Δexon4 corneal epithelial cells than on wild-type cells, and quantitative RT-PCR analysis showed that VEGFR3 gene expression was highly induced in MMP14 Δexon4 corneal epithelial cells but not in wild-type corneal epithelial cells or wild-type and MMP14 Δexon4 corneal keratocytes. Unlike in epithelial cells, MMP14 Δexon4 keratocytes did not express relatively higher levels of VEGFR3 than wild-type keratocytes. Interestingly, in vitro proteolysis experiments showed that MMP14 does not cleave VEGFR3 in vitro as it does VEGFR1, indicating that other genes may be involved in the modulation of VEGFR3 expression by MMP14. Using proteomic analysis to identify candidate factors, we found that 39 nuclear proteins were differentially expressed between wildtype and MMP14 Δexon4 corneal epithelial cells. These findings suggest that MMP14 may regulate VEGFR3 expression at the transcriptional level on corneal epithelial cells but not on corneal keratocytes.
MeSH term(s)	Animals ; Cells, Cultured ; Corneal Keratocytes/metabolism ; Epithelium, Corneal/blood supply ; Epithelium, Corneal/cytology ; Epithelium, Corneal/metabolism ; Gene Expression Regulation ; Matrix Metalloproteinase 14/genetics ; Matrix Metalloproteinase 14/metabolism ; Mice ; Neovascularization, Physiologic/physiology ; Proteomics ; Vascular Endothelial Growth Factor Receptor-2/metabolism ; Vascular Endothelial Growth Factor Receptor-3/metabolism
Chemical Substances	Mmp14 protein, mouse ; Kdr protein, mouse (EC 2.7.10.1) ; Vascular Endothelial Growth Factor Receptor-2 (EC 2.7.10.1) ; Vascular Endothelial Growth Factor Receptor-3 (EC 2.7.10.1) ; Matrix Metalloproteinase 14 (EC 3.4.24.80)
Language	English
Publishing date	2016-10-21
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1280776-x
ISSN	1875-5305 ; 0929-8665
ISSN (online)	1875-5305
ISSN	0929-8665
DOI	10.2174/0929866523666161024142824
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