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Relevant bibliographies by topics / Cleavage assay

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Academic literature on the topic 'Cleavage assay'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Cleavage assay"

1

Huitema, Carly, and Lindsay D. Eltis. "A Fluorescent Protein-Based Biological Screen of Proteinase Activity." Journal of Biomolecular Screening 15, no. 2 (2010): 224–29. http://dx.doi.org/10.1177/1087057109357790.

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A cell-based fluorescent protein reporter assay for proteinase activity amenable to high-throughput applications was developed. This assay is based on Förster resonance energy transfer (FRET) between 2 variants of the green fluorescent protein connected by a short cleavable linker and expressed in Escherichia coli as tagged proteins. A library to assay proteinase specificity was generated by randomizing a portion of the linker using PCR. The library could be grown in microplates, allowing cells to be lysed in situ and substrate cleavage to be monitored through loss of FRET signal using a plate

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Han, Yue, and X. Long Zheng. "A Sensitive and Specific Shear-Based Assay for Plasma ADAMTS13 Activity and Inhibitors-the Diagnostic Utility for Thrombotic Microangiopathies." Blood 114, no. 22 (2009): 2114. http://dx.doi.org/10.1182/blood.v114.22.2114.2114.

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Abstract Abstract 2114 Poster Board II-91 Severe deficiency of plasma ADAMTS13 activity causes a potentially fatal thrombotic thrombocytopenic purpura (TTP). To date, functional assays for plasma ADAMTS13 activity and inhibitors rely on cleavage of von Willebrand factor (VWF) in the presence of 1.5 M urea or guanidine-HCl or small peptides derived from the central VWF-A2 domain. To develop a more physiological assay under fluid shear stress, we assessed the proteolytic cleavage of plasma-derived VWF by plasma ADAMTS13 under constant vortexing (2,500 rpm) in a PCR tube mini-mixer that mimics ar

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3

Pope, Mark R., Leonard L. Saari, and Paul W. Ludden. "Fluorometric assay for ADP-ribosylarginine cleavage enzymes." Analytical Biochemistry 160, no. 1 (1987): 68–77. http://dx.doi.org/10.1016/0003-2697(87)90615-4.

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Belliot, Gaël, Stanislav V. Sosnovtsev, Tanaji Mitra, Carl Hammer, Mark Garfield, and Kim Y. Green. "In Vitro Proteolytic Processing of the MD145 Norovirus ORF1 Nonstructural Polyprotein Yields Stable Precursors and Products Similar to Those Detected in Calicivirus-Infected Cells." Journal of Virology 77, no. 20 (2003): 10957–74. http://dx.doi.org/10.1128/jvi.77.20.10957-10974.2003.

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ABSTRACT The MD145-12 strain (GII/4) is a member of the genus Norovirus in the Caliciviridae and was detected in a patient with acute gastroenteritis in a Maryland nursing home. The open reading frame 1 (ORF1) (encoding the nonstructural polyprotein) was cloned as a consensus sequence into various expression vectors, and a proteolytic cleavage map was determined. The virus-encoded cysteine proteinase mediated at least five cleavages (Q330/G331, Q696/G697, E875/G876, E1008/A1009, and E1189/G1190) in the ORF1 polyprotein in the following order: N-terminal protein; nucleoside triphosphatase; 20-k

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Ferracci, Géraldine, Raymond Miquelis, Shunji Kozaki, Michael Seagar, and Christian Lévêque. "Synaptic vesicle chips to assay botulinum neurotoxins." Biochemical Journal 391, no. 3 (2005): 659–66. http://dx.doi.org/10.1042/bj20050855.

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BoNTs (botulinum neurotoxins), considered to be the most toxic of all biological substances, inhibit neurotransmission through proteolytic cleavage of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins [VAMP (vesicle-associated membrane protein, or synaptobrevin), SNAP-25 (25 kDa synaptosome-associated protein) or syntaxin]. Expansion in the use of BoNTs as therapeutic and cosmetic agents, and the potential threat they constitute as biological weapons, underlines the need for rapid and sensitive in vitro assays. Here, we present new automatized bioassays to

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Amberg, Sean M., and Charles M. Rice. "Mutagenesis of the NS2B-NS3-Mediated Cleavage Site in the Flavivirus Capsid Protein Demonstrates a Requirement for Coordinated Processing." Journal of Virology 73, no. 10 (1999): 8083–94. http://dx.doi.org/10.1128/jvi.73.10.8083-8094.1999.

