Matriks Jordan Dan Aplikasinya Pada Sistem Linier Waktu Diskrit

Matrix is diagonalizable (similar with matrix diagonal) if and only if the sum of geometric multiplicities of its eigenvalues is n.If we search for an upper triangular form that is nearly diagonal as possible but is still attainable by similarity for every matrix, especially the sum of geometric multiplicities of its eigenvalues is less than n, the result is the Jordan canonical form, which is denoted by , and . In this paper, will be described how to get matrix S(in order to get matrix ) by using generalized eigenvector. In addition, it will also describe the Jordan canonical form and its properties, and some observation and application on discrete time linear system

The Prognosis of Breast Cancer Patients after Mastectomy and Immediate Breast Reconstruction: A Meta-Analysis

<div><p>Background</p><p>An increasing number of patients with breast cancer are being offered immediate breast reconstruction (IBR). The aim of this study was to analyze the impact of IBR on the prognosis of patients with breast cancer.</p><p>Methods</p><p>We searched the electronic databases of Medline (Pubmed), ISI Web of Knowledge, Embase, and Google Scholar databases for studies reporting the overall recurrence, disease-free survival (DFS), and overall survival (OS) of patients after mastectomy only and mastectomy with IBR. With these data, we conducted a meta-analysis of the clinical outcomes.</p><p>Results</p><p>Fourteen studies, including 3641 cases and 9462 controls, matched our criteria. Relevant information was extracted from these 14 studies. There was no significant heterogeneity (P for Q-statistic > 0.10 and I² < 25%). Patients who underwent IBR showed no increased risk of overall recurrence of breast cancer (RR = 0.89; 95% confidence interval [CI]: 0.75, 1.04; <i>P</i> = 0.14). Furthermore, patients receiving IBR had similar DFS (RR = 1.04; 95%CI: 0.99, 1.08); <i>P</i> = 0.10) and OS (RR = 1.02; 95%CI: 0.99, 1.05; <i>P</i> = 0.24)) as those of control patients.</p><p>Conclusion</p><p>This meta-analysis provides evidence that IBR does not have an adverse effect on prognosis. These data suggest that IBR is an appropriate and safe choice for patients with breast cancer.</p></div

Sensitive analysis by excluding each single study.

<p>Sensitive analysis by excluding each single study.</p

A Forest plot of the pooled RR of OS for the IBR and Control group

<p>A Forest plot of the pooled RR of OS for the IBR and Control group</p

A Forest plot of the pooled RR of DFS for the IBR and Control groups.

<p>A Forest plot of the pooled RR of DFS for the IBR and Control groups.</p

Structural Insights into the Assembly of CARMA1 and BCL10

<div><p>The CBM complex (CARMA1, BCL10 and MALT1) plays a crucial role in B and T lymphocyte activation. CARMA1 serves as a scaffold for BCL10, MALT1 and other effector proteins and regulates various signaling pathways related to the immune response. The assembly of CARMA1 and BCL10 is mediated through a CARD-CARD interaction. Here, we report the crystal structure of the CARD domain of CARMA1 at a resolution of 1.75 Å. The structure consists of six helices, as previously determined for CARD domains. Structural and computational analysis identified the binding interface between CARMA1-CARD and BCL10-CARD, which consists of a basic patch in CARMA1 and an acidic patch in BCL10. Site-directed mutagenesis, co-immunoprecipitation and an NF-κB activation assay confirmed that the interface is necessary for association and downstream signaling. Our studies provide molecular insight into the assembly of CARMA1 and BCL10.</p> </div

The binding surface of CARMA1-CARD.

<p>(<b>A</b>) The representative basic residues (R35, K41, K69 and R72) on the positive surface of the CARMA1-CARD are colored blue. (<b>B</b>) Interactions between the basic residues and surrounding sulfate ions. The side chains of basic residues R35, K41, K69 and R72 and sulfate ions are shown as sticks. The oxygen atoms and sulfur atoms are colored red and yellow, respectively. Hydrogen bonds are shown as red dashed lines. (<b>C</b>) Sequence alignment of CARMA1-CARD proteins from different species. The conserved amino acids are highlighted in red. Conserved residues in the basic patch are denoted with asterisks.</p

Association of CARMA1 and BCL10.

<p>(<b>A</b>) Co-IP analysis of interactions between BCL10-CARD and variants of CARMA1-CARD. HEK293T cells were transiently co-transfected with GFP-tagged BCL10-CARD and wild type or mutants of Myc-tagged CARMA1-CARD constructs. Cell extracts were immunoprecipitated using an anti-Myc antibody and blotted using anti-GFP. (<b>B</b>) Co-IP analysis of interactions between Myc-tagged CARMA1-CARD and wild type or mutants of GFP-tagged BCL10-CARD constructs. (<b>C,D</b>) Bar graph displaying interactions between CARMA1-CARD and BCL10-CARD. (<b>E</b>) The effect of wild type and mutants of CARMA1 on the NF-κB reporter assay. (<b>F</b>) The effect of wild type and mutants of BCL10 on NF-κB activity. RLU: relative luciferase unit; Luc: firefly luciferase activity; and Ren: Renilla luciferase activity. The error bars indicate the standard error of the mean (n = 3 separate experiments). * indicates a P value<0.05, ** indicates a P value<0.001. (<b>G, H</b>) The expression levels of CARMA1 and BCL10 in NF-κB assays were checked by immunoblotting with anti-GFP, anti-MYC and anti-GAPDH antibodys, respectively.</p

Data collection and refinement statistics.

a<p>the highest resolution shell.</p>b<p>.</p>c<p><b><i>R</i></b>_crystal = .</p>d<p><b><i>R</i></b>_free, calculated the same as <b><i>R</i></b>_crystal, but from a test set containing 5% of data excluded from the refinement calculation.</p

The binding surface of BCL10-CARD.

<p>(<b>A</b>) Superposition of homology models of BCL10-CARD. The computational results from the programs MODELLER and SWISS-MODEL are represented with green and blue cartoon models, respectively. (<b>B</b>) The electrostatic surface of BCL10-CARD. Red: negative; blue: positive; and white: neutral. Residues E50, E53 and E54 are labeled. (<b>C</b>) Sequence alignment of BCL10-CARD proteins from different species. The conserved amino acids are highlighted with red, and the conserved acidic residues that make up the acidic patch are denoted with asterisks. (<b>D</b>) Protein docking models of the CARMA1-CARD and BCL10-CARD calculated using the ZDOCK server. CARMA1-CARD and BCL10-CARD are colored magenta and gray, respectively. Three out of ten best scoring complexes place the BCL10-CARD domain approaching the interface containing residues R35, K41, K69 and R72 of CARMA1-CARD. The side chains of residues R35, K41, K69 and R72 are shown as sticks. (<b>E</b>) The interactions between CARD domains in the best docking complex model. CARMA1-CARD and BCL10-CARD are colored magenta and gray, respectively. Side chains of E50, E53 and E54 of BCL10 as well as R53, K41, K69 and R72 of CARMA1 are shown as stick.</p