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| Date | Name | Thumbnail | Size | Description |
|---|---|---|---|---|
| 11:26, 22 December 2024 | The VEGFR2 signaling pathways in endothelial cells.png (file) |  |
2.65 MB | {{Information |description=Figure 2. The VEGFR2 signaling pathways in endothelial cells. The VEGFR2 signaling pathways are induced by the binding of VEGF-C, VEGF-E and VEGF-A to VEGFR2. The binding of ligand to VEGFR2 can result in the activation of different pathways such as SCR, PLC-y, PI3K, P38MAPK and FAK. These different pathways control cell shape, cell adhesion and permeability, proliferation, survival, permeability, vasodilatation, and migration. |date=2021-05-04 |source=https://www.m... |
| 11:14, 22 December 2024 | Representation of the different bindings between VEGFVEGFR and the molecules inhibiting their signaling pathways.png (file) |  |
1.43 MB | {{Information |description=Figure 1. Representation of the different bindings between VEGF/VEGFR and the molecules inhibiting their signaling pathways. The mammalian VEGF family is composed of five members: PIGF, VEGF-A, VEGF-B, VEGF-C and VEGF-D. These different members bind VEGFR: VEGFR-1, VEGFR-2, and VEGFR-3. These receptors are present on the surface of various cells indicated under the receptor. Various inhibitors can target the VEGF/VEGFR signaling pathways. |date=2021-05-04 |source=ht... |
| 10:39, 22 December 2024 | VEGF-D mediated angiogenic signaling in lymphatic or blood capillary endothelial cells.png (file) |  |
744 KB | {{Information |description=Figure 2. VEGF-D mediated angiogenic signaling in lymphatic or blood capillary endothelial cells. PreproVEGF-D can bind VEGFR-3 and activate lymphangiogenesis. However, proteolytic cleavage of the preproVEGF-D provides mature VEGF-D, which can bind and activate VEGFR-3 but also VEGFR-2 and induce VEGFR-2/3 heterodimerization [47,58,59]. Created with BioRender.com accessed on 27 July 2023. |date=2023-08-28 |source=https://www.mdpi.com/1422-0067/24/17/13317 Bokhari,... |
| 10:33, 22 December 2024 | VEGF-receptors and their ligands.png (file) |  |
736 KB | {{Information |description=Figure 1. VEGF-receptors and their ligands. VEGF-A binds VEGFR-1 and 2. VEGF-B and PIGF both bind VEGFR-1 only. VEGF-C and -D can bind both VEGFR-2 and 3. VEGF-E binds only VEGFR-2. VEGFR-R1 and 2 regulate blood vessel angiogenesis, whereas VEGFR-3’s main function is the regulation of lymphangiogenesis. VEGFR-1 also acts as a decoy receptor, preventing its ligands from binding VEGFR-2 [7,8,10,11,12]. Created with BioRender.com accessed on 27 July 2023. |date=2023-08... |
| 10:28, 22 December 2024 | Steps of tumor angiogenesis.png (file) |  |
2.3 MB | {{Information |description=Figure 3. Steps of tumor angiogenesis. Created with BioRender.com accessed on 27 July 2023 based on: [91,100]. Step 1 (hypoxia): the hypoxic or inflamed tumor microenvironment (TME) induces the production of vasculogenetic growth factors. Step 2 (proteolytic degradation): VEGF-A and -D binding to VEGFR-2 induce the production of matrix metalloproteinases (MMPs), degrading the extracellular matrix (ECM). Step 3 (tip cell migration): VEGFR-2 activation induces the tra... |
| 18:47, 19 December 2024 | Structure and Function of Gremlin-1.png (file) |  |
696 KB | {{Information |description=Figure 1. Structure and Function of Gremlin-1. (A) Schematic diagram representing the structure of Gremlin-1 with its signal sequence, glycosylation site and cysteine-rich region. (B) Gremlin-1 can bind and inhibit the BMP signaling pathways including the SMAD family as well as direct binding to vascular endothelial growth factor receptor (VEGFR) and activating its downstream signaling pathway. |date=2022-01-28 |source=https://www.mdpi.com/2227-9059/10/2/301 Elema... |
| 20:27, 18 December 2024 | Heparin binding sites on TGF-β superfamily cytokines.png (file) |  |