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ABSTRACT Analysis of flavivirus polyprotein processing has revealed the presence of a substrate for the virus-encoded NS2B-NS3 protease at the carboxy-terminal end of the C (capsid or core) protein. Cleavage at this site has been implicated in the efficient generation of the amino terminus of prM via signal peptidase cleavage. Yellow fever virus has four basic residues (Arg-Lys-Arg-Arg) in the P1 through P4 positions of this cleavage site. Multiple alanine substitutions were made for these residues in order to investigate the substrate specificity and biological significance of this cleavage.

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Russell, Anthony G., Holger Ebhardt, and Patrick P. Dennis. "Substrate Requirements for a Novel Archaeal Endonuclease That Cleaves Within the 5′ External Transcribed Spacer of Sulfolobus acidocaldarius Precursor rRNA." Genetics 152, no. 4 (1999): 1373–85. http://dx.doi.org/10.1093/genetics/152.4.1373.

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Abstract During ribosome biogenesis in the hyperthermophilic archaeon Sulfolobus acidocaldarius, at least three separate precursor endonucleolytic cleavages occur within the 144-nucleotide-long 5′ external transcribed spacer (5′ ETS) region of the rRNA operon primary transcript. The 5′ ETS sequence contains three regions of very stable helical structure. One cleavage (5′ to position -98) is in the single-stranded region between the 5′ and the central helical domains; a second cleavage (5′ to position -31) is in the single-stranded region between the central and the 3′ helical domains; and a th

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Damodaran, Suresh, Sajag Adhikari, Marie Turner, and Senthil Subramanian. "Quantitative Amplification of Cleaved Ends (qACE) to assay miRNA-directed target cleavage." F1000Research 3 (July 1, 2015): 240. http://dx.doi.org/10.12688/f1000research.5266.2.

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microRNA (miRNA) regulation is crucial to achieve precise spatio-temporal expression patterns of their target genes. This makes it crucial to determine the levels of cleavage of a particular target mRNA in different tissues and under different conditions. We developed a quantitative PCR method “quantitative Amplification of Cleaved Ends (qACE)” to assay levels of specific cleavage products in order to determine the extent of miRNA-directed target cleavage of a specific target gene. qACE uses cDNA generated from adapter-ligated RNA molecules and relies on a carefully designed fusion primer that

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Nakajima, Yuto, Keiji Nogami, Hiroaki Minami, Kana Sasai, and Midori Shima. "Residues 1680-1684 in the A3 Domain of Factor VIII Contain a Novel Thrombin-Interactive Site Responsible for Proteolytic Cleavage at Arg1689." Blood 134, Supplement_1 (2019): 1107. http://dx.doi.org/10.1182/blood-2019-129313.

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Thrombin-catalyzed activation of factor (F)VIII by proteolytic cleavages at Arg372, Arg740, and Arg1689 is essential for the propagation phase of blood coagulation cascade. Activated FVIII (FVIIIa) forms the tenase complex and markedly amplifies FX activation as a cofactor of FIXa. We previously reported that thrombin interacts with FVIII through the A2 domain (residues 392-394 and 484-509) and C2 domain, and these interactions governed the cleavages at Arg740, Arg372 and Arg1689, respectively (Nogami, JBC 2000, 2005, BJH 2008). A previous report suggested, however, that FVIII lacking the C2 d

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Damodaran, Suresh, Sajag Adhikari, Marie Turner, and Senthil Subramanian. "Quantitative Amplification of Cleaved Ends (qACE) to assay miRNA-directed target cleavage." F1000Research 3 (October 9, 2014): 240. http://dx.doi.org/10.12688/f1000research.5266.1.

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microRNA (miRNA) regulation is crucial to achieve precise spatio-temporal expression patterns of their target genes. This makes it crucial to determine the levels of cleavage of a particular target mRNA in different tissues and under different conditions. We developed a quantitative PCR method “quantitative Amplification of Cleaved Ends (qACE)” to assay levels of specific cleavage products in order to determine the extent of miRNA regulation for a specific target gene. qACE uses cDNA generated from adapter-ligated RNA molecules and relies on a carefully designed fusion primer that spans the ad

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Dissertations / Theses on the topic "Cleavage assay"

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Wu, Wing-kei Ricky. "Development of an in vitro assay for MMP cleavage /." View the Table of Contents & Abstract, 2005. http://sunzi.lib.hku.hk/hkuto/record/B31494183.

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Wu, Wing-kei Ricky, and 胡永基. "Development of an in vitro assay for MMP cleavage." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2005. http://hub.hku.hk/bib/B4501050X.

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Zhao, Hongwei. "A Proteomic Study of Plant Messenger RNA Cleavage and Polyadenylation Specificity Factors and the Establishment of an In Vitro Cleavage Assay System." Oxford, Ohio : Miami University, 2008. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=miami1218547019.

