Relevant bibliographies by topics / Unfolded

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Unfolded'

Author: Grafiati
Published: 10 March 2023

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Journal articles on the topic "Unfolded"

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ALMAZ, E., A. CENGIZ, and A. TARTAR. "UNFOLDING CONTINUOUS PHOTON SPECTRUM EMITTED FROM 90Sr-90Y IN EQUILIBRIUM." International Journal of Modern Physics E 16, no. 06 (July 2007): 1733–40. http://dx.doi.org/10.1142/s0218301307006939.

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This paper presents an experiment with the 2×2 inch NaI(Tl) detector to measure the internal bremsstrahlung of 90 Sr -90 Y in equilibrium beta particle emitters using the beta-stopper method in the range 10–1750 keV. The Gold algorithm is applied to unfold the internal bremsstrahlung spectrum of 90 Sr -90 Y beta source. Unfolded IB spectrum is compared with the KUB theory. There is good agreement between the theory and the unfolded measured spectrum in the energy range below 1000 keV. Beyond this energy, there are discrepancies between the theory and unfolded spectrum.
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Ferri, Sabrina. "Unfolded History." New Vico Studies 25 (2007): 87–96. http://dx.doi.org/10.5840/newvico2007257.

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Anderson, K. "Drosophila Unfolded." Science 256, no. 5059 (May 15, 1992): 1053–54. http://dx.doi.org/10.1126/science.256.5059.1053.

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Snapp, Erik. "Unfolded Protein Responses With or Without Unfolded Proteins?" Cells 1, no. 4 (November 1, 2012): 926–50. http://dx.doi.org/10.3390/cells1040926.

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Lapidus, Lisa J. "Protein unfolding mechanisms and their effects on folding experiments." F1000Research 6 (September 22, 2017): 1723. http://dx.doi.org/10.12688/f1000research.12070.1.

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In this review, I discuss the various methods researchers use to unfold proteins in the lab in order to understand protein folding both in vitro and in vivo. The four main techniques, chemical-, heat-, pressure- and force-denaturation, produce distinctly different unfolded conformational ensembles. Recent measurements have revealed different folding kinetics from different unfolding mechanisms. Thus, comparing these distinct unfolded ensembles sheds light on the underlying free energy landscape of folding.
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Liu, Xiong, Shi Shu, and Edward D. Korn. "Polymerization pathway of mammalian nonmuscle myosin 2s." Proceedings of the National Academy of Sciences 115, no. 30 (July 11, 2018): E7101—E7108. http://dx.doi.org/10.1073/pnas.1808800115.

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The three mammalian nonmuscle myosin 2 (NM2) monomers, like all class 2 myosin monomers, are hexamers of two identical heavy (long) chains and two pairs of light (short) chains bound to the heavy chains. The heavy chains have an N-terminal globular motor domain (head) with actin-activated ATPase activity, a lever arm (neck) to which the two light chains bind, and a coiled-coil helical tail. Monomers polymerize into bipolar filaments, with globular heads at each end separated by a bare zone, by antiparallel association of their coiled-coil tails. NM2 filaments are highly dynamic in situ, frequently disassembling and reassembling at different locations within the cell where they are essential for multiple biological functions. Therefore, it is important to understand the mechanisms of filament polymerization and depolymerization. Monomers can exist in two states: folded and unfolded. It has been thought that unfolded monomers form antiparallel dimers that assemble into bipolar filaments. We now show that polymerization in vitro proceeds from folded monomers to folded antiparallel dimers to folded antiparallel tetramers that unfold forming antiparallel bipolar tetramers. Folded dimers and tetramers then associate with the unfolded tetramer and unfold, forming a mature bipolar filament consisting of multiple unfolded tetramers with an entwined bare zone. We also demonstrate that depolymerization is essentially the reverse of the polymerization process. These results will advance our understanding of NM2 filament dynamics in situ.
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Riddihough, G. "Unfolded in vivo." Science 353, no. 6306 (September 22, 2016): 1377–79. http://dx.doi.org/10.1126/science.353.6306.1377-l.