695 KB | {{Information |description=Figure 2. Heparin binding sites on TGF-β superfamily cytokines. Protein chains are shown as in Figure 1, and heparin binding site basic residues are shown in brown stick format. (A) The dimer of TGF-β1 (co-ordinates from 1KLC.pdb). Residues K25, R26, K31, K37, R94 and R97 form a discontinuous heparin binding site at the tips of the “fingers” [13]. (B) Sclerostin monomer (one of the NMR ensemble in 2K8P.pdb) with heparin-binding residues in brown. Cystine residues ar... |
| 18:58, 18 December 2024 | The heparin binding site of noggin in the noggin-BMP-7 complex (co-ordinates from 1M4U.pdb).png (file) | .png) |
489 KB | {{Information |description=Figure 4. The heparin binding site of noggin in the noggin-BMP-7 complex (co-ordinates from 1M4U.pdb). Noggin is shown as described in Figure 1, with amino acids 133–144, encompassing a cluster of eight basic arginine and lysine residues, shown in brown CPK format; BMP-7 is shown in blue ribbon format. The view of the dimer is rotated by 90° with respect to the plane of 1A. |date=2017-04-29 |source=https://www.mdpi.com/1420-3049/22/5/713 Rider, C.C.; Mulloy, B. H... |
| 18:35, 18 December 2024 | Mechanism for affinity switch in BMP-2 L100KN102D.tiff (file) |  |
1.04 MB | {{Information |description=Figure 6. Mechanism for affinity switch in BMP-2 L100K/N102D. H-bond network around the conserved serine residue in Act-A (a), the BMP-2 variant L100K/N102D with increased ActR-IIB affinity (b) and wildtype BMP-2 (c). The conserved central H-bond between Ser88 Oγ (Ser90 in Act-A) and Leu61 amide of ActR-IIB is shown as green thick stippled line. The intramolecular H-bond network comprising Lys100, Asp102, Ser88 (Lys102, Asp104 and Ser90 in Act-A) and a nearby struct... |
| 18:34, 18 December 2024 | Binding epitopes of BMPs and activin for interaction with activin receptors are very similar.tiff (file) |  |
1.7 MB | {{Information |description=Figure 5. Binding epitopes of BMPs and activin for interaction with activin receptors are very similar. (a) Structure based sequence alignment for the regions of BMP-2, BMP-7 and Act-A building the knuckle epitope. The putative contact residues based on the BMP-2:ActR-IIB interaction are color coded according to Fig. 4b. Asterisks mark the amino acid positions chosen for „domain swapping" between BMP-2 and Act-A, the conserved Ser is indicated by a triangle. (b) Seq... |
| 18:32, 18 December 2024 | BMP-2 type II receptor interface.tiff (file) |  |
1.09 MB | {{Information |description=Figure 4. BMP-2 type II receptor interface. (a) Location of the type II ligand/receptor binding epitopes on wildtype BMP-2 (left) and ActR-IIBECD(right). For designation of β-strands and finger-like structures see [62], the contact residues are marked in grey. (b) Surface representation of the type II ligand/receptor binding epitopes in the ''open book'' view. The surface of BMP-2 (left) is color coded by amino acid properties as follows: hydrophobic amino acids (A,... |
| 18:29, 18 December 2024 | BMP-2 type I receptor interface.tiff (file) |  |
2.29 MB | {{Information |description=Figure 3. BMP-2 type I receptor interface. (a) The tilt angle of BMPR-IA bound to BMP-2 changes upon binding of the type II receptor ActR-IIB. A superposition of the structures of BMP-2:(BMPR-IAECD)2 (blue, PDB entry 1REW), the ternary complex (1:1:1) of wildtype BMP-2:BMPR-IAECD:ActR-IIBECD (green) and the ternary complex (1:2:2) of BMP-2L100K/N102D:(BMPR-IAECD)2:(ActR-IIBECD)2 (red) is shown. The comparison of both assemblies reveals that the rearrangement is not... |
| 18:25, 18 December 2024 | Ternary ligand-receptor complex of BMP-2 variant L100KN102D.tiff (file) |  |
2.35 MB | {{Information |description=Figure 2. Ternary ligand-receptor complex of BMP-2 variant L100K/N102D. Ribbon representation (stereoview) of the ternary complex of the BMP-2 double variant L100K/N102D (in yellow and blue) bound to BMPR-IAECD (green) and ActR-IIBECD (red), viewed from the side (a) or from above (b). (c) Distances between the C-termini of the receptor ectodomains of each subtype are indicated. (d) The shortest distance between BMPR-IAECD and ActR-IIBECD occurs between the two recep... |
