Bud-Sequence conjecture on M fractal image and M–J conjecture between C and Z planes from z←zw+c(w=α+iβ)

Chen, Ning; Zhu, Wancheng

doi:10.1016/s0097-8493(98)00051-x

Cited by 38 publications

(31 citation statements)

References 2 publications

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“…BCR engagement leads to activation of a myriad of intracellular signaling molecules such as members of the protein kinase C (PKC) family of serine-threonine kinases (1). B-lymphocytes express various isoforms of the PKC family including PKC-␣, -␤, -␥, -␦, -⑀, -, -, and -, and BCR engagement has been shown to induce their activation (2)(3)(4).…”

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confidence: 99%

Synergistic B Cell Activation by CD40 and the B Cell Antigen Receptor

Haxhinasto

Bishop

2004

Journal of Biological Chemistry

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Protein kinase (PKD) is a downstream target of second messengers, primarily diacylglycerol, and represents a novel family of serine/threonine kinases. Previous studies show that PKD is activated by multiple signals (for review, see Ref. 5) including BCR engagement in B-lymphocytes (3, 6, 7), and it has been suggested that PKD negatively regulates BCR signaling by phosphorylating Syk and reducing its ability to phosphorylate phospholipase C␥ (3).CD40 engagement has been shown to cooperate with BCR signals particularly in the germinal center reaction, where follicular dendritic cells present antigen and T helper cells provide CD154. Additionally, detailed analysis of the phenotypic differences between naïve, germinal center, and memory cells show that CD40 and other tumor necrosis factor receptor family members are up-regulated in germinal center cells compared with naïve B cells (8). Co-engagement of the two receptors results in a synergistic activation of B cells (9, 10). Previous studies from our laboratory identified TRAF2 and TRAF3 in the CD40 signaling pathway and BCR-induced PKD activation as playing important roles in the cross-talk between these receptors (10, 11). To integrate the BCR and CD40 signaling pathways, potential ways in which PKD and TRAF molecules cooperate was examined. Because BCR signaling activates a number of kinases, we hypothesized that BCR-mediated TRAF phosphorylation might be important for the synergy. Site-directed mutagenesis of TRAF2 identified the potentially phosphorylatable tyrosine 484 as a critical residue for the synergy and led us to investigate the potential involvement of Bruton's tyrosine kinase (Btk), a tyrosine kinase, in this process. Our data showed a role for Btk in the synergy, and this was PKDand TRAF2-dependent. This work together with previous findings provides a model for BCR-CD40 synergy whereby BCRmediated activation of Btk and PKD modifies TRAF2 in a manner that allows it to block an inhibitory effect mediated by TRAF3. EXPERIMENTAL PROCEDURESCells and Mice-The mouse B cell line CH12.LX expresses surface IgM specific for phosphatidylcholine, an antigen found on the surface of sheep erythrocytes (sheep red blood cells) (12) and has been well characterized (13). The CH12.LacR subclone used for the inducible expression of stably transfected molecules has been previously described (14). Subclones of CH12.LX lacking TRAF2 were produced by homologous

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confidence: 99%

Synergistic B Cell Activation by CD40 and the B Cell Antigen Receptor

Haxhinasto

Bishop

2004

Journal of Biological Chemistry

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“…The ligation of activation receptors such as surface Igs and the direct activation of PKC generate a cascade of phosphorylation events in B cells (37)(38)(39)(40) which influences protein-protein interactions in the cytoplasm, activates gene transcription and modifies the cell morphology. Our goal was to investigate whether B cell activation influences the MHC class II presentation pathway.…”

Section: Discussionmentioning

confidence: 99%

“…Ligation of the BCR transduces activation signals, through the Ig␣ and Ig␤ coreceptors, leading to a cascade of protein tyrosine kinase activation (reviewed in Refs. 37 and 38) and to the production of second messengers, such as inositol triphosphate, and PKC activators, such as diacylglycerol (39). Several routes dependent on protein tyrosine kinase and PKC are then converging at the level of the activation of the mitogen-activated protein kinase pathway (40).…”

Section: Mhcmentioning

confidence: 99%

Selective Modulation of the Major Histocompatibility Complex Class II Antigen Presentation Pathway following B Cell Receptor Ligation and Protein Kinase C Activation