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LYKKEN, JOSEPH, and MARIA SPIROPULU. "LHC DISCOVERIES UNFOLDED." International Journal of Modern Physics A 23, no. 22 (September 10, 2008): 3441–59. http://dx.doi.org/10.1142/s0217751x08042298.

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Townley, W. A., R. Baker, N. Sheppard, and A. O. Grobbelaar. "Dupuytren's contracture unfolded." BMJ 332, no. 7538 (February 16, 2006): 397–400. http://dx.doi.org/10.1136/bmj.332.7538.397.

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Orr, Harry T. "An unfolded protein." Lancet 358 (December 2001): S35. http://dx.doi.org/10.1016/s0140-6736(01)07048-9.

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Dissertations / Theses on the topic "Unfolded"

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Griffiths, John Mark Ainsley. "The trinitarian gift unfolded : sacrifice, resurrection, communion." Thesis, University of Nottingham, 2015. http://eprints.nottingham.ac.uk/29014/.

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Contentious unresolved philosophical and anthropological questions beset contemporary gift theories. What is the gift? Does it expect, or even preclude, some counter-gift? Should the gift ever be anticipated, celebrated or remembered? Can giver, gift and recipient appear concurrently? Must the gift involve some tangible ‘thing’, or is the best gift objectless? Is actual gift-giving so tainted that the pure gift vaporises into nothing more than a remote ontology, causing unbridgeable separation between the gift-as-practised and the gift-as-it-ought-to-be? In short, is the gift even possible? Such issues pervade scholarly treatments across a wide intellectual landscape, often generating fertile inter-disciplinary crossovers whilst remaining philosophically aporetic. Arguing largely against philosophers Jacques Derrida and Jean-Luc Marion and partially against the empirical gift observations of anthropologist Marcel Mauss, I contend in this thesis that only a theological – specifically trinitarian – reading liberates the gift from the stubborn impasses which non-theological approaches impose. That much has been argued eloquently by theologians already, most eminently John Milbank, yet largely with a philosophical slant. I develop the field by demonstrating that the Scriptures, in dialogue with the wider Christian dogmatic tradition, enrich discussions of the gift, showing how creation, which emerges ex nihilo in Christ, finds its completion in him as creatures observe and receive his own perfect, communicable gift alignment. In the ‘gift-object’ of human flesh, believers rejoicingly discern Christ receiving-in-order-to-give and giving-in-order-to-receive, the very reciprocal giftedness that Adamic humanity spurned. Moreover, the depths of Christ’s crucified self-giving and the heights of resurrectional glory, culminating in the Spirit’s eternal communion, convey sin-bound creatures into the new creation, towards their deified end, through liturgical mediation which reveals true giftedness. The gift is thus no aporetic embarrassment but the means of entry into and – more significantly – the very texture of the new, eucharistic creation.
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Topping, K. D. "NMR studies of the unfolded stated of lysozyme." Thesis, University of Oxford, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.235073.

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Salsas, Escat Ramon. "The role of unfolded states in collagen degradation." Thesis, Massachusetts Institute of Technology, 2010. http://hdl.handle.net/1721.1/57555.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Computational and Systems Biology Program, 2010.
This electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections.
Cataloged from student-submitted PDF version of thesis.
Includes bibliographical references.
Excessive collagen degradation (collagenolysis) has been implicated in a series of diseases such as tumor metastasis, atherosclerosis and arthritis. There are still several unresolved questions about the mechanism of collagenolysis. First, the prototypical structure of the collagen triple helix does not fit into the active site of collagenases, the enzymes responsible of cleaving collagen. Moreover, the scissile bond that is degraded during collagenolysis is hidden from solvent. Therefore it is widely agreed that collagen unfolding must occur in order for collagenolysis to proceed. Some proposed mechanisms suggest that collagenases actively unfold collagen in order to expose the cleavage site, but no direct evidence of such mechanisms has been provided. Second, while several potential cleavage sites exist in the sequence of collagen, only one is cleaved in triple helical collagen. The hypothesis of this work is that locally unfolded states exist in collagen in the absence of collagenases. They occur as a result of the natural thermal fluctuations in the structure of collagen. Collagenolysis occurs when collagenases bind and cleave these unfolded states. In this work, a combination of computational and experimental methods is presented in order to test this hypothesis. Initially, computational results suggest that locally unfolded states are ubiquitous along the structure of collagen. However, it is shown that not all unfolded states are created equal, and that the precise sequence in the vicinity of the true collagenase cleavage site in type III collagen allows collagen to sample locally unfolded states that are complimentary to the collagenase active site. Therefore, it is hypothesized that cleavage site specificity is encoded in the nature of the unfolded states. Next, it is shown that types I and III collagen can be bound and cleaved at the actual cleavage site by just the catalytic domain of collagenases, a finding in apparent contradiction with previous work in this field. These results are interpreted in light of a novel conformational selection mechanism in which collagenases only cleave locally unfolded, vulnerable states. Finally, based on the new mechanism of collagenolysis presented here, new strategies to regulate collagenolysis are proposed.
by Ramon Salsas Escat.
Ph.D.
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Sanchez, Puig Nuria. "Biophysical studies on native unfolded and misfolded proteins." Thesis, University of Cambridge, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.613772.