| 18:20, 18 December 2024 | Ternary ligand-receptor complex of wildtype BMP-2.tiff (file) |  |
1,014 KB | {{Information |description=Figure 1. Ternary ligand-receptor complex of wildtype BMP-2. Ribbon representation (stereo figure) of the crystal structure of wildtype BMP-2 (monomers in yellow and blue) bound to one receptor ectodomain of BMPR-IA<sub>ECD</sub> (green) and ActR-IIB<sub>ECD</sub> (red), (a) viewed from the side, (b) or from above. The unexpected stoichiometry 1:1:1 is due to crystal packing forces resulting in the loss of one BMPR-IA<sub>ECD</sub> and one ActR-IIB<sub>ECD</sub> mol... |
| 15:34, 18 December 2024 | Fate mapping the late tailbud reveals continued cell ingression.png (file) |  |
1.63 MB | {{Information |Description=Figure 3. Fate mapping the late tailbud reveals continued cell ingression. Schematic of DiI labelling experiment for distinct cell populations in HH20/21 tailbud (NT, neural tube; CNH, chordo-neural-hinge; MP mesoderm progenitors) (A); DiI labelling of NT before incubation (B), fixed and analysed in sections (n = 5/5 confined to NT) (B′); after incubation, DiI is restricted to Sox2 positive NT (B′″); DiI labelling of CNH before incubation (C), fixed and analysed in... |
| 15:31, 18 December 2024 | FGF signalling regulates cell fate assignment in the tailbud.png (file) |  |
2.76 MB | {{Information |Description=Figure 4. FGF signalling regulates cell fate assignment in the tailbud. Schematic of whole tailbud explant assay (A); Spry2 expression in tailbud explants following exposure to vehicle control DMSO (A′), FGFR inhibitor PD173074 (A″), or MEK antagonist PD184352 (A′″); Bra expression in tailbud explants following exposure to DMSO (B), PD173074 (B′), or PD184352 (B″). Arrow indicates normal down regulation of Bra in CNH in DMSO control; nc, notochord; mp, mesoderm pro... |
| 15:21, 18 December 2024 | Dynamics of Sox2 and Bra expression in chick and human tailbuds.png (file) |  |
4.94 MB | {{Information |Description=Figure 2. Dynamics of Sox2 and Bra expression in chick and human tailbuds. (A–D) Neural progenitor marker Sox2 mRNA expands into the mesoderm progenitor domain from HH24 (arrows in A′ and B′) analysed in HH22–27 stages in wholemount (A–D) and in medial saggital sections (SS) (A′–D′) at low and high magnification. The mesoderm progenitor marker Brachyury (Bra) is expressed in notochord, CNH, and caudal presomitic mesoderm at HH22. Expression is lost from the distal... |
| 22:01, 17 December 2024 | Key tailbud cell populations and changing FGF pathway ligand expression and activity in the maturing tailbud.png (file) |  |
3.09 MB | {{Information |Description=Figure 1. Key tailbud cell populations and changing FGF pathway ligand expression and activity in the maturing tailbud. (A) Schematic of key tailbud tissues; chordoneural hinge (red dashed line) consists of caudal-most ventral neural tissue and distal end of notochord (black dashed line within red dashed line) and presomitic mesoderm progenitors (yellow dashed line). These cell populations are defined by position, morphology, and their fates, following mapping stud... |
| 02:05, 17 December 2024 | The function of GDF11 in various cells.jpg (file) |  |
1.13 MB | {{Information |Description=Figure 2 The function of GDF11 in various cells. (A). GDF11 is involved in the occurrence and development of liver cancer, pancreatic cancer, esophageal cancer, breast cancer, colon cancer, and melanoma. (B). The regulatory effect of GDF11 on cardiomyocytes. (C). The regulatory effects of GDF11 on stem cells, chondrocytes, erythrocytes, and macrophages. (D). The regulatory effect of GDF11 on endothelial cells. Created with BioRender.com |Source= https://www.frontier... |
