Journal articles on the topic 'Signal recycling'

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1

Raab, Frederick J. "Recycling for a cleaner signal." Nature 351, no. 6322 (May 1991): 98–99. http://dx.doi.org/10.1038/351098a0.

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2

Freeman, Brian C., and Keith R. Yamamoto. "Continuous recycling: a mechanism for modulatory signal transduction." Trends in Biochemical Sciences 26, no. 5 (May 2001): 285–90. http://dx.doi.org/10.1016/s0968-0004(01)01834-5.

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3

Thüring, André, R. Schnabel, H. Lück, and K. Danzmann. "Detuned Twin-Signal-Recycling for ultrahigh-precision interferometers." Optics Letters 32, no. 8 (March 19, 2007): 985. http://dx.doi.org/10.1364/ol.32.000985.

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4

Toh, Wei Hong, Pei Zhi Cheryl Chia, Mohammed Iqbal Hossain, and Paul A. Gleeson. "GGA1 regulates signal-dependent sorting of BACE1 to recycling endosomes, which moderates Aβ production." Molecular Biology of the Cell 29, no. 2 (January 15, 2018): 191–208. http://dx.doi.org/10.1091/mbc.e17-05-0270.

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The diversion of the β-secretase BACE1 from the endo-lysosomal pathway to recycling endosomes is important in the regulation of amyloid beta production. Here we define BACE1 transport from early to recycling endosomes and identify essential roles for the SNX4-mediated, signal-independent pathway and for a signal-mediated, GGA1-dependent pathway.
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Krsmanović, Tamara, Agnes Pawelec, Tobias Sydor, and Ralf Kölling. "Control of Ste6 Recycling by Ubiquitination in the Early Endocytic Pathway in Yeast." Molecular Biology of the Cell 16, no. 6 (June 2005): 2809–21. http://dx.doi.org/10.1091/mbc.e04-10-0941.

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We present evidence that ubiquitination controls sorting of the ABC-transporter Ste6 in the early endocytic pathway. The intracellular distribution of Ste6 variants with reduced ubiquitination was examined. In contrast to wild-type Ste6, which was mainly localized to internal structures, these variants accumulated at the cell surface in a polar manner. When endocytic recycling was blocked by Ypt6 inactivation, the ubiquitination deficient variants were trapped inside the cell. This indicates that the polar distribution is maintained dynamically through endocytic recycling and localized exocytosis (“kinetic polarization”). Ste6 does not appear to recycle through late endosomes, because recycling was not blocked in class E vps (vacuolar protein sorting) mutants (Δvps4, Δvps27), which are affected in late endosome function and in the retromer mutant Δvps35. Instead, recycling was partially affected in the sorting nexin mutant Δsnx4, which serves as an indication that Ste6 recycles through early endosomes. Enhanced recycling of wild-type Ste6 was observed in class D vps mutants (Δpep12, Δvps8, and Δvps21). The identification of putative recycling signals in Ste6 suggests that recycling is a signal-mediated process. Endocytic recycling and localized exocytosis could be important for Ste6 polarization during the mating process.
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Zhang, Xiao-long, Zhe-han Yang, Yuan-yuan Chang, Di Liu, Yun-rui Li, Ya-qin Chai, Ying Zhuo, and Ruo Yuan. "Programmable mismatch-fueled high-efficiency DNA signal converter." Chemical Science 11, no. 1 (2020): 148–53. http://dx.doi.org/10.1039/c9sc05084a.

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7

Zaliauskiene, Lolita, Sunghyun Kang, Christie G. Brouillette, Jacob Lebowitz, Ramin B. Arani, and James F. Collawn. "Down-Regulation of Cell Surface Receptors Is Modulated by Polar Residues within the Transmembrane Domain." Molecular Biology of the Cell 11, no. 8 (August 2000): 2643–55. http://dx.doi.org/10.1091/mbc.11.8.2643.

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How recycling receptors are segregated from down-regulated receptors in the endosome is unknown. In previous studies, we demonstrated that substitutions in the transferrin receptor (TR) transmembrane domain (TM) convert the protein from an efficiently recycling receptor to one that is rapidly down regulated. In this study, we demonstrate that the “signal” within the TM necessary and sufficient for down-regulation is Thr11Gln17Thr19 (numbering in TM). Transplantation of these polar residues into the wild-type TR promotes receptor down-regulation that can be demonstrated by changes in protein half-life and in receptor recycling. Surprisingly, this modification dramatically increases the TR internalization rate as well (∼79% increase). Sucrose gradient centrifugation and cross-linking studies reveal that propensity of the receptors to self-associate correlates with down-regulation. Interestingly, a number of cell surface proteins that contain TM polar residues are known to be efficiently down-regulated, whereas recycling receptors for low-density lipoprotein and transferrin conspicuously lack these residues. Our data, therefore, suggest a simple model in which specific residues within the TM sequences dramatically influence the fate of membrane proteins after endocytosis, providing an alternative signal for down-regulation of receptor complexes to the well-characterized cytoplasmic tail targeting signals.
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8

Suzuki, Sho W., Ya-Shan Chuang, Ming Li, Matthew N. J. Seaman, and Scott D. Emr. "A bipartite sorting signal ensures specificity of retromer complex in membrane protein recycling." Journal of Cell Biology 218, no. 9 (July 23, 2019): 2876–86. http://dx.doi.org/10.1083/jcb.201901019.

