103,048 research outputs found
Set Membership with Non-Adaptive Bit Probes
No full textWe consider the non-adaptive bit-probe complexity of the set membership problem, where a set S of size at most n from a universe of size m is to be represented as a short bit vector in order to answer membership queries of the form "Is x in S?" by non-adaptively probing the bit vector at t places. Let s_N(m,n,t) be the minimum number of bits of storage needed for such a scheme. In this work, we show existence of non-adaptive and adaptive schemes for a range of t that improves an upper bound of Buhrman, Miltersen, Radhakrishnan and Srinivasan (2002) on s_N(m,n,t). For three non-adaptive probes, we improve the previous best lower bound on s_N(m,n,3) by Alon and Feige (2009)
Improved Explicit Data Structures in the Bit-Probe Model Using Error-Correcting Codes
No full textWe consider the bit-probe complexity of the set membership problem: represent an n-element subset S of an m-element universe as a succinct bit vector so that membership queries of the form "Is x ∈ S" can be answered using at most t probes into the bit vector. Let s(m,n,t) (resp. s_N(m,n,t)) denote the minimum number of bits of storage needed when the probes are adaptive (resp. non-adaptive). Lewenstein, Munro, Nicholson, and Raman (ESA 2014) obtain fully-explicit schemes that show that
s(m,n,t) = ((2^t-1)m^{1/(t - min{2⌊log n⌋, n-3/2})}) for n ≥ 2,t ≥ ⌊log n⌋+1 .
In this work, we improve this bound when the probes are allowed to be superlinear in n, i.e., when t ≥ Ω(nlog n), n ≥ 2, we design fully-explicit schemes that show that
s(m,n,t) = ((2^t-1)m^{1/(t-{n-1}/{2^{t/(2(n-1))}})}),
asymptotically (in the exponent of m) close to the non-explicit upper bound on s(m,n,t) derived by Radhakrishan, Shah, and Shannigrahi (ESA 2010), for constant n.
In the non-adaptive setting, it was shown by Garg and Radhakrishnan (STACS 2017) that for a large constant n₀, for n ≥ n₀, s_N(m,n,3) ≥ √{mn}. We improve this result by showing that the same lower bound holds even for storing sets of size 2, i.e., s_N(m,2,3) ≥ Ω(√m)
Letter, [Author unclear] to Paulina T. Merritt
No full textHandwritten letter to Paulina Merritt from an unknown author, October 1, 1876.
Exploration of New Solitons for the Fractional Perturbed Radhakrishnan–Kundu–Lakshmanan Model
No full textThe key objective of the current manuscript was to investigate the exact solutions of the fractional perturbed Radhakrishnan–Kundu–Lakshmanan model. For this purpose, we applied two reliable and efficient approaches; specifically, the modified simple equation (MSE) and exponential rational function (ERF) techniques. The methods considered in this paper offer solutions for problems in nonlinear theory and mathematical physics practice. We also present solutions obtained graphically with the Maple package program
ERp44 mediates a thiol-independent retention of formylglycine-generating enzyme in the endoplasmic reticulum
No full textMariappan M, Radhakrishnan K, Dierks T, Schmidt B, von Figura K. ERp44 mediates a thiol-independent retention of formylglycine-generating enzyme in the endoplasmic reticulum. JOURNAL OF BIOLOGICAL CHEMISTRY. 2008;283(10):6375-6383.Inside the endoplasmic reticulum (ER) formylglycine-generating enzyme (FGE) catalyzes in newly synthesized sulfatases the post-translational oxidation of a specific cysteine. Thereby formylglycine is generated, which is essential for sulfatase activity. Here we show that ERp44 interacts with FGE forming heterodimeric and, to a lesser extent, also heterotetrameric and octameric complexes, which are stabilized through disulfide bonding between cysteine 29 of ERp44 and cysteines 50 and 52 in the N-terminal region of FGE. ERp44 mediates FGE retrieval to the ER via its C-terminal RDEL signal. Increasing ERp44 levels by overexpression enhances and decreasing ERp44 levels by silencing reduces ER retention of FGE. Suppressing disulfide bonding by mutating the critical cysteines neither abrogates ERp44.FGE complex formation nor interferes with ERp44-mediated retention of FGE, indicating that noncovalent interactions between ERp44 and FGE are sufficient to mediate ER retention. The N-terminal region of FGE harboring Cys(50) and Cys(52) is dispensible for catalytic activity in vitro but required for FGE-mediated activation of sulfatases in vivo. This in vivo activity is affected neither by overexpression nor by silencing of ERp44, indicating that a further ER component interacting with the N-terminal extension of FGE is critical for sulfatase activation