| 18:28, 16 December 2024 | Analysis of the BMP signaling pathway.jpg (file) |  |
198 KB | {{Information |Description=Analysis of the BMP signaling pathway. (A) Quantification of P-SMAD1/5/8 immunohistochemistry on sagittal sections of musculus flexor carpi ulnaris of Noggin+/+ and Noggin−/− mice at the three different stages investigated. Values plotted as mean ± SEM; n = 5; *p < 0.05. Representative immunohistochemistry for P-SMAD1/5/8 at 16.5 dpc in Noggin+/+ (B) and Noggin−/− muscle (C). Enlargement of muscle area delineated in black in B’ and C’. Muscle is delineated in red,... |
| 11:31, 16 December 2024 | Noggin. Analysis of the muscle fiber thickness.jpg (file) |  |
691 KB | {{Information |Description=Figure 1. Noggin in mice. Analysis of the muscle fiber thickness. (A,B) The limb at 15–16 dpc using Jatlasviewer. The musculus flexor carpi ulnaris is colored in red. (C–E’) H&E staining on sagittal sections of the limbs at the indicated stages and genotype. The musculus flexor carpi ulnaris is digitally indicated in green. (F–H’) Actin immunofluorescence on cross-sections of muscles at the indicated stages. (I) Quantification using ImageJ of the thickness of the f... |
| 22:17, 15 December 2024 | The suggested new signaling pathways induced by Noggin in human ASC osteogenic cultures.png (file) |  |
688 KB | {{Information |Description=Figure 7. The suggested new signaling pathways induced by Noggin in human ASC osteogenic cultures. We have demonstrated that Noggin can activate FGFR2 receptors and Src kinase associated with the receptor complex. This results in ERK1/2 phosphorylation and, independently of PI3k, Akt kinase phosphorylation. It is known that dexamethasone, a component of osteogenic medium, stimulates RUNX2 and TAZ expressions. We have shown Noggin activation of Akt that leads to bloc... |
| 21:52, 15 December 2024 | Hypothesized Noggin binding to the cell surface receptor FGFR2.jpg (file) |  |
230 KB | {{Information |Description=Figure 5. Hypothesized Noggin binding to the cell surface receptor FGFR2. (a) Molecular docking simulation of Noggin protein (PDB ID: 1M4U) and fibroblast growth factor receptor type 2 (PDB ID:1E0O). Results obtained with the use of ClusPro web server and visualized in Chimera. (b) Organization of FGFRs and Noggin proteins (cartoon representation) with heparin molecules (yellow stick representation) and possible heparan sulfate proteoglycans (HSPGs) connection withi... |
| 19:59, 15 December 2024 | Noggin genetically interacts with Ror2.jpg (file) |  |
411 KB | {{Information |Description=Figure 1. Noggin genetically interacts with Ror2. Skeletal preparations of E18.5 embryos of the indicated allelic combinations are shown. Cartilage stains blue, bone stains red. (A) Top panel: Limbs of compound Ror2 and Noggin heterozygous mutants have a normal appearance. Ror2−/− skeletal elements are visibly shortened and enlarged. Bottom panel: magnifications of humerus and radius/ulna. The width of the wild type or single heterozygous skeletal elements is indica... |
| 21:27, 13 December 2024 | Ectopic bone formation analyses.png (file) |  |
6.81 MB | {{Information |Description=Figure 6. Ectopic bone formation analyses. A: Bone formation capability of muscle-derived cells. Representative histological sections of a scaffold loaded with BMSCs or MuSCs cultured with both dexamethasone and BMP-2. Scale bar: 1 mm (left panels), 200 μm (middle panels) and 50 μm (right panels). Black arrows indicate new bone formation in the scaffold. Black arrow heads indicate osteocytes and green arrow heads indicate bone lining cells. B: Newly formed bone, T:... |
| 19:39, 13 December 2024 | Involvement of bone morphogenetic protein (BMP) antagonistic signaling in anterior subcapsular cataract (ASC) and posterior capsular opacification (PCO) progression.png (file) | _antagonistic_signaling_in_anterior_subcapsular_cataract_(ASC)_and_posterior_capsular_opacification_(PCO)_progression.png) |