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Retromer is an evolutionarily conserved protein complex, which sorts functionally diverse membrane proteins into recycling tubules/vesicles from the endosome. Many of the identified cargos possess a recycling signal sequence defined as ØX[L/M/V], where Ø is F/Y/W. However, this sequence is present in almost all proteins encoded in the genome. Also, several identified recycling sequences do not follow this rule. How then does retromer precisely select its cargos? Here, we reveal that an additional motif is also required for cargo retrieval. The two distinct motifs form a bipartite recycling signal recognized by the retromer subunits, Vps26 and Vps35. Strikingly, Vps26 utilizes different binding sites depending on the cargo, allowing retromer to recycle different membrane proteins. Thus, retromer interacts with cargos in a more complex manner than previously thought, which facilitates precise cargo recognition.
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9

Robertson, Sarah E., Subba Rao Gangi Setty, Anand Sitaram, Michael S. Marks, Robert E. Lewis, and Margaret M. Chou. "Extracellular Signal-regulated Kinase Regulates Clathrin-independent Endosomal Trafficking." Molecular Biology of the Cell 17, no. 2 (February 2006): 645–57. http://dx.doi.org/10.1091/mbc.e05-07-0662.

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Extracellular signal-regulated kinase (Erk) is widely recognized for its central role in cell proliferation and motility. Although previous work has shown that Erk is localized at endosomal compartments, no role for Erk in regulating endosomal trafficking has been demonstrated. Here, we report that Erk signaling regulates trafficking through the clathrin-independent, ADP-ribosylation factor 6 (Arf6) GTPase-regulated endosomal pathway. Inactivation of Erk induced by a variety of methods leads to a dramatic expansion of the Arf6 endosomal recycling compartment, and intracellular accumulation of cargo, such as class I major histocompatibility complex, within the expanded endosome. Treatment of cells with the mitogen-activated protein kinase kinase (MEK) inhibitor U0126 reduces surface expression of MHCI without affecting its rate of endocytosis, suggesting that inactivation of Erk perturbs recycling. Furthermore, under conditions where Erk activity is inhibited, a large cohort of Erk, MEK, and the Erk scaffold kinase suppressor of Ras 1 accumulates at the Arf6 recycling compartment. The requirement for Erk was highly specific for this endocytic pathway, because its inhibition had no effect on trafficking of cargo of the classical clathrin-dependent pathway. These studies reveal a previously unappreciated link of Erk signaling to organelle dynamics and endosomal trafficking.
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10

Wang, Bin, Zheng You, and Dahai Ren. "Target-assisted FRET signal amplification for ultrasensitive detection of microRNA." Analyst 144, no. 7 (2019): 2304–11. http://dx.doi.org/10.1039/c8an02266f.

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11

Gräf, Christian, André Thüring, Henning Vahlbruch, Karsten Danzmann, and Roman Schnabel. "Length sensing and control of a Michelson interferometer with power recycling and twin signal recycling cavities." Optics Express 21, no. 5 (February 25, 2013): 5287. http://dx.doi.org/10.1364/oe.21.005287.

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12

Itin, C., R. Schindler, and H. P. Hauri. "Targeting of protein ERGIC-53 to the ER/ERGIC/cis-Golgi recycling pathway." Journal of Cell Biology 131, no. 1 (October 1, 1995): 57–67. http://dx.doi.org/10.1083/jcb.131.1.57.

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ERGIC-53 is a lectin-type membrane protein that continuously recycles between the ER, ER-Golgi intermediate compartment (ERGIC) and the cis-Golgi. To identify the targeting signals that mediate this recycling, N-glycosylated and myc-tagged variants of ERGIC-53 were constructed. By monitoring endoglycosidase H resistance, we measured the loss from the ER-ERGIC-cis-Golgi cycle of ERGIC-53. A domain exchange approach with the plasma membrane reporter protein CD4 showed that the transmembrane and the lumenal domains are not sufficient, while the cytoplasmic domain of ERGIC-53 is required and sufficient for pre-medial-Golgi localization. However, the ERGIC-53 cytoplasmic domain on CD4 lead to increased ER-staining by immunofluorescence microscopy indicating that this domain alone cannot provide for unbiased recycling through the ER-ERGIC-cis-Golgi compartments. Complete progress through the ER-ERGIC-cis-Golgi recycling pathway requires the cytoplasmic domain acting together with the lumenal domain of ERGIC-53. Dissection of the cytoplasmic domain revealed a COOH-terminal di-lysine ER-retrieval signal, KKFF, and an RSQQE targeting determinant adjacent to the transmembrane domain. Surprisingly, the two COOH-terminal phenylalanines influence the targeting. They reduce the ER-retrieval capacity of the di-lysine signal and modulate the RSQQE determinant.
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13