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Dampanaboina, Lavanya. "FUNCTIONAL CHARACTERIZATION OF WD REPEAT PROTEINS, AtCstF50 AND AtFY IN CLEAVAGE AND POLYADENYLATION." UKnowledge, 2011. http://uknowledge.uky.edu/pss_etds/2.

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Polyadenylation is an essential post-transcriptional modification resulting in a mature mRNA in eukaryotes. Three cis-elements the Far Upstream Element (FUE), Near Upstream Element (NUE), and Cleavage Site (CS) - guide the process of cleavage and polyadenylation with the help of multi-subunit protein complexes cleavage and polyadenylation specificity factor (CPSF), cleavage stimulation factor (CstF) along with cleavage factors and poly(A) polymerase. Protein-protein interactions play an important role in the cleavage and polyadenylation process. WD repeat proteins play an important role in pro

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Zheng, Jun. "The Establishment and characterization of a novel plant in vitro cleavage and polyadenylation assay system." Miami University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=miami1281031132.

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Setiawan, Careza [Verfasser], and Moritz [Akademischer Betreuer] Rossner. "NRG1 cleavage assay and small molecule screen for modulators of NRG1 processing / Careza Setiawan ; Betreuer: Moritz Rossner." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2018. http://d-nb.info/1168145848/34.

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Vosyka, Oliver [Verfasser], Steven [Akademischer Betreuer] Verhelst, Aphrodite [Akademischer Betreuer] Kapurniotu, and Stefan [Akademischer Betreuer] Lichtenthaler. "Assay development for monitoring intramembrane (Rhomboid) serine protease substrate cleavage and inhibition / Oliver Vosyka. Gutachter: Aphrodite Kapurniotu ; Stefan Lichtenthaler ; Steven Verhelst. Betreuer: Steven Verhelst." München : Universitätsbibliothek der TU München, 2013. http://d-nb.info/1048176185/34.

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Gupte, Varsha [Verfasser], and Jürgen [Akademischer Betreuer] Wehland. "Development of a high throughput compatible cell assay based on the proteolytic cleavage or inhibition of the human La protein / Varsha Gupte ; Betreuer: Jürgen Wehland." Braunschweig : Technische Universität Braunschweig, 2009. http://d-nb.info/1175829234/34.

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TALASILA, PHANI KUMAR. "NOVEL THYROID HORMONE TARGET GENES IN THE LIVER, AND THEIR ROLES IN THYROID HORMONE SIGNALING AND PHYSIOLOGY." Kent State University / OhioLINK, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=kent1347474067.

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Chang, Chien-Chih, and 張健治. "Establishment of a MALT1-Mediated Proteolytic Cleavage Assay in vitro." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/92103927100306870552.

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碩士<br>國立臺灣大學<br>微生物學研究所<br>98<br>MALT1 (mucosa-associated-lymphoid-tissue lymphoma-translocation gene 1) acts as an adaptor protein with proteolytic activity that controls T/B-cell activation by regulating key molecules in T/B-cell-receptor-induced signaling pathways. It plays a central role in MALT lymphoma by its interaction with BCL10 and enforced activation of NF-κB signaling. Computer assisted amino acid sequence analysis indicated that MALT1 shared sequence similarity with caspases. However, MALT1 was not able to cleave substrates of caspases. It was, therefore, defined as a “paracas

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Book chapters on the topic "Cleavage assay"

1

Stoehr, Julia, and Gunter Meister. "In Vitro RISC Cleavage Assay." In Methods in Molecular Biology. Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-046-1_6.

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Schoonover, Michelle, and Sean M. Kerwin. "A Fluorescence-Based G-Quadruplex DNA Cleavage Assay." In ACS Symposium Series. American Chemical Society, 2011. http://dx.doi.org/10.1021/bk-2011-1082.ch002.

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Miyoshi, Keita, Hiroshi Uejima, Tomoko Nagami-Okada, Haruhiko Siomi, and Mikiko C. Siomi. "In vitro RNA Cleavage Assay for Argonaute-Family Proteins." In Methods in Molecular Biology™. Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-191-8_3.

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Karmakar, Subhasis, Deeptirekha Behera, Mirza Jaynul Baig, and Kutubuddin A. Molla. "In Vitro Cas9 Cleavage Assay to Check Guide RNA Efficiency." In Springer Protocols Handbooks. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1657-4_3.

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Colige, Alain C. "Purification of Native or Recombinant ADAMTS2, and Procollagen I Cleavage Assay." In Methods in Molecular Biology. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9698-8_5.

