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24 results for “calreticulin”
Structural variants of calreticulin mutants associated with essential thrombocythemia
<p>Video S1. CALRwt molecular simulation with Ca2+ ions binding to the structure. This movie shows the dynamics of Ca2+ ions over the 40 ns and how they rapidly bind to the CALRwt structure. Most of the ions bind to the C-terminal part of CALRwt, where the majority of the negative residues are located. The binding of Ca2+ ions creates an interaction between residues that can induce specific folding. In this example, residues E407 and E416 interact with a calcium ion and fold, as shown at the end of the movie.</p> <p>Video S2. CALRwt molecular simulation with calcium ions binding to the structure. This movie shows the dynamics of CALRwt and Ca2+ ions over 400 ns and how ions are rapidly bound to the CALRwt structure. Most of the ions bind to the C-terminal region of CALRwt, where the majority of the negative residues are located. The binding of calcium ions creates an interaction between residues that can induce specific folding (a specific example of fold is shown on Video S1). On this full movie, we are able to see the unfolding of the N-terminal region of the helix and the stabilization of the C- terminal region thanks to calcium binding.</p> <p>Video S3. CALRwt molecular simulation with Na+ ions. This movie shows the dynamics of CALRwt with Na+ ions. The absence of binding from calcium ions leaves the structure free of any external constraint, especially for the C-terminal region. The latter appears to be flexible but this region is in fact quite stable at the local level and has its own dynamics, unstructured slightly the C-terminal of the helix.</p> <p>Video S4. CALRm class A molecular simulation. This movie shows the dynamics of CALRm class A over 400ns. The C-terminal region of the structure is quite flexible at first and interacts with the N-terminal region after several ns. This interaction locally constrains the structure around residues 400-404, stabilizing an unstructured structure for this region.</p> <p>Video S5. CALRm class B molecular simulation. This movie shows the dynamics of CALRm class B over 400ns. The first and last helices move away from their initial position with great flexibility of the coiled regions between the helices. The first helix interacts closely with the second helix and forms a specific T-shaped fold which stabilize the whole structure.</p> <p>Video S6. CALRm class C molecular simulation. This movie shows the dynamics of CALRm class C over 400ns. Extremities are highly flexible but the helix remains stable. This high flexibility allow the C- terminal region to have some interaction with the helix at some frames</p> <p>Video S7. CALRm class D molecular simulation. This movie shows the dynamics of CALRm class D over 400ns. The C-terminal region appears to be flexible, but the helix remains stable the whole simulation.</p> <p>Video S8. CALRm class E molecular simulation. This movie shows the dynamics of CALRm class E over 400ns. This movie shows the dynamics of CALRm class E and calcium ions over 400 ns and how ions are rapidly bound to the CALRwt structure. Most of the ions bind to the C-terminal region of CALRm class E, where the majority of the negative residues are located. The N-terminal region of the helix is being unstructured and the C-terminal region is stabilized with calcium ions. This simulation of CALRm class E is very similar to the simulation of CALRwt.</p> <p>Video S9. Dimeric form of CALRm class A molecular simulation. This movie shows the dynamics of two CALRm class A monomers forming a dimer through disulphide bonds. Both chains seem to repulse each other due to electrostatic charges, but disulphide bonds maintain the dimeric form, otherwise both chains would have been separated.</p> <p>Video S10. Dimeric form of CALRm class A with broken disulphide bonds molecular simulation. This movie shows the dynamics of two CALRm class A monomers and their attempt to form a dimer with broken disulfide bonds. As each monomer repels each other, the dimeric form cannot be stable without any disulfide bonds. This is demonstrated by the separation of each chain from each other.</p> <p>Video S11. Dimeric form of CALRm class B molecular simulation. This movie shows the dynamics of two CALRm class B monomers forming a dimer through disulphide bonds. Both chains are interacting together to form a specific shape, similar to the simulation of the monomer of class B. This interaction implies that even without any disulphide bonds, the dimeric form of class B could be stable, contrary to class A.</p> <p>Video S12. Dimeric form of CALRm class B molecular simulation. It is an interesting replicate of the same system than Video S11. Helices are also well maintained.</p> <p>Video S13. Dimeric form of CALRm class C molecular simulation. This movie shows the dynamics of two CALRm class C monomers forming a dimer through disulphide bonds. Both chains seem to repulse each other due to electrostatic charges, but disulphide bonds maintain the dimeric form, otherwise both chains would have been separated.</p> <p>Video S14. Dimeric form of CALRm class E molecular simulation. This movie shows the dynamics of two CALRm class E monomers and their attempt to form a dimer without any disulphide bonds. Chains repel and are moving away from each other after several ns, indicating the inability for class E to form a dimer.</p> <p>Video S15. Dimeric form of CALRwt molecular simulation. This movie shows the dynamics of two CALRwt monomers and their attempt to form a dimer. Some interactions occur between the N- terminus of each chain, but this is not sufficient and the chains move away from each other. Subsequently, the dynamics of each chain resembles the dynamics of the CALRwt monomer simulated with sodium ions (Video S2). CALRwt is not able to be stable as dimer.</p> <p>Video S16. Dimeric form of CALRm class D molecular simulation. This movie shows the dynamics of two CALRm class D monomers and their attempt to form a dimer without any disulphide bonds. Both chains are separated very quickly which indicate that they can not be stable as dimer.</p>