Wang, Hai-Bo, Li-Juan Ou, Ke-Jing Huang, Xin-Ge Wen, Ling-Ling Wang, and Yan-Ming Liu. "A sensitive biosensing strategy for DNA detection based on graphene oxide and T7 exonuclease assisted target recycling amplification." Canadian Journal of Chemistry 91, no. 12 (December 2013): 1266–71. http://dx.doi.org/10.1139/cjc-2013-0285.

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A fluorescence biosensing strategy based on graphene oxide (GO) was reported for simple, rapid, sensitive, and selective DNA detection by T7 exonuclease assisted target recycling amplification. Due to the super fluorescence quenching efficiency of GO, the fluorescein amiditelabeled signal probe was firstly adsorbed onto the surface of GO and the fluorescence was quenched. Owing to its excellent selectivity for double-stranded DNA, T7 exonuclease was chosen as a signal-amplifying biocatalyst to improve the detection sensitivity. In the presence of target DNA, the signal probe could bind with target DNA and form a DNA duplex structure to trigger the digestion of the signal probe by T7 exonuclease, leading to the recycling of target DNA and the increasing of fluorescence intensity. Upon the recycling use of target DNA, this method achieved a high sensitivity towards target DNA with a detection limit of 0.3 pmol/L, which was lower than previously reported for GO-based DNA biosensors. Moreover, it does not require complex modifications of the molecular beacon and time-consuming thermal cycling procedures. Thus, the simple strategy provides a universal biosensing platform for DNA detection and it could find wide applications in DNA damage analysis and diagnostics.
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14

Tao, Duo, and Nelson Christensen. "Optimizing signal recycling for detecting a stochastic gravitational-wave background." Classical and Quantum Gravity 35, no. 12 (May 17, 2018): 125002. http://dx.doi.org/10.1088/1361-6382/aac148.

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15

Gray, Malcolm B., Andrew J. Stevenson, Hans-Albert Bachor, and David E. McClelland. "Broadband and tuned signal recycling with a simple Michelson interferometer." Applied Optics 37, no. 25 (September 1, 1998): 5886. http://dx.doi.org/10.1364/ao.37.005886.

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16

Campàs, Mònica, Maria G. Olteanu, and Jean-Louis Marty. "Enzymatic recycling for signal amplification: Improving microcystin detection with biosensors." Sensors and Actuators B: Chemical 129, no. 1 (January 2008): 263–67. http://dx.doi.org/10.1016/j.snb.2007.08.009.

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17

Yan, Mengmeng, Wenhui Bai, Chao Zhu, Yafei Huang, Jiao Yan, and Ailiang Chen. "Design of nuclease-based target recycling signal amplification in aptasensors." Biosensors and Bioelectronics 77 (March 2016): 613–23. http://dx.doi.org/10.1016/j.bios.2015.10.015.

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18

Zhou, Jiawan, Xiaohua Zhang, Erhu Xiong, Peng Yu, Xiaoyu Li, and Jinhua Chen. "SDR-recycling signal amplification for highly sensitive methyltransferase activity assay." Journal of Electroanalytical Chemistry 781 (November 2016): 304–9. http://dx.doi.org/10.1016/j.jelechem.2016.06.019.

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19

Zhang, Teng, Joe Bentley, and Haixing Miao. "A Broadband Signal Recycling Scheme for Approaching the Quantum Limit from Optical Losses." Galaxies 9, no. 1 (January 1, 2021): 3. http://dx.doi.org/10.3390/galaxies9010003.

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Quantum noise limits the sensitivity of laser interferometric gravitational-wave detectors. Given the state-of-the-art optics, the optical losses define the lower bound of the best possible quantum-limited detector sensitivity. In this work, we come up with a broadband signal recycling scheme which gives a potential solution to approaching this lower bound by converting the signal recycling cavity to be a broadband signal amplifier using an active optomechanical filter. We will show the difference and advantage of such a scheme compared with the previous white light cavity scheme using the optomechanical filter in [Phys.Rev.Lett.115.211104 (2015)]. The drawback is that the new scheme is more susceptible to the thermal noise of the mechanical oscillator.
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20

Schroder-Kohne, S., F. Letourneur, and H. Riezman. "Alpha-COP can discriminate between distinct, functional di-lysine signals in vitro and regulates access into retrograde transport." Journal of Cell Science 111, no. 23 (December 1, 1998): 3459–70. http://dx.doi.org/10.1242/jcs.111.23.3459.

