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Journal articles on the topic 'Unfolded'

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Author: Grafiati

Published: 10 March 2023

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1

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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2

Ferri, Sabrina. "Unfolded History." New Vico Studies 25 (2007): 87–96. http://dx.doi.org/10.5840/newvico2007257.

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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Fink, Anthony L. "Natively unfolded proteins." Current Opinion in Structural Biology 15, no. 1 (February 2005): 35–41. http://dx.doi.org/10.1016/j.sbi.2005.01.002.

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12

Garg, Pankaj. "Infantile colic — Unfolded." Indian Journal of Pediatrics 71, no. 10 (October 2004): 903–6. http://dx.doi.org/10.1007/bf02830833.

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13

Cao, Stewart Siyan, and Randal J. Kaufman. "Unfolded protein response." Current Biology 22, no. 16 (August 2012): R622—R626. http://dx.doi.org/10.1016/j.cub.2012.07.004.

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14

Liu, Xiaochun, and Richard Luger. "Unfolded GARCH models." Journal of Economic Dynamics and Control 58 (September 2015): 186–217. http://dx.doi.org/10.1016/j.jedc.2015.06.007.

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15

Alcaraz, Luis A., Javier Gómez, Pablo Ramírez, Juan J. Calvente, Rafael Andreu, and Antonio Donaire. "Folding and Unfolding in the Blue Copper Protein Rusticyanin: Role of the Oxidation State." Bioinorganic Chemistry and Applications 2007 (2007): 1–9. http://dx.doi.org/10.1155/2007/54232.

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The unfolding process of the blue copper protein rusticyanin has been studied from the structural and the thermodynamic points of view at two pH values (pH 2.5 and 7.0). When Rc unfolds, copper ion remains bound to the polypeptide chain. Nuclear magnetic resonance data suggest that three of the copper ligands in the folded state are bound to the metal ion in the unfolded form, while the other native ligand is detached. These structural changes are reflected in the redox potentials of the protein in both folded and unfolded forms. The affinities of the copper ion in both redox states have been also determined at the two specified pH values. The results indicate that the presence of two histidine ligands in the folded protein can compensate the change in the net charge that the copper ion receives from their ligands, while, in the unfolded protein, charges of aminoacids are completely transferred to the copper ion, altering decisively the relative stability of its two-redox states.

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16

Hou, Xi-Miao, Wen-Qiang Wu, Xiao-Lei Duan, Na-Nv Liu, Hai-Hong Li, Jing Fu, Shuo-Xing Dou, Ming Li, and Xu-Guang Xi. "Molecular mechanism of G-quadruplex unwinding helicase: sequential and repetitive unfolding of G-quadruplex by Pif1 helicase." Biochemical Journal 466, no. 1 (February 6, 2015): 189–99. http://dx.doi.org/10.1042/bj20140997.

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We revealed that Pif1 repetitively unfolds G-quadruplex (G4) structure in two large steps and the unfolded G4 can be rapidly refolded through an intermediate G-triplex (G3). The repetitive cycling is linked strictly with intrinsic properties of G4–G3 and Pif1.

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17

Webb, Dylan C., Elissa Reynolds, Denise M. Halverson, and Larry L. Howell. "Miura-Ori Inspired Smooth Sheet Attachments for Zipper-Coupled Tubes." Mathematics 10, no. 15 (July 28, 2022): 2643. http://dx.doi.org/10.3390/math10152643.

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Zipper-coupled tubes are a broadly applicable, deployable mechanism with an angular surface that can be smoothed by attaching an additional smooth sheet pattern. The existing design for the smooth sheet attachment, however, leaves small gaps that can only be covered by adding flaps that unfold separately, limiting applicability in situations requiring a seamless surface and simultaneous deployment. We provide a novel construction of the smooth sheet attachment that unfolds simultaneously with zipper-coupled tubes to cover the entire surface without requiring additional actuation and without inhibiting the tubes’ motion up to an ideal, unfolded state of stability. Furthermore, we highlight the mathematics underlying the design and motion of the new smooth sheet pattern, thereby demonstrating its rigid-foldability and compatibility with asymmetric zipper-coupled tubes.

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18

Howell, Stephen H. "When is the unfolded protein response not the unfolded protein response?" Plant Science 260 (July 2017): 139–43. http://dx.doi.org/10.1016/j.plantsci.2017.03.014.

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19

Marston, Steph. "T. Gricoski, Being unfolded." Phenomenological Reviews 7 (2021): 25. http://dx.doi.org/10.19079/pr.7.25.