Data from Native adiponectin in serum binds to mammalian cells expressing T-cadherin, but not AdipoRs or calreticulin
<p>Adiponectin is an adipocyte-derived atypically abundant circulating factor that protects various organs and tissues through its receptors, AdipoRs, calreticulin, and T-cadherin. To identify the major binding partner of circulating native adiponectin, we expressed these receptors on the surface of HEK293 cells. Adiponectin, either that in mouse or human serum, purified from serum, or produced by mammalian cells, bound to cells expressing T-cadherin, but not to those expressing AdipoR1 or calreticulin. The stable introduction of T-cadherin and AdipoR1 into CHO cells resulted in the cell surface localization of these receptors. Native adiponectin in serum bound to cells expressing T-cadherin, not to those expressing AdipoR1. The knockdown of T-cadherin, but not AdipoRs resulted in the significant attenuation of native adiponectin binding to C2C12 myotubes. Therefore, native adiponectin binding depended on the amount of T-cadherin expressed in HEK293 cells, CHO cells, and C2C12 myotubes. Collectively, our mammalian cell-based studies suggest that T-cadherin is the major binding partner of native adiponectin in serum.</p> <p> </p>
Oncogenic calreticulin induces TGF-β expression and Treg expansion in the bone marrow microenvironment as a mechanism of immune escape
<p>This repository contains all necessary scRNA-seq inputs to reproduce the results described in "Oncogenic calreticulin induces TGF-β expression and Treg expansion in the bone marrow microenvironment as a mechanism of immune escape" by Schmidt et al. (Cancer Research 2024). </p> <p>Content:</p> <ol> <li>"MPN_calreticulin_bm.R" --> R script containing all code</li> <li>"cells_table.RDS" --> cells table containing, cell_id, UMAP coordinates, complexity, cell type annotation and metadata</li> <li>"normalized_matrix.RDS" --> quality control filtered, log2-normalized and centered expression matrix</li> <li>"reference_signatures.RDS" --> all external signatures used for this study</li> <li>"EV2_*", "EV5_*", "MPN2_*", "MPN5_*", --> cellranger outputs</li> </ol>
Data from Native adiponectin in serum binds to mammalian cells expressing T-cadherin, but not AdipoRs or calreticulin
Open the record for dataset details and reuse information.
A genome wide CRISPR/Cas9 screen identifies calreticulin as a selective repressor of ATF6⍺
GEO Series GSE254745. Cricetulus griseus. 16 samples. Type: Other.
Human MCF7 cells: Mock control vs. siRNA transfected against calreticulin
GEO Series GSE44371. Homo sapiens. 3 samples. Type: Expression profiling by array.
RNA-seq analysis of Calreticulin(Calr) knockout LLC cells identified ER stress response
GEO Series GSE285113. Mus musculus. 6 samples. Type: Expression profiling by high throughput sequencing.
Type 2 calreticulin mutations activate ATF6 to promote BCL-xL-mediated survival in myeloproliferative neoplasms
GEO Series GSE288386. Homo sapiens. 37 samples. Type: Expression profiling by high throughput sequencing.
Programed cell removal of Neutrophils regulated by calreticulin
GEO Series GSE95631. Mus musculus. 12 samples. Type: Expression profiling by high throughput sequencing.
Physical interaction between mutant calreticulin and the thrombopoietin receptor is required for transformation of hematopoietic cells
GEO Series GSE74890. Mus musculus. 12 samples. Type: Expression profiling by high throughput sequencing.
Oncogenic Calreticulin Induces Immune Escape by Stimulating TGF-β Expression and Regulatory T Cell Expansion in the Bone Marrow Microenvironment
GEO Series GSE241365. Mus musculus. 12 samples. Type: Expression profiling by array; Expression profiling by high throughput sequencing.
Oncogenic Calreticulin Induces Immune Escape by Stimulating TGF-β Expression and Regulatory T Cell Expansion in the Bone Marrow Microenvironment - scRNAseq
GEO Series GSE241364. Mus musculus. 4 samples. Type: Expression profiling by high throughput sequencing.
Gene expression analysis of cardiac-specific calreticulin transgenic mice
GEO Series GSE82188. Mus musculus. 6 samples. Type: Expression profiling by array.
A Study of JNJ-88549968 for the Treatment of Calreticulin (CALR)-Mutated Myeloproliferative Neoplasms
ClinicalTrials.gov study NCT06150157. IPD Sharing: YES. Countries: 8. Publications: 0.
Study the effect of calreticulin knockdown on genome-wide transcript expression in HepG2 cells
GEO Series GSE57261. Homo sapiens. 6 samples. Type: Expression profiling by array.
Calreticulin Ins5 and Del52 mutations impair unfolded protein and oxidative stress responses in K562 cells expressing CALR mutants.
GEO Series GSE127250. Homo sapiens. 18 samples. Type: Expression profiling by array.
Oncogenic Calreticulin Induces Immune Escape by Stimulating TGF-β Expression and Regulatory T Cell Expansion in the Bone Marrow Microenvironment - microarray
GEO Series GSE241162. Mus musculus. 8 samples. Type: Expression profiling by array.
Expression data from C. elegans harboring type 1-like and type 2-like calreticulin mutations of MPN patients
GEO Series GSE201599. Caenorhabditis elegans. 10 samples. Type: Expression profiling by array.
Expression data from wild type and calreticulin deficient murine embryonic stem cells
GEO Series GSE13805. Mus musculus. 7 samples. Type: Expression profiling by array.
Aberrant Calreticulin expression in articular cartilage of Dio2 deficient mice
GEO Series GSE79239. Mus musculus. 20 samples. Type: Expression profiling by array.
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