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Kwok, Alice. "Unfolded protein responses in models of Motor Neuron Disease." Thesis, University of Oxford, 2010. http://ora.ox.ac.uk/objects/uuid:2f3efba7-dce1-4521-bda6-4db8ee81094d.

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Motor neuron disorders are a heterogeneous group of diseases characterized by the selective degeneration of motor neurons leading to muscle wasting and atrophy. Amyotrophic Lateral Sclerosis (ALS) is the most common amongst these disorders and is characterized by the selective loss of both upper and lower motor neurons in the brain and spinal cord. 20% of familial cases of ALS are caused by mutations in the Cu, Zn-superoxide dismutase gene (SOD1), a ubiquitously expressed enzyme responsible for scavenging superoxide radicals. The exact mechanisms underlying mutant SOD1-mediated neurotoxicity are unknown. Misfolded mutant SOD1 accumulates in the cytosol and mitochondrial intermembrane space (IMS) indicating the involvement of unfolded protein responses in ALS pathogenesis. Unfolded protein responses (UPRs) are complex signal transduction cascades which detect perturbations in protein folding and couple them to the expression of protein quality control machinery thereby allowing individual compartments to adapt to stress. In the cytosol, this study has shown that HspB8 was upregulated by SOD1 mutants, where it induced the clearance of aggregates by macroautophagy. This is a protective mechanism, as overexpression of HspB8 suppressed mutant-SOD1 mediated toxicity. In contrast, HspB8 mutants were impaired in macroautophagy and are toxic to NSC-34 cells. The mechanisms for the IMS-UPR have not been previously identified. To address this issue, a model for the accumulation of misfolded mutant SOD1 within the IMS was created and candidate proteins involved in protein quality control within the IMS were explored at the transcriptional level and at the level of protein expression. Preliminary results revealed some possible candidates that may have a role in the adaptation to mitochondrial stress. Interestingly, increased mitophagy was also found in IMS-G93A expressing cells, advocating the central role of macroautophagy in eliminating protein aggregates and damaged mitochondria in SOD1-FALS.
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Gianni, Davide. "The role of unfolded protein deposits in cardiac dysfunction." Thesis, Imperial College London, 2011. http://hdl.handle.net/10044/1/7029.