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20

Vaughan, Adam. "How the drama unfolded." New Scientist 252, no. 3361 (November 2021): 8. http://dx.doi.org/10.1016/s0262-4079(21)02046-7.

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21

Baeissa, Elham. "Lanthanide Ions Unfolded Im9." Journal of King Abdulaziz University-Science 22, no. 1 (2010): 203–21. http://dx.doi.org/10.4197/sci.22-1.14.

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22

Schröder, Martin. "The Unfolded Protein Response." Molecular Biotechnology 34, no. 2 (2006): 279–90. http://dx.doi.org/10.1385/mb:34:2:279.

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23

Liu, C. Y. "The unfolded protein response." Journal of Cell Science 116, no. 10 (May 15, 2003): 1861–62. http://dx.doi.org/10.1242/jcs.00408.

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24

Chawla, Aditi, and Maho Niwa. "The unfolded protein response." Current Biology 15, no. 22 (November 2005): R907. http://dx.doi.org/10.1016/j.cub.2005.11.005.

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25

Chatterjee, Amarnath, Ashutosh Kumar, Jeetender Chugh, Sudha Srivastava, Neel S. Bhavesh, and Ramakrishna V. Hosur. "NMR of unfolded proteins." Journal of Chemical Sciences 117, no. 1 (January 2005): 3–21. http://dx.doi.org/10.1007/bf02704356.

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26

Foroutan, Arash, and Anne Skaja Robinson. "How Unfolded is Tau?" Biophysical Journal 108, no. 2 (January 2015): 62a—63a. http://dx.doi.org/10.1016/j.bpj.2014.11.374.

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27

Li, Qi, Lijie Dong, Fan Sun, Jing Huang, Haian Xie, and Chuanxi Xiong. "Self-Unfolded Graphene Sheets." Chemistry - A European Journal 18, no. 23 (May 8, 2012): 7055–59. http://dx.doi.org/10.1002/chem.201200596.

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28

KAPARULIN, D. S., S. L. LYAKHOVICH, and A. A. SHARAPOV. "ON LAGRANGE STRUCTURE OF UNFOLDED FIELD THEORY." International Journal of Modern Physics A 26, no. 07n08 (March 30, 2011): 1347–62. http://dx.doi.org/10.1142/s0217751x11052840.

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Any local field theory can be equivalently reformulated in the so-called unfolded form. General unfolded equations are non-Lagrangian even though the original theory is Lagrangian. Making use of the unfolded massless scalar field equations as a basic example, the concept of Lagrange anchor is applied to perform a consistent path-integral quantization of unfolded dynamics. It is shown that the unfolded representation for the canonical Lagrange anchor of the d'Alembert equation inevitably involves an infinite number of space–time derivatives.

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29

Tajielyato, Nayere, and Emil Alexov. "Modeling pKas of unfolded proteins to probe structural models of unfolded state." Journal of Theoretical and Computational Chemistry 18, no. 04 (June 2019): 1950020. http://dx.doi.org/10.1142/s0219633619500202.

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Modeling unfolded states of proteins has implications for protein folding and stability. Since in unfolded state proteins adopt multiple conformations, any experimentally measured quantity is ensemble averaged, therefore the computed quantity should be ensemble averaged as well. Here, we investigate the possibility that one can model an unfolded state ensemble with the coil model approach, algorithm such as “flexible-meccano” [Ozenne V et al., Flexible-meccano: A tool for the generation of explicit ensemle descriptions of intrinsically disordered proteins and their associated experimental observables, Bioinformatics 28:1463–1470, 2012], developed to generate structures for intrinsically disordered proteins. We probe such a possibility by using generated structures to calculate pKas of titratable groups and compare with experimental data. It is demonstrated that even with a small number of representative structures of unfolded state, the average calculated pKas are in very good agreement with experimentally measured pKas. Also, predictions are made for titratable groups for which there is no experimental data available. This suggests that the coil model approach is suitable for generating 3D structures of unfolded state of proteins. To make the approach suitable for large-scale modeling, which requires limited number of structures, we ranked the structures according to their solvent accessible surface area (SASA). It is shown that in the majority of cases, the top structures with smallest SASA are enough to represent unfolded state.

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30

Lee, Eun Ryeong, and Kisang Kwon. "Regulation of Unfolded Protein Response by Ethylene Glycol in Rat." Journal of Life Science 23, no. 9 (September 30, 2013): 1104–8. http://dx.doi.org/10.5352/jls.2013.23.9.1104.

