Determination of the Length of Target Recognition Sequence in sgRNA Required for CRISPR Interference

In some practical application of target recognition with sensors, the sensors will give the recognition sequence of targets, which is more detailed than the single recognition result. How to properly construct the basic probability assignment by the recognition sequence becomes the key to successful application of evidence theory. For the recognition sequence of the target recognition results of general sensor is incomplete, and the importance of the types in the recognition sequence is in descending order, this paper proposes a method to construct weights of recognition sequence, the basic probability assignments constructed by the weights are closer to the real recognition results. Simulation results show that this method is more reasonable and effective than the method of contrast.

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Adaptive determination of eigenvalues and eigenvectors from perturbed autocorrelation matrices for automatic target recognition

10.1117/12.665750 ◽

2006 ◽

Cited By ~ 1

Author(s):

P. Ragothaman ◽

W. B. Mikhael ◽

R. Muise ◽

A. Mahalanobis ◽

T. Yang

Keyword(s):

Target Recognition ◽

Automatic Target Recognition ◽

Eigenvalues And Eigenvectors

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An improved method to determine basic probability assignment based on fuzzy mathematics

MATEC Web of Conferences ◽

10.1051/matecconf/202235502002 ◽

2022 ◽

Vol 355 ◽

pp. 02002

Author(s):

Leihui Xiong ◽

Xiaoyan Su

Keyword(s):

Target Recognition ◽

Evidence Theory ◽

Intersection Point ◽

Fuzzy Mathematics ◽

Improved Method ◽

Probability Assignment ◽

Basic Probability Assignment ◽

Robot Hands ◽

Basic Probability

In D-S evidence theory, the determination of the basic probability assignment function (BPA) is the first and important step. However, the generation of BPA is still a problem to be solved. Based on the concepts in fuzzy mathematics, this paper proposes an improved BPA generation method. By introducing the value of the intersection point of membership function of different targets under the same index to describe the overlap degree of targets, the assignment of unknown items is optimized on this basis. This article applies it to target recognition of robot hands. The results show that the proposed method is more reliable and more accurate.

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Determination of the structure of two novel echistatin variants and comparison of the ability of echistatin variants to inhibit aggregation of platelets from different species

Biochemical Journal ◽

10.1042/bj3050513 ◽

1995 ◽

Vol 305 (2) ◽

pp. 513-520 ◽

Cited By ~ 14

Author(s):

Y L Chen ◽

T F Huang ◽

S W Chen ◽

I H Tsai

Keyword(s):

Platelet Glycoprotein ◽

Medium Size ◽

Recognition Sequence ◽

High Affinity ◽

Cnbr Cleavage ◽

Echis Carinatus ◽

Fluorescent Spectra ◽

Methionine Residues ◽

Aggregation Of Platelets

Two new variants of short disintegrins were purified from the venom of Echis carinatus leakeyi and named echistatin beta and gamma. These proteins were found to be about 85% similar in amino acid sequence to echistatin alpha which has been well studied. The disulphide pattern of echistatin gamma appeared to be identical with that of echistatin alpha. They all contain the adhesive recognition sequence Arg-Gly-Asp (RGD) but inhibit the aggregation of platelets from human and other mammals with different potencies. Echistatin beta and alpha are far more effective on platelets from humans and guinea pigs than those from rabbits and rats whereas echistatin gamma is less discriminating of the platelets of the species tested. This species-dependent platelet sensitivity to echistatin beta and gamma could be attributed to the variations in residues 15, 21, 22 and 27, which are close to or within the RGD loop, rather than to the C-terminal variations after residue 46. Taking advantage of the presence of methionine residues flanking both sides of the ARGDDM motif in echistatin gamma, we deleted this hexapeptide by CNBr cleavage to produce des-(23-28)-echistatin gamma. The modified protein showed c.d. and fluorescent spectra grossly similar to the intact echistatin but its antiplatelet potency decreased more than 200-fold. We thus propose that a favourable conformation of the RGD region is responsible mainly for the high-affinity binding of echistatin to the platelet glycoprotein IIb-IIIa as shown previously for the binding of medium-size disintegrin.

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Numerically Efficient Determination of the Optimal Threshold in Natural Frequency-Based Radar Target Recognition

IEEE Transactions on Antennas and Propagation ◽

10.1109/tap.2014.2354416 ◽

2014 ◽

Vol 62 (11) ◽

pp. 5889-5894 ◽

Cited By ~ 1

Author(s):

Joon-Ho Lee ◽

Hyun-Jin Moon ◽

So-Hee Jeong

Keyword(s):

Natural Frequency ◽

Target Recognition ◽

Optimal Threshold ◽

Radar Target ◽

Radar Target Recognition

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Bone-Specific Expression of the Alpha Chain of the Nascent Polypeptide-Associated Complex, a Coactivator Potentiating c-Jun-Mediated Transcription

Molecular and Cellular Biology ◽

10.1128/mcb.18.3.1312 ◽

1998 ◽

Vol 18 (3) ◽

pp. 1312-1321 ◽

Cited By ~ 54

Author(s):