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In this study we investigated the role of unfolded proteins as a toxic insult for cardiomyocytes in idiopathic dilated cardiomyopathy (DCM). We first confirmed the presence of amyloid fibers in DCM cardiomyocytes by histological and ultrastructural analysis, showing their preferentially intracellular distribution. These molecular species seem to coexist with low-complexity β-folded precursors (oligomers) which in our experiments could promote increase of systolic Ca2+ in normal cardiomyocytes and alterations of contractility. Our results suggest that these molecular species trigger the overexpression of UPR components such as GRPs, Chop and Caspase 12. In addition we demonstrated the presence of interactions between presenilins (PS) and Serca2a, suggesting a regulatory role of these Alzheimer’s-related proteins on the Ca2+ pump. The genetic analysis of the presenilin genes in DCM samples identified two undescribed mutations in the promoter of PS1, which appeared to inhibit the expression of the protein. The quantification of the presenilin levels showed a considerable decrease of PS2 associated with an increase of PS1. In order to characterize the protein(s) involved in the aggregasomes, we developed a series of purification protocols, which, unfortunately, did not identify a single protein species. As an alternative approach, we focused on the identification of transcripts differentially expressed in iDCM. Our study introduces an innovative three-group analysis in which we used amyloid samples to eliminate the interference related to the accumulation of unfolded peptides and deriving from the progression of HF. Interestingly we recognized a limited number of iDCM-specific genes, including nestin and DSCR1, which are normally correlated to neural development. In conclusion, our findings open intriguing perspectives to increase our knowledge of the etiology and progression of DCM. However further investigation is required to identify the protein(s) involved in the formation of the aggregasomes and the role of these molecular structures in the etiology of the disease.
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Pashley, Clare Louise. "Characterising the unfolded state of Im7 in non-denaturing conditions." Thesis, University of Leeds, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.550343.

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An understanding of the structural ensemble of the species present at the commencement of protein folding may help to elucidate the role of the primary amino acid sequence in narrowing the search for the native conformation during protein folding. Characterisation of this species is often difficult since the folded state is the predominantly populated species at equilibrium. In addition to this, the study of disordered proteins suffers from a lack of restraints, since the protein can adopt many different conformations in solution. However, advances in computational methods now make it possible to build an ensemble model of the unfolded state using experimentally measured parameters. Previous work has shown the 87-residue, 4-helix protein, Im7, folds with a three-state mechanism via an on-pathway intermediate. While the transition states and populated intermediate on the folding pathway have been characterised in atomistic detail, knowledge of the unfolded ensemble under the same ambient conditions remained sparse. Although the urea denatured state of Im7 has been characterised, single molecule experiments revealed that this species of Im7 becomes compact upon dilution of the denaturant. These observations suggest that the structural ensemble of the unfolded state of Im7 is different in the absence of urea. In this thesis, destabilising amino acid substitutions were introduced into the sequence of Im7, such that the unfolded state is predominantly populated at equilibrium in the absence of denaturant. Results from far and near-UV CD, fluorescence, urea titration and heteronuclear NMR experiments reveal that three amino acid substitutions (L18A L19A L37A) are sufficient to prevent Im7 folding. Using this variant the unfolded state of Im7 under ambient conditions was then shown to be more compact, and to have increased tendency towards sampling the a-region of Φ/Ψ space compared with the protein in 6 M urea. Measurements of 15N-transverse relaxation rates revealed that sequences corresponding to helical regions in the native protein are conformationally restricted within the unfolded ensemble as a consequence of local hydrophobic clustering without substantial helix formation. By creating hydrophobic deletion mutants and measuring paramagnetic . relaxation effects, possible transient interactions between regions of the sequence relating to the native helix IV and the N-terminal region of the protein were identified, which may restrict conformational sampling within the ensemble. An atomistic model of the unfolded ensemble is then presented to create the first atomistic impression of the unfolded state of Im7. This provides a powerful tool for designing future experiments for refinement of the presented model, and for probing the effect of unfolded state interactions on the folding pathway of Im7.
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Padda, Rajneet. "Regulation of the unfolded protein response by GADD34 and CReP." Scholarly Commons, 2016. https://scholarlycommons.pacific.edu/uop_etds/170.