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31

Baytshtok, Vladimir, Tania A. Baker, and Robert T. Sauer. "Assaying the kinetics of protein denaturation catalyzed by AAA+ unfolding machines and proteases." Proceedings of the National Academy of Sciences 112, no. 17 (April 13, 2015): 5377–82. http://dx.doi.org/10.1073/pnas.1505881112.

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ATP-dependent molecular machines of the AAA+ superfamily unfold or remodel proteins in all cells. For example, AAA+ ClpX and ClpA hexamers collaborate with the self-compartmentalized ClpP peptidase to unfold and degrade specific proteins in bacteria and some eukaryotic organelles. Although degradation assays are straightforward, robust methods to assay the kinetics of enzyme-catalyzed protein unfolding in the absence of proteolysis have been lacking. Here, we describe a FRET-based assay in which enzymatic unfolding converts a mixture of donor-labeled and acceptor-labeled homodimers into heterodimers. In this assay, ClpX is a more efficient protein-unfolding machine than ClpA both kinetically and in terms of ATP consumed. However, ClpP enhances the mechanical activities of ClpA substantially, and ClpAP degrades the dimeric substrate faster than ClpXP. When ClpXP or ClpAP engage the dimeric subunit, one subunit is actively unfolded and degraded, whereas the other subunit is passively unfolded by loss of its partner and released. This assay should be broadly applicable for studying the mechanisms of AAA+ proteases and remodeling chaperones.

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32

Gardner, B. M., and P. Walter. "Unfolded Proteins Are Ire1-Activating Ligands That Directly Induce the Unfolded Protein Response." Science 333, no. 6051 (August 18, 2011): 1891–94. http://dx.doi.org/10.1126/science.1209126.

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33

VASILIEV, M. A. "ACTIONS, CHARGES AND OFF-SHELL FIELDS IN THE UNFOLDED DYNAMICS APPROACH." International Journal of Geometric Methods in Modern Physics 03, no. 01 (February 2006): 37–80. http://dx.doi.org/10.1142/s0219887806001016.

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Within unfolded dynamics approach, we represent actions and conserved charges as elements of cohomology of the L∞ algebra underlying the unfolded formulation of a given dynamical system. The unfolded off-shell constraints for symmetric fields of all spins in Minkowski space are shown to have the form of zero curvature and covariant constancy conditions for 1-forms and 0-forms taking values in an appropriate star product algebra. Unfolded formulation of Yang–Mills and Einstein equations is presented in a closed form.

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34

Ruan, Linhao, Joshua T. McNamara, Xi Zhang, Alexander Chih-Chieh Chang, Jin Zhu, Yi Dong, Gordon Sun, Amy Peterson, Chan Hyun Na, and Rong Li. "Solid-phase inclusion as a mechanism for regulating unfolded proteins in the mitochondrial matrix." Science Advances 6, no. 32 (August 2020): eabc7288. http://dx.doi.org/10.1126/sciadv.abc7288.

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Proteostasis declines with age, characterized by the accumulation of unfolded or damaged proteins. Recent studies suggest that proteins constituting pathological inclusions in neurodegenerative diseases also enter and accumulate in mitochondria. How unfolded proteins are managed within mitochondria remains unclear. Here, we found that excessive unfolded proteins in the mitochondrial matrix of yeast cells are consolidated into solid-phase inclusions, which we term deposits of unfolded mitochondrial proteins (DUMP). Formation of DUMP occurs in mitochondria near endoplasmic reticulum–mitochondria contact sites and is regulated by mitochondrial proteins controlling the production of cytidine 5′-diphosphate–diacylglycerol. DUMP formation is age dependent but accelerated by exogenous unfolded proteins. Many enzymes of the tricarboxylic acid cycle were enriched in DUMP. During yeast cell division, DUMP formation is necessary for asymmetric inheritance of damaged mitochondrial proteins between mother and daughter cells. We provide evidence that DUMP-like structures may be induced by excessive unfolded proteins in human cells.

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35

Promlek, Thanyarat, Yuki Ishiwata-Kimata, Masahiro Shido, Mitsuru Sakuramoto, Kenji Kohno, and Yukio Kimata. "Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways." Molecular Biology of the Cell 22, no. 18 (September 15, 2011): 3520–32. http://dx.doi.org/10.1091/mbc.e11-04-0295.