1.93 MB | {{Information |Description=Figure 4. Involvement of bone morphogenetic protein (BMP) antagonistic signaling in anterior subcapsular cataract (ASC) and posterior capsular opacification (PCO) progression. |Source=https://www.mdpi.com/2073-4409/10/10/2604# Shu, D.Y.; Lovicu, F.J. Insights into Bone Morphogenetic Protein—(BMP-) Signaling in Ocular Lens Biology and Pathology. Cells 2021, 10, 2604. https://doi.org/10.3390/cells10102604 |Date=2021-09-30 |Author=Shu, D.Y.; Lovicu, F.J. |Permission=... |
| 18:30, 13 December 2024 | Involvement of bone morphogenetic protein (BMP) signaling in lens development.png (file) | _signaling_in_lens_development.png) |
3.36 MB | {{Information |Description=Figure 3. Involvement of bone morphogenetic protein (BMP) signaling in lens development. |Source=https://www.mdpi.com/2073-4409/10/10/2604# Shu, D.Y.; Lovicu, F.J. Insights into Bone Morphogenetic Protein—(BMP-) Signaling in Ocular Lens Biology and Pathology. Cells 2021, 10, 2604. https://doi.org/10.3390/cells10102604 |Date=2021-09-30 |Author=Shu, D.Y.; Lovicu, F.J. |Permission= |other_versions= }} {{Licensereview}} © 2021 by the authors. Licensee MDPI, Basel, Sw... |
| 18:26, 13 December 2024 | Bone Morphogenetic Protein—(BMP-) Signaling in Ocular Lens.png (file) | _Signaling_in_Ocular_Lens.png) |
485 KB | {{Information |Description=Figure 1. Graphical Abstract. Bone Morphogenetic Protein—(BMP-) Signaling in Ocular Lens |Source=https://www.mdpi.com/2073-4409/10/10/2604# Shu, D.Y.; Lovicu, F.J. Insights into Bone Morphogenetic Protein—(BMP-) Signaling in Ocular Lens Biology and Pathology. Cells 2021, 10, 2604. https://doi.org/10.3390/cells10102604 |Date=2021-09-30 |Author=Shu, D.Y.; Lovicu, F.J. |Permission= |other_versions= }} {{Licensereview}} © 2021 by the authors. Licensee MDPI, Basel, Sw... |
| 18:20, 13 December 2024 | Transforming growth factor beta (TGFβ) and bone morphogenetic protein (BMP) receptor signal transduction.png (file) | _and_bone_morphogenetic_protein_(BMP)_receptor_signal_transduction.png){kind=spacer} |
2.42 MB | {{Information |Description=Figure 2. Transforming growth factor beta (TGFβ) and bone morphogenetic protein (BMP) receptor signal transduction. TGFβ and BMP bind to their respective type I and II receptors to activate the downstream canonical Smad-signaling to initiate gene transcription by binding various co-activators and co-repressors. While TGFβ activates Smad2/3 and BMP activates Smad1/5/8, both require the common Smad, Smad4, to form a complex for nuclear translocation. Inhibitory Smads... |
| 11:43, 13 December 2024 | Histology images (PAS (A) and von Kossa (B) staining) under 10-fold magnification).png (file) | _and_von_Kossa_(B)_staining)_under_10-fold_magnification).png) |
6.1 MB | {{Information |Description=Figure 3. Histology images (PAS (A) and von Kossa (B) staining) under 10-fold magnification). The scale bars in the right column indicate 120 μm. The tendon specimens revealed an increased formation of extracellular matrix (*) after stimulation with BMP-7 at week 4 (bT+BMP and pOB+bT+BMP). Stimulation with BMP-7 led to intratendinous calcification (arrowhead). At 8 weeks, limited extracellular matrix formation was found in monoculture without BMP (bT-BMP), whereas... |
| 08:43, 13 December 2024 | The emerging role of BMP signaling during osteoclastogenesis and osteoblast-osteoclast coupling.jpg (file) |  |
152 KB | {{Information |Description=Figure 1. The emerging role of BMP signaling during osteoclastogenesis and osteoblast-osteoclast coupling. Conditional knockout models and cell culture studies indicate a vital role of canonical and non-canonical BMP signaling in osteoclastogenesis. Several distinct BMP ligands, BMP receptors, BMP inhibitors and downstream mediators regulate osteoclast differentiation, fusion, and resorption activity as well as osteoblast-osteoclast coupling. |Source=https://www.fro... |