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Yen, Laising, Brent R. Stockwell, and Richard C. Mulligan. "A Mammalian Cell-Based Assay for Screening Inhibitors of RNA Cleavage." In Methods in Molecular Biology. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-558-9_24.

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Leksa, Vladimir, Herbert B. Schiller, and Hannes Stockinger. "Biotin-Chasing Assay to Evaluate uPAR Stability and Cleavage on the Surface of Cells." In Methods in Molecular Biology. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7595-2_4.

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Stankovic-Valentin, Nicolas, Lukasz Kozaczkiewicz, Katja Curth, and Frauke Melchior. "An In Vitro FRET-Based Assay for the Analysis of SUMO Conjugation and Isopeptidase Cleavage." In Methods in Molecular Biology. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-566-4_16.

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9

Deshpande, Milind S., and Susan P. Manly. "HIV-1 protease substrate based on the p17/p24 cleavage site of gag-pol polyprotein: Synthesis and assay." In Peptides. Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_291.

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Hsu, Erh-Ting, Jeffrey S. Vervacke, Mark D. Distefano, and Christine A. Hrycyna. "A Quantitative FRET Assay for the Upstream Cleavage Activity of the Integral Membrane Proteases Human ZMPSTE24 and Yeast Ste24." In Methods in Molecular Biology. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9532-5_21.

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Conference papers on the topic "Cleavage assay"

1

Petersen, L. C., M. Johannessen, D. Foster, A. Kumar, and E. Mulvihill. "CATALYTIC ACTIVITIES OF ONE-CHAIN tPA AS REVEALED BY AN ANALOGUE RESISTANT TO PLASMIN CLEAVAGE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643845.

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Substitution of Arg275 with Gly in the activation site of tPA provides a one-chain recombinant analogue, tPA-Gly275, which is very resistant to cleavage by plasmin. The amidolytic activity of tPA-Gly275 with simple synthetic substrates was investigated and compared to the kinetics obtained with authentic one- and two-chain tPA. Both one-chain (zymogen) forms possess enzymatic activity, however, in the absence of fibrin it is much lower than that of two-chain tPA. Fibrin enhances the activity of the one-chain tPA forms, but not of two-chain tPA.A chromogenic assay was developed for measurement

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2

Rånby, M., A. Brändstrôm, L. Hansen, K. Henson, and G. Larsen. "REC. t-PA GENETICALLY MODIFIED AT THE CLEAVAGE SITE OF ONE-CHAIN TO TWO-CHAIN CONVERSION: ENZYMOLOGY AND DIAGNOSTIC APPLICATIONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644410.

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Native one-chain t-PA is cleaved by plasmin or by trypsin after the Arg in the sequence -Gln-Phe-Arg-Ile-Lys-. Variants of one-chain t-PA where the -Arg- was replaced by a His (Arg to His) or by a Lys (Arg to Lys) or by a Thr (Arg to Thr) were made through genetic modification. The three mutants and the wild type were expressed in animal cells and purified in the one-chain form by affinity chromatography as was t-PA from Bowes melanoma cells. In contrast to wild type and melanoma t-PA the mutants reacted poorly with polyclonal antibodies raised against the peptide -Gln-Pro-Gln-Phe-Arg-Ile-Lys-

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3

Howard, M. A., M. Coghlan, and B. G. Firkin. "EFFECT OF ELASTASE INDUCED CLEAVAGE OF VON WILLEBRAND FACTOR (vWf) ON ITS STRUCTURE AND FUNCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644091.

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A proteolytic product of vWf termed fast migrating protein (vWf:FMP) has been identified using crossed immunoelectrophoresis (CIE) in normal serum and in the plasma from patients with disseminated intravascular coagulation (DIC). A fragment of vWf antigen (vWf:Ag) migrating to a similar position on CIE as vWf:FMP results from digestion of vWf:Ag with polymorphonuclear cells (PMNC). Since parallels exist between the conditions for generation of vWf:FMP by PMNC and elastase release by these cells the effect of purified elastase from porcine pancrease on vWf was investigated.VWf was purified from

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4

Weitz, J., S. Landman, and S. Birken. "IDENTIFICATION OF A NEUTROPHIL ELASTASE CLEAVAGE SITE ON THE Act -CHAIN OF PRIMATE FIBRINOGEN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643896.