Barois¹,

Forquet

Davoust

1997

Journal of Biological Chemistry

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We noticed that B cell receptor ligation or phorbol 12-myristate 13-acetate treatment induced intracellular vesicles containing major histocompatibility complex (MHC) class II and invariant chain (Ii), and increased the amount of transmembrane p12 Ii fragments coimmunoprecipitated with class II molecules. To determine the influence of protein kinase C activation on the MHC class II presentation pathway, we analyzed the subcellular distribution of Ii, the induction of SDS-stable forms of class II molecules, and their ability to present different antigens. Ii chains visualized with luminal and cytoplasmic directed antibodies appeared in early endosomal compartments accessible to transferrin in response to phorbol 12-myristate 13-acetate treatment, whereas transmembrane Ii degradation products equivalent to the p12 Ii fragments were colocalized with the B cell receptors internalized after cross-linking. Protein kinase C activation delayed in parallel the formation of SDS-stable forms of class II molecules and reduced the presentation of antigenic determinants requiring newly synthesized class II ␣␤-Ii complexes. These data indicate that B cell activation affects Ii processing and MHC class II peptide loading in endosomal compartments intersecting the biosynthetic pathway. MHC1 class II molecules bind in their groove antigenic peptides generally derived from endocytosed proteins for their presentation to specific CD4 ϩ T lymphocytes (reviewed in Refs. 1-3). Shortly after their biosynthesis, the MHC class II ␣ and ␤ chains assemble with Ii through a sequence from amino acid 81 to 104 of Ii called CLIP for class II associated Ii peptide (4 -6), and form (␣␤) 3 Ii 3 nonameric structures (7,8). Ii prevents the association of antigenic peptides with class II ␣␤ heterodimers (9 -11) through CLIP peptide (5), which occupies the peptidebinding groove in crystallized MHC class II molecules (12). The trimerization of Ii cytoplasmic domains, containing two dileucine motives each, drives the targeting of newly synthesized class II molecules to specialized endosomal compartments (13-15), which were further characterized as compartments of antigen processing and of peptide loading (16 -19). The amount of class II molecules located in these intracellular compartments can differ to a considerable extent, depending on the cell type (20 -23), and proteolytic cleavage of Ii occurs at this stage as indicated by ultrastructural observations (22). Upon removal of CLIP from class II molecules catalyzed by HLA-DM or its murine equivalent H2-M class II molecules (24 -26), peptide-loaded MHC class II complexes are exported to the cell surface by a poorly defined pathway. Recycling of class II molecules, from the plasma membrane through endosomes, has also been observed in B cells (27-29), allowing binding and presentation of different antigens to T cells (27,30). MHC class II molecules can therefore gain access to the antigen-processing compartments by at least two different routes, a direct targeting of newly synthesized ␣␤-Ii complexes and...

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“…Huang presented a method to compute periodic orbits of k-M set for positive integer k by constructing polynomial equations [11]. Then, Chen and Shirriff researched basic structure of k-M set for complex exponent k [7,25]. Meantime, Gujar and Dhurandhar explored basic structure of k-M set for real exponent k [8,10].…”

Section: Introductionmentioning

confidence: 99%

Fractal generation method based on asymptote family of generalized Mandelbrot set and its application

Liu¹,

Zheng²,

Fu³

et al. 2017

J. Nonlinear Sci. Appl.

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Generalized Mandelbrot set (k-M set) is the basis of fractal analysis. This paper presents a novel method to generate k-M set, which generates k-M set precisely by constructing its asymptote family. Correctness of the proposed method is proved as well as computational complexity is researched. Further, application of the generation method is studied, which is used to analyze distribution of boundary points and periodic points of k-M set. Finally, experiments have been implemented to evaluate the theoretical results.

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Bud-Sequence conjecture on M fractal image and M–J conjecture between C and Z planes from z←zw+c(w=α+iβ)

Cited by 38 publications

References 2 publications

Synergistic B Cell Activation by CD40 and the B Cell Antigen Receptor

Synergistic B Cell Activation by CD40 and the B Cell Antigen Receptor

Selective Modulation of the Major Histocompatibility Complex Class II Antigen Presentation Pathway following B Cell Receptor Ligation and Protein Kinase C Activation

Fractal generation method based on asymptote family of generalized Mandelbrot set and its application

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