| 21:33, 11 December 2024 | Load Spatially Controls Resorption and Deposition.png (file) |  |
803 KB | {{Information |Description=FIGURE 2. Load Spatially Controls Resorption and Deposition. Unloaded osteocytes secrete sclerostin, preventing osteoblast differentiation. Disinhibited RANKL expression allows for increased osteoclast differentiation and resorption. Load suppresses local sclerostin expression, allowing osteoblast differentiation. Local osteoclastic resorption and differentiation are downregulated through reduced RANKL availability. Bolded arrows indicate upregulated pathways for gi... |
| 21:28, 11 December 2024 | Loading Supports Osteoblast Differentiation and Suppresses Osteoclast Differentiation.png (file) |  |
637 KB | {{Information |Description=FIGURE 1. Loading Supports Osteoblast Differentiation and Suppresses Osteoclast Differentiation. In unloaded bone, sclerostin and RANKL expression is upregulated, supporting osteoclastogenesis and resorption. Following load, osteoblast and osteocyte differentiation increases, while osteoblast apoptosis and osteoclast differentiation decreases, leading to bone matrix deposition. Osteoblasts may embed and mature into osteocytes within the newly formed bone or may tran... |
| 20:29, 11 December 2024 | Sclerostin are involved in the mechanism of osteoporosis.png (file) |  |
451 KB | {{Information |Description=Figure 1. Sclerostin are involved in the mechanism of osteoporosis. Sclerostin binds to LRP5/6 coreceptors, acts on the WNT signaling pathway, inhibits osteoblasts and promotes osteoclastogenesis, leading to osteoporosis. |Source=https://www.frontiersin.org/journals/endocrinology/articles/10.3389/fendo.2024.1491066/full Li Y, Luo Y, Huang D and Peng L (2024) Sclerostin as a new target of diabetes-induced osteoporosis. Front. Endocrinol. 15:1491066. doi: 10.3389/fen... |
| 20:08, 11 December 2024 | Canonical and non-canonical Wnt signaling pathways (01).png (file) | .png) |
2.3 MB | {{Information |Description=Figure 1. Canonical and non-canonical Wnt signaling pathways. (a) Wnt signaling OFF: If there is no Wnt ligand, or if sclerostin prevents its binding to the receptor complex, the destruction complex Axin-APC-CK1α-GSK3 phosphorylates β-catenin, targeting it for ubiquitination and degradation by the proteasome. (b) Wnt signaling ON: Canonical Wnt signaling is activated by Wnt ligands binding to Frizzled receptors and LRP5/6 co-receptors, resulting in the recruitment o... |
| 18:39, 11 December 2024 | WNT ON-active signaling pathway extracellular Wnt proteins bind to LRP56 and frizzled (FZD) receptors, and form an active Wnt-FZD-LRP56 receptor system.jpg (file) | _receptors,_and_form_an_active_Wnt-FZD-LRP56_receptor_system.jpg) |
666 KB | {{Information |Description=Figure 2 WNT ON-active signaling pathway: extracellular Wnt proteins bind to LRP5/6 and frizzled (FZD) receptors, and form an active Wnt-FZD-LRP5/6 receptor system leading to accumulation of the active form of β-catenin and its translocation to the cell nucleus. Attachment of β-catenin to the transcription factor TCF activates transcription of Wnt pathway target genes. WNT OFF – inactive signaling pathway: sclerostin binds to LRP5/6 receptors on the cell surface pre... |
| 18:19, 11 December 2024 | Influence of sclerostin on bone formation and resorption.jpg (file) |  |
461 KB | {{Information |Description=Figure 1 Influence of sclerostin on bone formation and resorption: inhibiting proliferation and differentiation of mesenchymal cells to osteoblasts, keeping the bone lining cells in dormant state, inhibition of bone matrix formation, inhibition of ostoblasts differentiation to osteocytes, promoting osteoblast apoptosis, and stimulating bone resorption. |Source=https://www.frontiersin.org/journals/endocrinology/articles/10.3389/fendo.2022.954895/full Oniszczuk A, Ka... |
| 22:03, 10 December 2024 | Sclerostin. An inhibitor of canonical Wnt signaling pathway.jpg (file) |  |