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Eukaryotic cells activate the unfolded-protein response (UPR) upon endoplasmic reticulum (ER) stress, where the stress is assumed to be the accumulation of unfolded proteins in the ER. Consistent with previous in vitro studies of the ER-luminal domain of the mutant UPR initiator Ire1, our study show its association with a model unfolded protein in yeast cells. An Ire1 luminal domain mutation that compromises Ire1's unfolded-protein–associating ability weakens its ability to respond to stress stimuli, likely resulting in the accumulation of unfolded proteins in the ER. In contrast, this mutant was activated like wild-type Ire1 by depletion of the membrane lipid component inositol or by deletion of genes involved in lipid homeostasis. Another Ire1 mutant lacking the authentic luminal domain was up-regulated by inositol depletion as strongly as wild-type Ire1. We therefore conclude that the cytosolic (or transmembrane) domain of Ire1 senses membrane aberrancy, while, as proposed previously, unfolded proteins accumulating in the ER interact with and activate Ire1.

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36

Peran, Ivan, Alex S. Holehouse, Isaac S. Carrico, Rohit V. Pappu, Osman Bilsel, and Daniel P. Raleigh. "Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions." Proceedings of the National Academy of Sciences 116, no. 25 (June 5, 2019): 12301–10. http://dx.doi.org/10.1073/pnas.1818206116.

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Proteins are marginally stable molecules that fluctuate between folded and unfolded states. Here, we provide a high-resolution description of unfolded states under refolding conditions for the N-terminal domain of the L9 protein (NTL9). We use a combination of time-resolved Förster resonance energy transfer (FRET) based on multiple pairs of minimally perturbing labels, time-resolved small-angle X-ray scattering (SAXS), all-atom simulations, and polymer theory. Upon dilution from high denaturant, the unfolded state undergoes rapid contraction. Although this contraction occurs before the folding transition, the unfolded state remains considerably more expanded than the folded state and accommodates a range of local and nonlocal contacts, including secondary structures and native and nonnative interactions. Paradoxically, despite discernible sequence-specific conformational preferences, the ensemble-averaged properties of unfolded states are consistent with those of canonical random coils, namely polymers in indifferent (theta) solvents. These findings are concordant with theoretical predictions based on coarse-grained models and inferences drawn from single-molecule experiments regarding the sequence-specific scaling behavior of unfolded proteins under folding conditions.

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37

GOENKA, Shradha, Bakthisaran RAMAN, Tangirala RAMAKRISHNA, and Ch Mohan RAO. "Unfolding and refolding of a quinone oxidoreductase: α-crystallin, a molecular chaperone, assists its reactivation." Biochemical Journal 359, no. 3 (October 25, 2001): 547–56. http://dx.doi.org/10.1042/bj3590547.

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α-Crystallin, a member of the small heat-shock protein family and present in vertebrate eye lens, is known to prevent the aggregation of other proteins under conditions of stress. However, its role in the reactivation of enzymes from their non-native inactive states has not been clearly demonstrated. We have studied the effect of α-crystallin on the refolding of ∊-crystallin, a quinone oxidoreductase, from its different urea-denatured states. Co-refolding ∊-crystallin from its denatured state in 2.5M urea with either calf eye lens α-crystallin or recombinant human αB-crystallin could significantly enhance its reactivation yield. αB-crystallin was found to be more efficient than αA-crystallin in chaperoning the refolding of ∊-crystallin. In order to understand the nature of the denatured state(s) of ∊-crystallin that can interact with α-crystallin, we have investigated the unfolding pathway of ∊-crystallin. We find that it unfolds through three distinct intermediates: an altered tetramer, a partially unfolded dimer, which is competent to fold back to its active state, and a partially unfolded monomer. The partially unfolded monomer is inactive, exhibits highly exposed hydrophobic surfaces and has significant secondary structural elements with little or no tertiary structure. This intermediate does not refold into the active state without assistance. α-Crystallin provides the required assistance and improves the reactivation yield several-fold.

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38

Del Galdo, Sara, and Andrea Amadei. "The unfolding effects on the protein hydration shell and partial molar volume: a computational study." Physical Chemistry Chemical Physics 18, no. 40 (2016): 28175–82. http://dx.doi.org/10.1039/c6cp05029h.

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In this paper we apply the computational analysis recently proposed by our group to characterize the solvation properties of a native protein in aqueous solution, and to four model aqueous solutions of globular proteins in their unfolded states thus characterizing the protein unfolded state hydration shell and quantitatively evaluating the protein unfolded state partial molar volumes.