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The regulation of protein synthesis and protein folding is crucial for normal cell function. The endoplasmic reticulum (ER) has crucial roles in safeguarding the correct folding and assembling of proteins through the use of ER molecular chaperones. Homeostasis disruption of the ER leads to activation of the Unfolded Protein Response. The UPR is a three-arm pathway that plays a role in regulating ER stress and ultimately leads to cell survival or cell death if the cell fails to recover. There are three major proteins for sensing Endoplasmic Reticulum stress: RNA dependent protein kinase RNA like endoplasmic reticulum kinase (PERK), activating transcription factor 6 (ATF6), and inositol-requiring ER-to-nucleus signal kinase 1 (IRE1). PERK activation leads to the phosphorylation of the α-subunit of the translation initiation factor eIF2α on Serine 51 in activating its function. EIF2α phosphorylation leads to up-regulation of GADD34 and GADD34 bind protein phosphatase 1 (PP1) to dephosphorylate eIF2α and brings the cell back into homeostasis. CReP, similar to GADD34, binds to PP1, to dephosphorylate eIF2α. The RVxF motif, RARA sequence, and amino acids throughout the GADD34 sequence play a role in PP1 binding and are essential for dephosphorylating eIF2α in cells. The first 180 amino acids of GADD34 play a role in subcellular localization whereas the first 300 amino acids of CReP play a role for localization to the ER. Early on in the UPR the levels of binding immunoglobulin protein (BiP), CHOP, GADD34, and CReP increase; however, the mRNA levels of CReP drop during the 24-HR Thapsigargin treated stage. Two primary proteins that bind CReP were COPS5 and SNAPIN. Understanding the UPR is important because the inhibiting of GADD34 and CReP have been shown to improve many neurodegenerative diseases.
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Xu, Ping. "Sensing and analyzing unfolded protein response during heterologous protein production :." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 205 p, 2008. http://proquest.umi.com/pqdweb?did=1555621341&sid=2&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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Ghosh, Rajarshi. "Transcriptional Regulation of VEGFA by Unfolded Protein Response Signaling Pathway." eScholarship@UMMS, 2010. https://escholarship.umassmed.edu/gsbs_diss/469.

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The endoplasmic reticulum is the primary organelle in the cell which has the responsibility of properly folding proteins belonging to the secretory pathway. Secretory proteins are essential for a variety of functions within the body like metabolism, growth and survival. Hence, proper folding of the proteins in the ER is absolutely essential to maintain cellular and body function. The environment of the ER is substantially different from that of the cytoplasm and is primed essentially to provide the optimum conditions to fold newly synthesized polypeptides following translation by the ribosomes in the cytoplasm and on the surface of the ER. In order for secretory proteins to fold properly, ER homeostasis must be maintained. ER homeostasis is defined by the dynamic balance between the ER protein load and the ER capacity to process this load. The optimum environment of the ER, or ER homeostasis, can be perturbed by pathological processes such as hypoxia, glucose deprivation, viral infections, environmental toxins, inflammatory cytokines, and mutant protein expression, as well as by physiological processes such as aging. Disruption of ER homeostasis causes accumulation of unfolded and misfolded proteins in the ER. This condition is referred to as ER stress. Cells cope with ER stress by activating the unfolded protein response (UPR). The UPR is initiated by three ER transmembrane proteins: Inositol requiring 1 (IRE1), PKR-like ER kinase, and activating transcription factor 6 (ATF6). These three master regulators sense and interpret protein folding conditions in the ER and translate this information across the ER membrane to activate downstream effectors, spliced XBP1, phosphorylated eIF2α and ATF4, and cleaved active ATF6 respectively. These effectors have two distinct outputs, homeostatic and apoptotic. Homeostatic outputs are adaptive responses that function to attenuate ER stress and restore ER homeostasis. These responses include the attenuation of protein translation to reduce ER workload and prevent further accumulation of unfolded proteins, upregulation of molecular chaperones and protein processing enzymes to enhance the ER folding activity, and the increase in ER-associated degradation (ERAD) components to promote clearance of unfolded proteins. When ER stress reaches a point where the cells cannot tolerate the load of unfolded proteins any more, apoptosis sets in. One of the major secretory proteins in mammals, vascular endothelial growth factor VEGF, is essential for either normal or pathological angiogenesis (blood vessel development). VEGFA is the primary member of this family which is expressed in all endothelial cells and is responsible for sprouting and invasion of blood vessels into the interstitium and thus helps in supplying nutrients and oxygen to growing cells. Recent studies have indicated that cells suffering from insufficient blood supply experience ER stress. The ER needs energy and oxygen for the folding process, thus nutrient deprivation (low ATP production) and hypoxia caused by insufficient blood supply leads to inefficient protein folding and ER stress in cells, especially in cancer cells that grow and spread rapidly. This condition also occurs in the development of the mammalian placenta. The placenta is an essential tissue characterized by a lot of blood vessels. It is responsible for the exchange of nutrients and growth factors between maternal and fetal blood vessels and hence is essential for survival of the embryo. Nutrient deprivation and hypoxia stimulate the production of VEGFA and other angiogenic factors, leading to protection against ischaemic injury in both cancer cells as well as the developing placenta. In this dissertation, we report that the three master regulators of the UPR, IRE1α, PERK and ATF6α, mediate transcriptional regulation of VEGFA under ER stress in cancer cells. Inactivation of any of the three master regulators leads to attenuation of VEGFA expression under ER stress. We show that IRE1α is able to regulate VEGFA through its downstream transcription factor XBP1 which activates the VEGFA promoter. IRE1α mediated VEGFA regulation is also essential for normal development of labyrinthine trophoblast cells in the placenta. ATF6α also regulates VEGFA via its promoter. PERK is able to activate VEGFA by preferential activation of its downstream effector, ATF4, which binds intron 1 of the VEGFA gene. Thus our work reveals a twopronged differential regulatory action of the UPR sensors on VEGFA gene expression. This work suggests that a fully active UPR is essential for VEGFA upregulation under ER stress. All three regulators are required in cancer cells for normal VEGFA expression. This tight regulation of VEGFA by the UPR presents a wonderful opportunity for therapeutic intervention into angiogenic growth of tumors.
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Books on the topic "Unfolded"