305 KB | {{Information |Description=Figure 1 Sclerostin: an inhibitor of canonical Wnt signaling pathway. Wnt-LRP5/6-Fz complex elicits a molecular cascade that transfer Axin-mediated destruction complex, which is essential to β-catenin degradation, to the plasma membrane. Increased β-catenin moves into the nucleus, where it represents the molecular mechanism that β-catenin binds to TCF/LEF, which are the main partners of β-catenin to serve the transcriptional function of canonical Wnt signaling pathw... |
| 20:23, 10 December 2024 | The role of sclerostin in Wntβ-catenin signaling.png (file) |  |
264 KB | {{Information |Description=Figure 1. The role of sclerostin in Wnt/β-catenin signaling. |Source=https://link.springer.com/article/10.1186/s12967-023-04563-z Wu, D., Li, L., Wen, Z. et al. Romosozumab in osteoporosis: yesterday, today and tomorrow. J Transl Med 21, 668 (2023). https://doi.org/10.1186/s12967-023-04563-z |Date=2023-09-27 |Author=Wu, D., Li, L., Wen, Z. et al. |Permission= |other_versions= }} {{Licensereview}} Open Access This article is licensed under a Creative Commons Attrib... |
| 20:07, 10 December 2024 | The role of sclerostin in bone.png (file) |  |
356 KB | {{Information |Description=Figure 2. The role of sclerostin in bone. |Source=https://link.springer.com/article/10.1186/s12967-023-04563-z Wu, D., Li, L., Wen, Z. et al. Romosozumab in osteoporosis: yesterday, today and tomorrow. J Transl Med 21, 668 (2023). https://doi.org/10.1186/s12967-023-04563-z |Date=2023-09-27 |Author=Wu, D., Li, L., Wen, Z. et al. |Permission= |other_versions= }} {{Licensereview}} Open Access This article is licensed under a Creative Commons Attribution 4.0 Internati... |
| 17:59, 10 December 2024 | Upper panel Trabecular surfaces (L2) of OVX rats treated with vehicle or Scl-Ab.png (file) | _of_OVX_rats_treated_with_vehicle_or_Scl-Ab.png) |
341 KB | {{Information |Description=Figure 2. Upper panel Trabecular surfaces (L2) of OVX rats treated with vehicle or Scl-Ab. Surfaces were characterized as modeling-based bone formation (MBF), remodeling-based bone formation (RBF), quiescent (QS) or osteoclastic (OCs), and expressed as % of the total surface. Lower panel Endocortical surfaces (proximal diaphysis) of male cynomolgus monkeys. Bone surfaces are characterized as modeling-based bone formation (MBF), remodeling-based bone formation (RBF),... |
| 11:25, 10 December 2024 | Schematic presentation of the canonical Wnt-signaling pathway and of the effect of sclerostin on bone cells.png (file) |  |
203 KB | {{Information |Description=Figure 1. Schematic presentation of the canonical Wnt-signaling pathway and of the effect of sclerostin on bone cells. a Wnts bind to the receptor complex of frizzled (FZD) and LRP5/6, prevent the degradation of beta-catenin, and increase its accumulation in the cytoplasm; beta-catenin is translocated to the nucleus where it associates with transcription factors to control transcription of target genes in osteoblasts. b Osteocyte-produced sclerostin is transported t... |
| 11:12, 10 December 2024 | Bone remodeling and modeling under physiological conditions, in osteoporosis, and during treatment with sclerostin inhibitors.png (file) |  |
371 KB | {{Information |Description=Figure 3. Bone remodeling and modeling under physiological conditions, in osteoporosis, and during treatment with sclerostin inhibitors. a Within an active BMU bone is constantly removed by osteoclasts (OCs) and new bone matrix is produced by osteoblasts (OBs), at sites where bone resorption has occurred with the amount of bone formed being equal to the amount of bone resorbed. Once the BMU is completed, osteoblasts become entrapped as osteocytes (OCYs) into the new... |
| 21:44, 6 December 2024 | Bone regeneration-Bone remodeling cycle II-Pre-Osteoblast Osteoblast Bone-lining cell etc --Smart-Servie cropped.jpg (file) |  |