Rapid degradation of an active formylglycine generating enzyme variant leads to a late infantile severe form of multiple sulfatase deficiency
No full textSchlotawa L, Radhakrishnan K, Baumgartner M, et al. Rapid degradation of an active formylglycine generating enzyme variant leads to a late infantile severe form of multiple sulfatase deficiency. European Journal Of Human Genetics. 2013;21(9):1020-1023.Multiple sulfatase deficiency (MSD) is a rare inborn error of metabolism affecting posttranslational activation of sulfatases by the formylglycine generating enzyme (FGE). Due to mutations in the encoding SUMF1 gene, FGE's catalytic capacity is impaired resulting in reduced cellular sulfatase activities. Both, FGE protein stability and residual activity determine disease severity and have previously been correlated with the clinical MSD phenotype. Here, we report a patient with a late infantile severe course of disease. The patient is compound heterozygous for two so far undescribed SUMF1 mutations, c.156delC (p.C52fsX57) and c.390A>T (p.E130D). In patient fibroblasts, mRNA of the frameshift allele is undetectable. In contrast, the allele encoding FGE-E130D is expressed. FGE-E130D correctly localizes to the endoplasmic reticulum and has a very high residual molecular activity in vitro (55% of wildtype FGE); however, it is rapidly degraded. Thus, despite substantial residual enzyme activity, protein instability determines disease severity, which highlights that potential MSD treatment approaches should target protein folding and stabilization mechanisms
Damage detection in non-metallic materials using nonlinear acoustics with piezo-based excitation
No full textHandwritten biographical information on Paulina T. McClung Merritt
No full textA handwritten biography of Paulina T. McClung Merritt by an unknown author, 1892.
Heterogeneous and tissue-specific regulation of effector T cell responses by IFN-gamma during Plasmodium berghei ANKA infection.
No full textIFN-γ and T cells are both required for the development of experimental cerebral malaria during Plasmodium berghei ANKA infection. Surprisingly, however, the role of IFN-γ in shaping the effector CD4(+) and CD8(+) T cell response during this infection has not been examined in detail. To address this, we have compared the effector T cell responses in wild-type and IFN-γ(-/-) mice during P. berghei ANKA infection. The expansion of splenic CD4(+) and CD8(+) T cells during P. berghei ANKA infection was unaffected by the absence of IFN-γ, but the contraction phase of the T cell response was significantly attenuated. Splenic T cell activation and effector function were essentially normal in IFN-γ(-/-) mice; however, the migration to, and accumulation of, effector CD4(+) and CD8(+) T cells in the lung, liver, and brain was altered in IFN-γ(-/-) mice. Interestingly, activation and accumulation of T cells in various nonlymphoid organs was differently affected by lack of IFN-γ, suggesting that IFN-γ influences T cell effector function to varying levels in different anatomical locations. Importantly, control of splenic T cell numbers during P. berghei ANKA infection depended on active IFN-γ-dependent environmental signals--leading to T cell apoptosis--rather than upon intrinsic alterations in T cell programming. To our knowledge, this is the first study to fully investigate the role of IFN-γ in modulating T cell function during P. berghei ANKA infection and reveals that IFN-γ is required for efficient contraction of the pool of activated T cells
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