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Emp47p is a yeast Golgi transmembrane protein with a retrograde, Golgi to ER transport di-lysine signal in its cytoplasmic tail. Emp47p has previously been shown to recycle between the Golgi complex and the ER and to require its di-lysine signal for Golgi localization. In contrast to other proteins with di-lysine signals, the Golgi-localization of Emp47p has been shown to be preserved in ret1-1 cells expressing a mutant alpha-COP subunit of coatomer. Here we demonstrate by sucrose gradient fractionation and immunofluorescence analysis that recycling of Emp47p was unimpaired in ret1-1. Furthermore we have characterized three new alleles of ret1 and showed that Golgi localization of Emp47p was intact in cells with those mutant alleles. We could correlate the ongoing recycling of Emp47p in ret1-1 with preserved in vitro binding of coatomer from ret1-1 cells to immobilized GST-Emp47p-tail fusion protein. As previously reported, the di-lysine signal of Wbp1p was not recognized by ret1-1 mutant coatomer, suggesting a possible role for alpha-COP in the differential binding to distinct di-lysine signals. In contrast to results with alpha-COP mutants, we found that Emp47p was mislocalised to the vacuole in mutants affecting beta'-, gamma-, delta-, and zeta-COP subunits of coatomer and that the mutant coatomer bound neither to the Emp47p nor to the Wbp1p di-lysine signal in vitro. Therefore, the retrograde transport of Emp47p displayed a differential requirement for individual coatomer subunits and a special role of alpha-COP for a particular transport step in vivo.
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21

Vieira, Peter A., He Zhizhuang, Shi-Kit Chan, and Akbar Montaser. "Evaluation of Recycling Cyclone Spray Chambers for ICP-AES." Applied Spectroscopy 40, no. 8 (November 1986): 1141–46. http://dx.doi.org/10.1366/0003702864507512.

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Two cyclone spray chambers of different sizes are evaluated for inductively coupled plasma/atomic emission spectrometry. On the basis of a simplified mathematical model, the cut-off diameters of the aerosol droplets are estimated to be 2.2 to 4.3 and 1.8 to 3.5 μm for the large and the small cyclones, respectively. The sample consumption rate can be reduced to about 50 μL/min when the cyclone chamber is used in a recycling mode. In general, the signal-to-background ratios, detection limits, and precisions of the analyte signal intensities obtained with the small cyclone chamber are slightly superior to those achieved with a Scott spray chamber and a recycling gravitational sedimentation chamber. The performance of the recycling cyclone chamber is also evaluated for the determination of copper in the NBS freeze-dried urine.
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22

Lu, Yao, Hau-tieng Wu, and John Malik. "Recycling cardiogenic artifacts in impedance pneumography." Biomedical Signal Processing and Control 51 (May 2019): 162–70. http://dx.doi.org/10.1016/j.bspc.2019.02.027.

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23

Chen, Zhe-Yu, Alessandro Ieraci, Michael Tanowitz, and Francis S. Lee. "A Novel Endocytic Recycling Signal Distinguishes Biological Responses of Trk Neurotrophin Receptors." Molecular Biology of the Cell 16, no. 12 (December 2005): 5761–72. http://dx.doi.org/10.1091/mbc.e05-07-0651.

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Endocytic trafficking of signaling receptors to alternate intracellular pathways has been shown to lead to diverse biological consequences. In this study, we report that two neurotrophin receptors (tropomyosin-related kinase TrkA and TrkB) traverse divergent endocytic pathways after binding to their respective ligands (nerve growth factor and brain-derived neurotrophic factor). We provide evidence that TrkA receptors in neurosecretory cells and neurons predominantly recycle back to the cell surface in a ligand-dependent manner. We have identified a specific sequence in the TrkA juxtamembrane region, which is distinct from that in TrkB receptors, and is both necessary and sufficient for rapid recycling of internalized receptors. Conversely, TrkB receptors are predominantly sorted to the degradative pathway. Transplantation of the TrkA recycling sequence into TrkB receptors reroutes the TrkB receptor to the recycling pathway. Finally, we link these divergent trafficking pathways to alternate biological responses. On prolonged neurotrophin treatment, TrkA receptors produce prolonged activation of phosphatidylinositol 3-kinase/Akt signaling as well as survival responses, compared with TrkB receptors. These results indicate that TrkA receptors, which predominantly recycle in signal-dependent manner, have unique biological properties dictated by its specific endocytic trafficking itinerary.
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24

Liang, Dong, Wei You, Yang Yu, Yao Geng, Feng Lv, and Bin Zhang. "A cascade signal amplification strategy for ultrasensitive colorimetric detection of BRCA1 gene." RSC Advances 5, no. 35 (2015): 27571–75. http://dx.doi.org/10.1039/c5ra01766a.