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D, Rose George, ed. Unfolded proteins. Amsterdam: Academic Press, 2002.

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Pearsall, Duane D. My life unfolded. [United States]: Duane D. Pearsall, 2009.

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Kiran Nadar Museum of Art (Noida, India), ed. Crossings: Time unfolded - II. New Delhi: Kiran Nadar Museum of Art, 2012.

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Pérez-Torrado, Roberto, ed. The Unfolded Protein Response. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1732-8.

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Robert, Jacks, ed. Robert Jacks: Past unfolded. St Leonards, Sydney, NSW: Craftsman House, 2001.

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Bible chronology carefully unfolded . New York: Fleming H. Revell, 1985.

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Somdutt, Dikshit, ed. Ancestry unfolded =: Virāsata kī maṇiyām̐. [Lucknow?]: Dikshit Publications, 2008.

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Unfolded: The story of God. Nashville, TN: LifeWay Press, 2016.

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Clarke, Robert, ed. The Unfolded Protein Response in Cancer. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-05067-2.

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1941-, Logan George M., and Teskey Gordon 1953-, eds. Unfolded tales: Essays on Renaissance romance. Ithaca: Cornell University Press, 1989.

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Book chapters on the topic "Unfolded"

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Fischer, Wieland, and Jean-Pierre Seifert. "Unfolded Modular Multiplication." In Algorithms and Computation, 726–35. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-540-24587-2_74.

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"L." In Unfolded, 103–6. Birkhäuser, 2009. http://dx.doi.org/10.1515/9783034609050.103.

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"M." In Unfolded, 107–17. Birkhäuser, 2009. http://dx.doi.org/10.1515/9783034609050.107.

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"N." In Unfolded, 118–27. Birkhäuser, 2009. http://dx.doi.org/10.1515/9783034609050.118.

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"P." In Unfolded, 128–29. Birkhäuser, 2009. http://dx.doi.org/10.1515/9783034609050.128.

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"R." In Unfolded, 130–41. Birkhäuser, 2009. http://dx.doi.org/10.1515/9783034609050.130.

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"A." In Unfolded, 14–19. Birkhäuser, 2009. http://dx.doi.org/10.1515/9783034609050.14.

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"S." In Unfolded, 142–59. Birkhäuser, 2009. http://dx.doi.org/10.1515/9783034609050.142.

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"T." In Unfolded, 160–61. Birkhäuser, 2009. http://dx.doi.org/10.1515/9783034609050.160.