2.18 MB | {{Artwork |author = {{Institution:Laboratoires Servier}} |title = |description = {{en|1=Bone structure - Bone regeneration - Bone remodeling cycle II - Endosteal sinus Monocyte Pre-osteoclast Osteocyte Osteoclast Macrophage Pre-osteoblast Osteoblast Bone-lining cell Osteoid New bone Old bone}} {{fr|1=Structure osseuse - Cycle de remodelage osseux II - Sinus endosté Monocyte Pré-ostéoclaste Ostéocyte Ostéoclaste Macrophage Pré-ostéoblaste Ostéoblaste Cellule... |
| 21:48, 5 December 2024 | Structure of the V-ATPase proton pump.jpg (file) |  |
365 KB | {{Information |description=Figure 3. Structure of the V-ATPase proton pump. The V-ATPase complex is composed of two domains: the peri-membranous V1 domain composed of subunits A to H responsible for the hydrolysis of ATP shown in blue, and the intramembranous V0 domain who allows the translocation of protons across the membrane shown in purple in the diagram. The V0 domain is composed of the subunits a, e, d and of a hexameric ring formed by subunits c, c′ and c″. |date=2021-02-26 |source= ht... |
| 21:45, 5 December 2024 | Ins and outs of membrane transport proteins in osteoclasts.jpg (file) |  |
964 KB | {{Information |description=FFigure 2. Ins and outs of membrane transport proteins in osteoclasts. (A) Schema depicting the major types of transport proteins and their modes of substrate movement across biological membranes. (B) Model summarizing the reported membrane localization of all the major membrane transport proteins expressed in osteoclasts. Known substrates are indicated in gray. Intracellular compartments correspond to: ER, endoplasmic reticulum; SL, Secretory lysosome; LE, Late end... |
| 21:43, 5 December 2024 | Anatomy of the Osteoclast.jpg (file) |  |
362 KB | {{Information |description=Figure 1. Anatomy of the Osteoclast. Illustration of the unique configuration and membrane organization of an osteoclast during active bone resorption. The osteoclast’s specialized plasma membrane domains are labeled and color-coded: Purple = the functional secretory domain, Orange = the basolateral membrane, Yellow = the sealing zone and Green = the ruffled border membrane. Created with BioRender.com. |date=2021-02-26 |source= https://www.frontiersin.org/journals/c... |
| 21:38, 5 December 2024 | Key mediators of osteoblast-osteoclast interaction.png (file) |  |
502 KB | {{Information |description=Figure 2. Key mediators of osteoblast-osteoclast interaction. Osteoblast-osteoclast communications are essential for fine-tuning of bone remodeling during bone homeostasis. (1) Osteoblasts and osteoclasts have direct contacts through the interactions between EFNB2-EPHB4, FAS-FASL and NRP1-SEMA3A to regulate cell proliferation, differentiation, and survival. (2) Osteoclast-mediated bone resorption releases TGF-β and IGF-1 from bone matrix to induce osteoblast-mediate... |
| 21:36, 5 December 2024 | Strategies of osteoclastogenesis and osteoblastogenesis.png (file) |  |
740 KB | {{Information |description=Figure 1. Strategies of osteoclastogenesis and osteoblastogenesis. (a) Osteoclastogenesis. Osteoclasts are tissue-specific macrophages derived from hematopoietic stem cells. In the presence of M-CSF, hematopoietic stem cells are committed to macrophage colony-forming units (CFU-M), the common precursor cells of macrophages and osteoclasts. When activated by the RANKL-RANK signal, CFU-M is further differentiated into mononucleated osteoclasts and subsequently fuse to... |
| 16:08, 5 December 2024 | Tissus osseux nl txt.png (file) |  |
204 KB | {{Information |description={{fr|1=Schéma du tissus osseux}} nl txt |date=2023-09-25 |source=Biology 2e, OpenStax, Rice University (https://openstax.org/details/books/biology-2e) |author=Mary Ann Clark, Texas Wesleyan University, Matthew Douglas, Grand Rapids Community College, Jung Choi, Georgia Institute of Technology. Rasbak nl txt |permission= |other versions=thumb|left|150px }} =={{int:license-header}}== {{cc-by-4.0}} [[Category:Medical illustr... |