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25

Schulze, U., M. Broich, O. Weiss, and T. G. Noll. "A low power clock generator with adaptive inter-phase charge balancing for variability compensation in 40-nm CMOS." Advances in Radio Science 9 (August 1, 2011): 241–45. http://dx.doi.org/10.5194/ars-9-241-2011.

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Abstract. Power dissipation besides chip area is still one main optimization issue in high performance CMOS design. Regarding high throughput building blocks for digital signal processing architectures which are optimized down to the physical level a complementary two-phase clocking scheme (CTPC) is often advantageous concerning ATE-efficiency. The clock system dissipates a significant part of overall power up to more than 50% in some applications. One efficient power saving strategy for CTPC signal generation is the charge balancing technique. To achieve high efficiency with this approach a careful optimization of timing relations within the control is inevitable. However, as in modern CMOS processes device variations increase, timing relations between sensitive control signals can be affected seriously. In order to compensate for the influence of global and local variations in this work, an adaptive control system for charge balancing in a CTPC generator is presented. An adjustment for the degree of charge recycling is performed in each clock cycle. In the case of insufficient recycling the delay elements which define duration and timing position of the recycling pulse are corrected by switchable timing units. In a benchmark with the conventional clock generation system, a power reduction gain of up to 24.7% could be achieved. This means saving in power of more than 12% for a complete number-crunching building block.
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26

Marsh, E. W., P. L. Leopold, N. L. Jones, and F. R. Maxfield. "Oligomerized transferrin receptors are selectively retained by a lumenal sorting signal in a long-lived endocytic recycling compartment." Journal of Cell Biology 129, no. 6 (June 15, 1995): 1509–22. http://dx.doi.org/10.1083/jcb.129.6.1509.

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Cross-linking of surface receptors results in altered receptor trafficking in the endocytic system. To better understand the cellular and molecular mechanisms by which receptor cross-linking affects the intracellular trafficking of both ligand and receptor, we studied the intracellular trafficking of the transferrin receptor (TfR) bound to multivalent-transferrin (Tf10) which was prepared by chemical cross-linking of transferrin (Tf). Tf10 was internalized about two times slower than Tf and was retained four times longer than Tf, without being degraded in CHO cells. The intracellular localization of Tf10 was investigated using fluorescence and electron microscopy. Tf10 was not delivered to the lysosomal pathway followed by low density lipoprotein but remained accessible to Tf in the pericentriolar endocytic recycling compartment for at least 60 min. The retained Tf10 was TfR-associated as demonstrated by a reduction in surface TfR number when cells were incubated with Tf10. The presence of Tf10 within the recycling compartment did not affect trafficking of subsequently endocytosed Tf. Retention of Tf10 within the recycling compartment did not require the cytoplasmic domain of the TfR since Tf10 exited cells with the same rate when bound to the wild-type TfR or a mutated receptor with only four amino acids in the cytoplasmic tail. Thus, cross-linking of surface receptors by a multivalent ligand acts as a lumenal retention signal within the recycling compartment. The data presented here show that the recycling compartment labeled by Tf10 is a long-lived organelle along the early endosome recycling pathway that remains fusion accessible to subsequently endocytosed Tf.
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27

Gerasimova, Yulia V., and Dmitry M. Kolpashchikov. "Enzyme-assisted target recycling (EATR) for nucleic acid detection." Chem. Soc. Rev. 43, no. 17 (2014): 6405–38. http://dx.doi.org/10.1039/c4cs00083h.

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28

Lin, Xiaoyan, Liang Cui, Yishun Huang, Ya Lin, Yi Xie, Zhi Zhu, Bincheng Yin, Xi Chen, and Chaoyong James Yang. "Carbon nanoparticle-protected aptamers for highly sensitive and selective detection of biomolecules based on nuclease-assisted target recycling signal amplification." Chem. Commun. 50, no. 57 (2014): 7646–48. http://dx.doi.org/10.1039/c4cc02184c.

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29

Li, Na, Zhong Feng Gao, Bei Hua Kang, Nian Bing Li, and Hong Qun Luo. "Sensitive mutant DNA biomarker detection based on magnetic nanoparticles and nicking endonuclease assisted fluorescence signal amplification." RSC Advances 5, no. 26 (2015): 20020–24. http://dx.doi.org/10.1039/c4ra17059h.