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"V." In Unfolded, 162–63. Birkhäuser, 2009. http://dx.doi.org/10.1515/9783034609050.162.

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Conference papers on the topic "Unfolded"

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Wang, Huan, Shuicheng Yan, Thomas Huang, and Xiaoou Tang. "Maximum unfolded embedding." In the 14th annual ACM international conference. New York, New York, USA: ACM Press, 2006. http://dx.doi.org/10.1145/1180639.1180656.

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Berloffa, E. H. "Hidden variables: basically unfolded." In SPIE Optical Engineering + Applications, edited by Chandrasekhar Roychoudhuri, Al F. Kracklauer, and Hans De Raedt. SPIE, 2013. http://dx.doi.org/10.1117/12.2019776.

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Takabe, Satoshi, and Tadashi Wadayama. "Deep Unfolded Multicast Beamforming." In GLOBECOM 2020 - 2020 IEEE Global Communications Conference. IEEE, 2020. http://dx.doi.org/10.1109/globecom42002.2020.9322114.

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Pyune, Joohyun. "A Hundred Unfolded Sighs." In ACM SIGGRAPH 2004 Art gallery. New York, New York, USA: ACM Press, 2004. http://dx.doi.org/10.1145/1185884.1185949.

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Dardikman-Yoffe, Gili, and Yonina C. Eldar. "LSPARCOM: Deep Unfolded Super-Resolution Microscopy." In 3D Image Acquisition and Display: Technology, Perception and Applications. Washington, D.C.: OSA, 2020. http://dx.doi.org/10.1364/3d.2020.jw5a.5.

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Dardikman-Yoffe, Gili, and Yonina C. Eldar. "LSPARCOM: deep unfolded super-resolution microscopy." In Single Molecule Spectroscopy and Superresolution Imaging XIV, edited by Ingo Gregor, Rainer Erdmann, and Felix Koberling. SPIE, 2021. http://dx.doi.org/10.1117/12.2577185.

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Zhu, Xue-Yang. "Efficient Retiming of Unfolded Synchronous Dataflow Graphs." In 2019 24th International Conference on Engineering of Complex Computer Systems (ICECCS). IEEE, 2019. http://dx.doi.org/10.1109/iceccs.2019.00022.

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Saon, George, Hagen Soltau, Ahmad Emami, and Michael Picheny. "Unfolded recurrent neural networks for speech recognition." In Interspeech 2014. ISCA: ISCA, 2014. http://dx.doi.org/10.21437/interspeech.2014-81.

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Mokrý, Ondřej, and Jiří Vitouš. "Unfolded Low-rank + Sparse Reconstruction for MRI." In STUDENT EEICT 2022. Brno: Fakulta elektrotechniky a komunikacnich technologii VUT v Brne, 2022. http://dx.doi.org/10.13164/eeict.2022.271.

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Goyal, Pranav, Satish Mulleti, Anubha Gupta, and Yonina C. Eldar. "DURAS: Deep Unfolded Radar Sensing Using Doppler Focusing." In ICASSP 2021 - 2021 IEEE International Conference on Acoustics, Speech and Signal Processing (ICASSP). IEEE, 2021. http://dx.doi.org/10.1109/icassp39728.2021.9414967.

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Reports on the topic "Unfolded"

1

Clarke, Robert. XBP1, Unfolded Protein Response, and Endocrine Responsiveness. Fort Belvoir, VA: Defense Technical Information Center, May 2009. http://dx.doi.org/10.21236/ada516632.

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Clarke, Robert. XBP1, Unfolded Protein Response, and Endocrine Responsiveness. Fort Belvoir, VA: Defense Technical Information Center, May 2012. http://dx.doi.org/10.21236/ada563383.

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Clarke, Robert. XBP1, Unfolded Protein Response, and Endocrine Responsiveness. Fort Belvoir, VA: Defense Technical Information Center, May 2011. http://dx.doi.org/10.21236/ada550804.

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4

Mitchell, Dean J., Steven M. Horne, Sean O'Brien, and Gregory G. Thoreson. Directional Unfolded Source Term (DUST) for Compton Cameras. Office of Scientific and Technical Information (OSTI), March 2018. http://dx.doi.org/10.2172/1426428.