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Human neutrophil elastase (HNE) cleaves the Aα21-22 bond of fibrinogen thus releasing the fibrinopeptide A (FPA)-containing fragment Aαl-21. Plasma Aal-21 levels reflect in vivo HNE activity and peptide levels are increased in cigarette smokers and patients with chronic lung disease. To further explore the HNE-fibrinogen interaction, we set out to develop an animal model. The digestion of purified baboon and marmoset fibrinogen by human thrombin, HNE and extracts of baboon and marmoset neutrophils was monitored with a specific radioimmunoassay for human FPA. Thrcmbin produced quantitative rele

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Exner, T. "CONCENTRATION DEPENDENCE OF ACTIVATION OF ACARBOXYPROTEIN C BY THE CONTORTRIX ACTIVATOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644301.

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The protein C activator in Southern Copperhead (Agkistrodon Contortrix Contortrix) venom was isolated by sequential chromatographies on SP�Sephadex, Con A Sepharose and hydroxylapatite. It was found to be a single chain glycoprotein with an apparent molecular weight of 36,000 and an enzymatic specificity on chromogenic substrates resembling kallikein.This "contortrix activator" was used in a solid-phase immunochromometric assay (ICMA) for functional protein C in which heterologous antibody against protein C was passively coated onto microtitre wells and used to immoblize protein C. This was th

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Piérard, L., P. Jacobs, D. Gheysen, et al. "MUTANT AND CHIMAERIC RECOMBINANT PLASMINOGEN ACTIVATORS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643942.

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In order to produce plasminogen activators (PA) more specific and more active than their natural counterparts, we designed recombinant genes encoding mutant forms of urokinase (u-PA) and chimaeric molecules combining fragments of tissue type plasminogen activator (t-PA) and of u-PA. The following constructs have been realized : 1°) u-PA where amino acids Arg156 and Lys158 have been replaced by Thr. The purpose of this approach was to obtain a prourokinase molecule displaying similar properties as the natural single chain urokinase (scu-PA) but resistant to the cleavage by plasmin ; 2°) u-PA wh

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Schwartz, B. S., and M. C. Monroe. "INCREASED SECRETION OF A FIBRINOLYTIC INHIBITOR BY HUMAN MONONUCLEAR LEUKOCYTES PARALLELS THE PR0COAGULANT RESPONSE TO SPECIFIC ANTIGEN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644384.

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The presence of fibrin is a characteristic finding of Immune mediated tissue lesions. It is known that peripheral blood mononuclear cells (PBM) express tissue factor in response to recognition of a specific protein antigen. We have found PBM secrete a plasminogen activator (PA) Inhibitor (I) in parallel to expression of tissue factor upon exposure to a sensitizing antigen. Increased PA-I can be detected by Inhibition of urokinase (UK) in an 125I-fibrin plate assay, Inhibition of 125I-plasminogen cleavage, and formation of complexes between 125I-urokinase and UK-I. PA-I secretion is dose depend

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Li, Jianwei J., Charles Z. Cao, Ronald Geyer, and Weihong Tan. "Novel molecular beacon assays for DNA cleavage reactions." In BiOS 2001 The International Symposium on Biomedical Optics, edited by Ramesh Raghavachari and Weihong Tan. SPIE, 2001. http://dx.doi.org/10.1117/12.424592.

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Berndt, M. "STRUCTURE AND FUNCTION OF THE GLYCOPROTEIN Ib-IX COMPLEX." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643729.

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At high shear flow, the adhesion of platelets to the exposed vascular subendothelium requires von Willebrand factor (vWF) and is dependent upon a specific platelet membrane adhesion receptor, the human platelet membrane glycoprotein (GP) Ib-IX complex. Recent evidence suggests that vWFbinding to the GP Ib-IX complex plays an important role in other key aspects of hemostasis and thrombosis such as shear-induced platelet aggregation and the interaction of platelets with fibrin.Studies in our laboratory with a seriesof murine monoclonal antibodies directed against epitopes on GP lb, GP IX, or aga

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Eckhardt, Th, S. Haas, B. Lange, and H. Pfeiffer. "MEASUREMENT OF ELASTASE-INDUCED FIBRINOGEN-DERIVED PEPTIDES IN VITRO." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643165.

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Leukocyte elastase (EL) cleaves peptides from the N-terminal fibrinogen (fbg) Aα and B6 chains. The Aα peptide (Aα 1-21) and the as yet unidentified BIB peptide contain thrombin (TB)cleavage sites. As we were interested in fbg proteolysis in sepsis and leukemia, we have tried to measure these peptides (generated by incubating a crude granulocyte extract with fbg) using available fibrinopeptide A (FPA) - und Bß 15-42-antigen-RIA techniques. As the indirect measurement of Aα 1-21 in terms of FPA releasable by TB treatment in vitro (TB-inducible FPA, TIFPA) requires the use of a highly specific a

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