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30

Xiao, Yanqing, Jingkuang Liu, and Yongshi Pang. "Co-evolution of Construction Waste Recycling Industrial Chain Based on Lotka–volterra Model." International Journal of Circuits, Systems and Signal Processing 15 (August 5, 2021): 859–82. http://dx.doi.org/10.46300/9106.2021.15.94.

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Under the green building policy, the recycling of construction waste has become an important issue. However, many obstructions in the industrial chain of construction waste recycling, slow integration of production elements in the chain, and inefficient resource allocation hinder the development of the construction waste recycling industry. In this study, a co-evolution model of the industrial chain of construction waste recycling is constructed based on the Lotka–Volterra model, and the Jacobian matrix is used for stability analysis. Finally, a numerical simulation is performed. The simulation results indicate that: (1) There is a high product correlation between upstream and downstream enterprises in the industrial chain of construction waste recycling; (2) The conversion coefficient of supply and demand of upstream and downstream enterprises has a higher impact on and is more sensitive to the evolution of this industrial chain; (3) The co-evolution of upstream and downstream enterprises promotes the added value of products and maximizes the overall benefits of the industrial chain, which provides reference value and theoretical basis for the development of the industrial chain of construction waste recycling.
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Xu, Yuanyuan, Linghao Sun, Xiaocui Huang, Yangyang Sun, and Chenhe Lu. "A label-free and signal-on electrochemical aptasensor for ultrasensitive kanamycin detection based on exonuclease recycling cleavage." Analytical Methods 8, no. 4 (2016): 726–30. http://dx.doi.org/10.1039/c5ay02754c.

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32

Zhang, Zhang, Min Mei, Juan Yao, Ting Ye, Jing Quan, and Jinbo Liu. "An off/on thrombin activated energy driven molecular machine for sensitive detection of human thrombin via non-enzymatic catalyst recycling amplification." Analyst 145, no. 21 (2020): 6868–74. http://dx.doi.org/10.1039/d0an01054e.

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33

Lv, Lei, Donghao Li, Chengbi Cui, Yangyang Zhao, and Zhijun Guo. "Nuclease-aided target recycling signal amplification strategy for ochratoxin A monitoring." Biosensors and Bioelectronics 87 (January 2017): 136–41. http://dx.doi.org/10.1016/j.bios.2016.08.024.

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Zhao, Zhihan, Shixing Chen, Jianbang Wang, Jing Su, Jiaqiang Xu, Sanjay Mathur, Chunhai Fan, and Shiping Song. "Nuclease-free target recycling signal amplification for ultrasensitive multiplexing DNA biosensing." Biosensors and Bioelectronics 94 (August 2017): 605–8. http://dx.doi.org/10.1016/j.bios.2017.03.051.

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35

Nishizawa, A., S. Kawamura, and Masa-aki Sakagami. "Quantum noise in differential-type gravitational-wave interferometer and signal recycling." Journal of Physics: Conference Series 122 (July 1, 2008): 012019. http://dx.doi.org/10.1088/1742-6596/122/1/012019.

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36

Kang, H., and S. B. Kaplan. "Current recycling and SFQ signal transfer in large scale RSFQ circuits." IEEE Transactions on Appiled Superconductivity 13, no. 2 (June 2003): 547–50. http://dx.doi.org/10.1109/tasc.2003.813932.

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37

Ballmer-Hofer, Kurt, Anneli E. Andersson, Laura E. Ratcliffe, and Philipp Berger. "Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output." Blood 118, no. 3 (July 21, 2011): 816–26. http://dx.doi.org/10.1182/blood-2011-01-328773.

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Abstract Vascular endothelial growth factors (VEGFs) regulate blood and lymph vessel development by activating 3 receptor tyrosine kinases (RTKs), VEGFR-1, -2, and -3, and by binding to coreceptors such as neuropilin-1 (NRP-1). We investigated how different VEGF-A isoforms, in particular VEGF-A165a and VEGF-A165b, control the balance between VEGFR-2 recycling, degradation, and signaling. Stimulation of cells with the NRP-1–binding VEGF-A165a led to sequential NRP-1–mediated VEGFR-2 recycling through Rab5, Rab4, and Rab11 vesicles. Recycling was accompanied by dephosphorylation of VEGFR-2 between Rab4 and Rab11 vesicles and quantitatively and qualitatively altered signal output. In cells stimulated with VEGF-A165b, an isoform unable to bind NRP-1, VEGFR-2 bypassed Rab11 vesicles and was routed to the degradative pathway specified by Rab7 vesicles. Deletion of the GIPC (synectin) binding motif of NRP-1 prevented transition of VEGFR-2 through Rab11 vesicles and attenuated signaling. Coreceptor engagement was specific for VEGFR-2 because EGFR recycled through Rab11 vesicles in the absence of known coreceptors. Our data establish a distinct role of NRP-1 in VEGFR-2 signaling and reveal a general mechanism for the function of coreceptors in modulating RTK signal output.
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38

Xu, Lin, Bingying Jiang, Wenjiao Zhou, Ruo Yuan, and Yun Xiang. "Coupling strand extension/excision amplification with target recycling enables highly sensitive and aptamer-based label-free sensing of ATP in human serum." Analyst 145, no. 2 (2020): 434–39. http://dx.doi.org/10.1039/c9an02000d.