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39

Davenport, Emma L., Gareth J. Morgan, and Faith E. Davies. "Untangling the unfolded protein response." Cell Cycle 7, no. 7 (April 2008): 865–69. http://dx.doi.org/10.4161/cc.7.7.5615.

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40

Nishikawa, Ken. "Natively unfolded proteins: An overview." BIOPHYSICS 5 (2009): 53–58. http://dx.doi.org/10.2142/biophysics.5.53.

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41

Uversky, Vladimir. "Amyloidogenesis of Natively Unfolded Proteins." Current Alzheimer Research 5, no. 3 (June 1, 2008): 260–87. http://dx.doi.org/10.2174/156720508784533312.

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42

OHNISHI, Satoshi. "Do Unfolded Polypeptides Have Structures?" Seibutsu Butsuri 49, no. 1 (2009): 017–19. http://dx.doi.org/10.2142/biophys.49.017.

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43

Schröder, Martin, and Randal J. Kaufman. "THE MAMMALIAN UNFOLDED PROTEIN RESPONSE." Annual Review of Biochemistry 74, no. 1 (June 2005): 739–89. http://dx.doi.org/10.1146/annurev.biochem.73.011303.074134.

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44

ARBUZOVA, Anna, Arndt A. P. SCHMITZ, and Guy VERGÈRES. "Cross-talk unfolded: MARCKS proteins." Biochemical Journal 362, no. 1 (February 15, 2002): 1. http://dx.doi.org/10.1042/0264-6021:3620001.

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45

ARBUZOVA, Anna, Arndt A. P. SCHMITZ, and Guy VERGÈRES. "Cross-talk unfolded: MARCKS proteins." Biochemical Journal 362, no. 1 (February 8, 2002): 1–12. http://dx.doi.org/10.1042/bj3620001.

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The proteins of the MARCKS (myristoylated alanine-rich C kinase substrate) family were first identified as prominent substrates of protein kinase C (PKC). Since then, these proteins have been implicated in the regulation of brain development and postnatal survival, cellular migration and adhesion, as well as endo-, exo- and phago-cytosis, and neurosecretion. The effector domain of MARCKS proteins is phosphorylated by PKC, binds to calmodulin and contributes to membrane binding. This multitude of mutually exclusive interactions allows cross-talk between the signal transduction pathways involving PKC and calmodulin. This review focuses on recent, mostly biophysical and biochemical results renewing interest in this protein family. MARCKS membrane binding is now understood at the molecular level. From a structural point of view, there is a consensus emerging that MARCKS proteins are ‘natively unfolded'. Interestingly, domains similar to the effector domain have been discovered in other proteins. Furthermore, since the effector domain enhances the polymerization of actin in vitro, MARCKS proteins have been proposed to mediate regulation of the actin cytoskeleton. However, the recent observations that MARCKS might serve to sequester phosphatidylinositol 4,5-bisphosphate in the plasma membrane of unstimulated cells suggest an alternative model for the control of the actin cytoskeleton. While myristoylation is classically considered to be a co-translational, irreversible event, new reports on MARCKS proteins suggest a more dynamic picture of this protein modification. Finally, studies with mice lacking MARCKS proteins have investigated the functions of these proteins during embryonic development in the intact organism.

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46

Rax, J. M., and J. Robiche. "Theory of unfolded cyclotron accelerator." Physics of Plasmas 17, no. 10 (October 2010): 103112. http://dx.doi.org/10.1063/1.3498677.

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47

Khamsi, Roxanne. "Q&A: Origami unfolded." Nature 459, no. 7244 (May 2009): 169. http://dx.doi.org/10.1038/459169a.

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48

Wek, Ronald C., and Tracy G. Anthony. "Obesity: stressing about unfolded proteins." Nature Medicine 16, no. 4 (April 2010): 374–76. http://dx.doi.org/10.1038/nm0410-374.

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49

Larner, Stephen F., Ronald L. Hayes, and Kevin K. W. Wang. "Unfolded Protein Response after Neurotrauma." Journal of Neurotrauma 23, no. 6 (June 2006): 807–29. http://dx.doi.org/10.1089/neu.2006.23.807.

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50

Plaxco, Kevin W., and Michael Groβ. "The importance of being unfolded." Nature 386, no. 6626 (April 1997): 657–59. http://dx.doi.org/10.1038/386657a0.

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