Alain Moreau ◽

Wagner V. Yotov ◽

Francis H. Glorieux ◽

René St-Arnaud

Keyword(s):

Leucine Zipper ◽

Transcriptional Coactivator ◽

Recognition Sequence ◽

Developmentally Regulated ◽

Specific Expression ◽

Nascent Polypeptide ◽

Alpha Chain ◽

Two Hybrid

ABSTRACT The alpha chain of the nascent polypeptide-associated complex (α-NAC) coactivator was shown to potentiate the activity of the homodimeric c-Jun activator, while transcription mediated by the c-Fos/c-Jun heterodimer was unaffected. The use of deletion mutants in pull-down assays revealed that α-NAC interacted with amino acids 1 to 89 of the c-Jun protein and that the coactivator could interact with both the unphosphorylated and the serine 73-phosphorylated form of c-Jun. N-terminal-deleted c-Jun protein failed to interact with α-NAC in mammalian two-hybrid assays, while mutant c-Jun proteins lacking the leucine zipper or the basic domain retained interaction with α-NAC in vivo. Kinetics studies with purified c-Jun homodimer and recombinant α-NAC proteins allowed determination of the mechanism of coactivation by α-NAC: the coactivator stabilized the AP-1 complex formed by the c-Jun homodimer on its DNA recognition sequence through an eightfold reduction in the dissociation constant (kd ) of the complex. This effect of α-NAC was specific, because α-NAC could not stabilize the interactions of JunB or Sp1 with their cognate binding sites. Interestingly, the expression of α-NAC was first detected at 14.5 to 15 days postconception, concomitantly with the onset of ossification during embryogenesis. The α-NAC protein was specifically expressed in differentiated osteoblasts at the centers of ossification. Thus, the α-NAC gene product exhibits the properties of a developmentally regulated, bone-specific transcriptional coactivator.

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Determination of the recognition sequence of the type II restriction endonuclease,LlaCI, fromLactococcus lactisW15

FEMS Microbiology Letters ◽

10.1111/j.1574-6968.1998.tb13021.x ◽

1998 ◽

Vol 163 (1) ◽

pp. 25-29 ◽

Cited By ~ 4

Author(s):

Jytte Josephsen ◽

Bettina JÃ¸rgen-Jensen ◽

Niels R Nyengaard

Keyword(s):

Restriction Endonuclease ◽

Type Ii ◽

Recognition Sequence

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Determination of the recognition sequence of Mycobacterium smegmatis topoisomerase I on mycobacterial genomic sequences

Nucleic Acids Research ◽

10.1093/nar/28.8.1830 ◽

2000 ◽

Vol 28 (8) ◽

pp. 1830-1837 ◽

Cited By ~ 21

Author(s):

D. Sikder

Keyword(s):

Mycobacterium Smegmatis ◽

Topoisomerase I ◽

Genomic Sequences ◽

Recognition Sequence

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Naturally Occurring Arg−1 to His Mutation in Human Protein C Leads to Aberrant Propeptide Processing and Secretion of Dysfunctional Protein C

Blood ◽

10.1182/blood.v89.8.2807 ◽

1997 ◽

Vol 89 (8) ◽

pp. 2807-2816 ◽

Cited By ~ 12

Author(s):

Bent Lind ◽

Anders H. Johnsen ◽

Sixtus Thorsen

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Light Chain ◽

Protein C ◽

High Performance ◽

Basic Amino Acid ◽

Recognition Sequence ◽

Recognition Element ◽

Gla Domain

Abstract The dysfunctional protein C from a thrombophilic patient heterozygote for a G1388 to A converting the codon for Arg−1 to His was purified from plasma and characterized. N-terminal amino acid sequence analysis of the light chain of the protein C demonstrated that the dysfunctional protein C is elongated with one amino acid, namely the mutated His. This finding is compatible with disruption by the mutated His of the original basic propeptidase recognition sequence (Arg−5-Ile-Arg-Lys-Arg−1), resulting in a shift of the cleavage site to a new position, Lys−2-His−1, which follows an alternative basic amino acid propeptidase recognition sequence (Arg−5-Ile-Arg-Lys−2). Because the mutation affects the propeptide that directs the γ-carboxylation converting Glu to Gla residues in the Gla domain, it was investigated whether the mutation impaired this reaction. Gla fragment obtained by cleavage of the dysfunctional protein C light chain with endoproteinase Asp-N was isolated by reverse-phase high-performance liquid chromatography, methylated, and subjected to N-terminal sequence analysis. The methylation step enabled the positive identification of Gla residues as well as the determination of the relative amount of Gla and Glu residues at each of the nine γ-carboxylation sites of the Gla domain. The analysis showed that all nine potential γ-carboxylation sites of the dysfunctional protein C were normally carboxylated. This result is compatible with the notion that position −1 is not a part of the recognition element for the γ-carboxylase. In conclusion, evidence is provided showing that the mutation leads to aberrant propeptide processing and secretion of dysfunctional normally carboxylated protein C extended with the mutated His.

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