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Zhang, Jun, Fengying Ran, Wenbo Zhou, Bing Shang, Fei Yu, Lun Wu, Wanbao Hu, Xueqin He, and Qinhua Chen. "Ultrasensitive fluorescent aptasensor for MUC1 detection based on deoxyribonuclease I-aided target recycling signal amplification." RSC Advances 8, no. 56 (2018): 32009–15. http://dx.doi.org/10.1039/c8ra06498a.

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40

Iovine, M. Kathryn, and Susan R. Wente. "A Nuclear Export Signal in Kap95p Is Required for Both Recycling the Import Factor and Interaction with the Nucleoporin GLFG Repeat Regions of Nup116p and Nup100p." Journal of Cell Biology 137, no. 4 (May 19, 1997): 797–811. http://dx.doi.org/10.1083/jcb.137.4.797.

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During nuclear import, cytosolic transport factors move through the nuclear pore complex (NPC) to the nuclear compartment. Kap95p is required during import for docking the nuclear localization signal-receptor and ligand to the NPC. Recycling of this factor back to the cytoplasm is necessary for continued rounds of import; however, the mechanism for Kap95p recycling is unknown. We have determined that recycling of Kap95p requires a nuclear export signal (NES). A region containing the NES in Kap95p was sufficient to mediate active nuclear export in a microinjection assay. Moreover, the NES was necessary for function. Mutation of the NES in Kap95p resulted in a temperaturesensitive import mutant, and immunofluorescence microscopy experiments showed that the mutated Kap95p was not recycled but instead localized in the nucleus and at the nuclear envelope. Srp1p, the yeast nuclear localization signal-receptor, also accumulated in the nuclei of the arrested kap95 mutant cells. Wild-type and NES-mutated Kap95p both bound Gsp1p (the yeast Ran/TC4 homologue), Srp1p, and the FXFG repeat region of the nucleoporin Nup1p. In contrast, the NES mutation abolished Kap95p interaction with the GLFG repeat regions from the nucleoporins Nup116p and Nup100p. In vivo interaction was demonstrated by isolation of Kap95p from yeast nuclear lysates in either protein A–tagged Nup116p or protein A–tagged Nup100p complexes. The protein A–tagged Nup116p complex also specifically contained Gle2p. These results support a model in which a step in the recycling of Kap95p is mediated by interaction of an NES with GLFG regions. Analysis of genetic interactions suggests Nup116p has a primary role in Kap95p recycling, with Nup100p compensating in the absence of Nup116p. This finding highlights an important role for a subfamily of GLFG nucleoporins in nuclear export processes.
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Qiang Wei, M. Ripeanu, and K. Beznosov. "Cooperative Secondary Authorization Recycling." IEEE Transactions on Parallel and Distributed Systems 20, no. 2 (February 2009): 275–88. http://dx.doi.org/10.1109/tpds.2008.80.

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Fu, Caili, Chang Liu, Shaoyun Wang, Fang Luo, Zhenyu Lin, and Guonan Chen. "A signal-on homogeneous electrochemical biosensor for sequence-specific microRNA based on duplex-specific nuclease-assisted target recycling amplification." Analytical Methods 8, no. 39 (2016): 7034–39. http://dx.doi.org/10.1039/c6ay02039a.

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Bao, Ting, Wei Wen, Lei Shu, Xiuhua Zhang, and Shengfu Wang. "Label-free and dual-amplified electrochemical detection of Hg2+ based on self-assembled DNA nanostructures and target-triggered exonuclease cleavage activity." New Journal of Chemistry 40, no. 8 (2016): 6686–91. http://dx.doi.org/10.1039/c6nj00265j.

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Li, Xiang, Xuelian Ding, and Jing Fan. "Nicking endonuclease-assisted signal amplification of a split molecular aptamer beacon for biomolecule detection using graphene oxide as a sensing platform." Analyst 140, no. 23 (2015): 7918–25. http://dx.doi.org/10.1039/c5an01759a.

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Yan, Xing, Wenkai Li, Keyi Liu, and Le Deng. "Highly sensitive fluorescent aptasensor for Salmonella paratyphi A via DNase I-mediated cyclic signal amplification." Analytical Methods 7, no. 24 (2015): 10243–50. http://dx.doi.org/10.1039/c5ay02298c.