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McHugh, Colleen A., Ralph F. Tammariello, Charles B. Millard, and John H. Carra. Improved Stability of a Protein Vaccine Through Elimination of a Partially Unfolded State. Fort Belvoir, VA: Defense Technical Information Center, January 2004. http://dx.doi.org/10.21236/ada428734.

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Giacometti, Alberto, and Mari Wøien Meijer. Closed borders and divided communities: status report and lessons from Covid-19 in cross-border areas. Nordregio, March 2021. http://dx.doi.org/10.6027/r2021:6.1403-2503.

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The situation that has unfolded due to the COVID-19 pandemic has exposed the fragility of Nordic co-operation. In this status report, we look at the situation in border communities following the closing of the border, and what this may tell us about the state of Nordic co-operation – Vision 2030 for which includes integration.
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Matita, Mirriam, and Masautso Chimombo. A Multi-Phase Assessment of the Effects of COVID-19 on Food Systems and Rural Livelihoods in Malawi. Institute of Development Studies (IDS), November 2021. http://dx.doi.org/10.19088/apra.2021.035.

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The COVID-19 pandemic has caused disruptions to national and global economies with devastating effects on food systems and livelihoods across the globe. These effects of the pandemic on poverty, hunger, and malnutrition, among others, are likely to be greater among low and middle-income countries like those in sub- Saharan Africa, including Malawi. This is because even before the COVID-19 pandemic began the proportion of people facing poverty, and food and nutrition insecurity were already high. It is, therefore, imperative to understand the effects of COVID-19 on food systems and rural livelihoods. Using a multi-stage ‘rapid assessment’, this study provides real-time insights into how the COVID-19 crisis unfolded in Malawi and how rural people and food and livelihood systems respond.
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Wøien Meijer, Mari, and Alberto Giacometti. Nordic border communities in the time of COVID-19. Nordregio, May 2021. http://dx.doi.org/10.6027/pb2021:3.2001-3876.

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Re-building cross-border collaboration will be vital after the COVID-19 crisis to secure resilient border communities and Nordic collaboration. The measures to limit the spread of the COVID-19 virus were disproportionally damaging for border communities. Healing the wounds inflicted on society, business and institutions demand coordinated actions at local, national, and Nordic levels. This policy brief gives a brief overview of the impact of border restrictions on border communities during the first nine months of the COVID-19 pandemic. The social and economic implications of closed borders have exposed the fragility of Nordic co-operation. The ability of border areas to exist side-by-side in an integrated, seamless way corresponds to the Nordic vision of being the most integrated region in the world, but the situation that unfolded shows a different story.
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Baader, Franz, and Oliver Fernández Gil. Extending the Description Logic τEL(deg) with Acyclic TBoxes. Technische Universität Dresden, 2016. http://dx.doi.org/10.25368/2022.226.

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In a previous paper, we have introduced an extension of the lightweight Description Logic EL that allows us to define concepts in an approximate way. For this purpose, we have defined a graded membership function deg, which for each individual and concept yields a number in the interval [0; 1] expressing the degree to which the individual belongs to the concept. Threshold concepts C~t for ~ 2 ∈ {<, ≤, >, ≥} then collect all the individuals that belong to C with degree ~ t. We have then investigated the complexity of reasoning in the Description Logic τEL(deg), which is obtained from EL by adding such threshold concepts. In the present paper, we extend these results, which were obtained for reasoning without TBoxes, to the case of reasoning w.r.t. acyclic TBoxes. Surprisingly, this is not as easy as might have been expected. On the one hand, one must be quite careful to define acyclic TBoxes such that they still just introduce abbreviations for complex concepts, and thus can be unfolded. On the other hand, it turns out that, in contrast to the case of EL, adding acyclic TBoxes to τEL(deg) increases the complexity of reasoning by at least on level of the polynomial hierarchy.
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Radtke, Gregg. AXIOM Unfold 0.7.0, Users Manual. Office of Scientific and Technical Information (OSTI), September 2021. http://dx.doi.org/10.2172/1821806.

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