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Zhang, Jingjing, Chunyuan Song, Huiling Zhou, Juan Jia, Yinna Dai, Daxiang Cui, Lianhui Wang, and Lixing Weng. "A dual signal amplification strategy for the highly sensitive fluorescence detection of nucleic acids." Analyst 145, no. 4 (2020): 1219–26. http://dx.doi.org/10.1039/c9an02183c.

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Hong, Zhilin, Genwang Chen, Shaoyang Yu, Rongfu Huang, and Chunmei Fan. "A potentiometric aptasensor for carcinoembryonic antigen (CEA) on graphene oxide nanosheets using catalytic recycling of DNase I with signal amplification." Analytical Methods 10, no. 45 (2018): 5364–71. http://dx.doi.org/10.1039/c8ay02113a.

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A label-free potentiometric aptasensing platform was designed for detection of carcinoembryonic antigen on a graphene oxide-modified electrode coupling with target recycling-assisted signal amplification.
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48

Lewis, Michael J., Benjamin J. Nichols, Cristina Prescianotto-Baschong, Howard Riezman, and Hugh R. B. Pelham. "Specific Retrieval of the Exocytic SNARE Snc1p from Early Yeast Endosomes." Molecular Biology of the Cell 11, no. 1 (January 2000): 23–38. http://dx.doi.org/10.1091/mbc.11.1.23.

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Many endocytosed proteins in yeast travel to the vacuole, but some are recycled to the plasma membrane. We have investigated the recycling of chimeras containing green fluorescent protein (GFP) and the exocytic SNARE Snc1p. GFP-Snc1p moves from the cell surface to internal structures when Golgi function or exocytosis is blocked, suggesting continuous recycling via the Golgi. Internalization is mediated by a conserved cytoplasmic signal, whereas diversion from the vacuolar pathway requires sequences within and adjacent to the transmembrane domain. Delivery from the Golgi to the surface is also influenced by the transmembrane domain, but the requirements are much less specific. Recycling requires the syntaxins Tlg1p and Tlg2p but not Pep12p or proteins such as Vps4p and Vps5p that have been implicated in late endosome–Golgi traffic. Subtle changes to the recycling signal cause GFP-Snc1p to accumulate preferentially in punctate internal structures, although it continues to recycle to the surface. The internal GFP-Snc1p colocalizes with Tlg1p, and immunofluorescence and immunoelectron microscopy reveal structures that contain Tlg1p, Tlg2p, and Kex2p but lack Pep12p and Sec7p. We propose that these represent early endosomes in which sorting of Snc1p and late Golgi proteins occurs, and that transport can occur directly from them to the Golgi apparatus.
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Zheng, Li, and Sean D. Conner. "Glycogen synthase kinase 3β inhibition enhances Notch1 recycling." Molecular Biology of the Cell 29, no. 4 (February 15, 2018): 389–95. http://dx.doi.org/10.1091/mbc.e17-07-0474.

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The Notch signaling pathway is essential throughout development and remains active into adulthood, where it performs a critical role in tissue homeostasis. The fact that defects in signaling can lead to malignancy illustrates the need to control Notch activity tightly. GSK3β is an established regulator of the Notch signaling pathway, although its mechanism of action remains unclear. Given the emerging role for GSK3β in receptor trafficking, we tested the idea that GSK3β controls signaling by regulating Notch transport. Consistent with published reports, we find that GSK3β inhibition enhances Notch1 signaling activity. Immunolocalization analysis reveals that Notch1 localization within a tubulovesicular compartment is altered when GSK3β activity is disrupted. We also find that receptor cell surface levels increase following acute GSK3β inhibition. This is followed by elevated Notch intra­cellular domain (NICD) production and a corresponding increase in signaling activity. Moreover, Notch transport assays reveal that receptor recycling rates increase when GSK3β activity is inhibited. Collectively, results presented here support a model where GSK3β regulates signaling by controlling postendocytic transport of Notch1. Given that GSK3β activity is suppressed following stimulation by multiple signal transduction pathways, our findings also suggest that cells can modulate Notch1 activity in response to extracellular signals by mobilizing Notch1 from endosomal stores.
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Liu, Zhongzhi, Dan Luo, Fangling Ren, Fengying Ran, Wei Chen, Bingqiang Zhang, Ceming Wang, Hao Chen, Jian Wei, and Qinhua Chen. "Ultrasensitive fluorescent aptasensor for CRP detection based on the RNase H assisted DNA recycling signal amplification strategy." RSC Advances 9, no. 21 (2019): 11960–67. http://dx.doi.org/10.1039/c9ra01352k.

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An aptamer-based method for the ultrasensitive fluorescence detection of C-reactive protein (CRP) was developed using the ribonuclease H (RNase H) assisted DNA recycling signal amplification strategy.
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