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Статті в журналах з теми "Conformational constraint"

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Автор: Grafiati
Опубліковано: 10 грудня 2022
Оновлено: 28 січня 2023

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1

Campeotto, F., A. Dal Palù, A. Dovier, F. Fioretto, and E. Pontelli. "A Constraint Solver for Flexible Protein Model." Journal of Artificial Intelligence Research 48 (December 30, 2013): 953–1000. http://dx.doi.org/10.1613/jair.4193.

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Анотація:
This paper proposes the formalization and implementation of a novel class of constraints aimed at modeling problems related to placement of multi-body systems in the 3-dimensional space. Each multi-body is a system composed of body elements, connected by joint relationships and constrained by geometric properties. The emphasis of this investigation is the use of multi-body systems to model native conformations of protein structures---where each body represents an entity of the protein (e.g., an amino acid, a small peptide) and the geometric constraints are related to the spatial properties of the composing atoms. The paper explores the use of the proposed class of constraints to support a variety of different structural analysis of proteins, such as loop modeling and structure prediction. The declarative nature of a constraint-based encoding provides elaboration tolerance and the ability to make use of any additional knowledge in the analysis studies. The filtering capabilities of the proposed constraints also allow to control the number of representative solutions that are withdrawn from the conformational space of the protein, by means of criteria driven by uniform distribution sampling principles. In this scenario it is possible to select the desired degree of precision and/or number of solutions. The filtering component automatically excludes configurations that violate the spatial and geometric properties of the composing multi-body system. The paper illustrates the implementation of a constraint solver based on the multi-body perspective and its empirical evaluation on protein structure analysis problems.
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2

ÖTVÖS, FERENC L., DMITRY S. GEMBITSKY, RICHARD F. MURPHY, and SÁNDOR LOVAS. "38 NKA, analogs with conformational constraint." Biochemical Society Transactions 26, no. 1 (February 1, 1998): S30. http://dx.doi.org/10.1042/bst026s030.

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3

Arttamangkul, Seksiri, Thomas F. Murray, Gary E. DeLander, and Jane V. Aldrich. "Synthesis and Opioid Activity of Conformationally Constrained Dynorphin A Analogs. 1. Conformational Constraint in the "Message" Sequence." Journal of Medicinal Chemistry 38, no. 13 (June 1995): 2410–17. http://dx.doi.org/10.1021/jm00013a016.

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4

Anthony, Peter C., Adelene Y. L. Sim, Vincent B. Chu, Sebastian Doniach, Steven M. Block, and Daniel Herschlag. "Electrostatics of Nucleic Acid Folding under Conformational Constraint." Journal of the American Chemical Society 134, no. 10 (February 27, 2012): 4607–14. http://dx.doi.org/10.1021/ja208466h.

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5

Capozzi, Maria Annunziata M., Claudia Pigliacelli, Giancarlo Terraneo, and Cosimo Cardellicchio. "Stacked aryl groups in P-resolved cyclic phosphonamides as a new conformational constraint." CrystEngComm 21, no. 47 (2019): 7224–32. http://dx.doi.org/10.1039/c9ce01382b.

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6

Wang, L. Y., Q. L. Deng, L. H. Lai, Y. Z. Han, and X. J. Xu. "Constraint peptide conformational analysis by Monte Carlo simulated annealing." Acta Crystallographica Section A Foundations of Crystallography 49, s1 (August 21, 1993): c152. http://dx.doi.org/10.1107/s0108767378095641.

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7

Liu, Hao-Miao, Dong Chen, Wen-Dan Xu, Li-Zhi Dang, and Hong-Bo Qin. "Total synthesis of (−)-akaol A via a conformational constraint strategy." Organic Chemistry Frontiers 5, no. 12 (2018): 1886–89. http://dx.doi.org/10.1039/c8qo00375k.

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8

Blount, Kenneth F., Fang Zhao, Thomas Hermann, and Yitzhak Tor. "Conformational Constraint as a Means for Understanding RNA-Aminoglycoside Specificity." Journal of the American Chemical Society 127, no. 27 (July 2005): 9818–29. http://dx.doi.org/10.1021/ja050918w.

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9

Fnu, Gulimirerouzi, Palak Agrawal, Gopal C. Kundu, and Georg F. Weber. "Structural Constraint of Osteopontin Facilitates Efficient Binding to CD44." Biomolecules 11, no. 6 (May 30, 2021): 813. http://dx.doi.org/10.3390/biom11060813.

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Анотація:
Since the original description in 1996, the interaction between the cytokine osteopontin (OPN) and the homing receptor CD44 has been extensively studied in cancer, inflammation, bone remodeling, and various other conditions. Alternative splicing and extensive posttranslational modifications by both binding partners, as well as the possibility for lateral recruitment of additional membrane receptors or soluble co-ligands into a complex have left the exact molecular requirements for high-affinity OPN-CD44 binding unresolved. We now report that there is a moderate engagement between the unmodified molecules, which results in curved double-reciprocal plots for OPN titration, suggesting the existence of two binding sites or two binding conformations. Structural constraint of OPN, by immobilization or by addition of heparin, is required for its strong ligation of CD44. Prior literature provides evidence that heparin binding to OPN prompts the unfolding of a core element in the protein. This conformational adjustment may be essential for efficient CD44 interaction. The integrin α9β1 seems to compete with the OPN-CD44 engagement, while the integrin αVβ3 reflects additive binding, suggesting that the CD44 contact sites on OPN are downstream of the RGD motif but overlap with the SVVYGLR domain. Hyaluronate has no effect, placing the relevant domain on CD44 downstream of the N-terminus.
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10

Smith, Jason G., Walther Mothes, Stephen C. Blacklow, and James M. Cunningham. "The Mature Avian Leukosis Virus Subgroup A Envelope Glycoprotein Is Metastable, and Refolding Induced by the Synergistic Effects of Receptor Binding and Low pH Is Coupled to Infection." Journal of Virology 78, no. 3 (February 1, 2004): 1403–10. http://dx.doi.org/10.1128/jvi.78.3.1403-1410.2004.

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ABSTRACT The spring-loaded model stipulates that influenza virus infection is coupled to the transition of the virus hemagglutinin (HA) from a metastable conformation to a highly stable conformation at low pH. The properties of retrovirus envelope glycoproteins indicate that infection is coupled to an analogous conformational change. As a test of this hypothesis, the requirements for avian leukosis virus A (ALV-A) infection were examined. These studies indicate that, like HA, the conformation of the mature ALV-A envelope glycoprotein is metastable and that infection is linked to refolding at low pH. However, unlike HA, low-pH activation is only observed after priming by receptor. Therefore, ALV-A infection is dependent on the synergistic effects of receptor binding and low pH, suggesting that receptor binding superimposes an additional constraint on activation of ALV-A fusion that proceeds by a mechanism comparable to that of influenza virus.
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11

Lu-Hua, Lai, Wang Le-Yu, Deng Qiao-Lin, Han Yu-Zhen, Ma Li-Bin, Xu Xiao-Jie, and Tang You-Qi. "Constraint Monte-Carlo Simulated Annealing:Application in Peptide Conformational Analysis in Solution." Acta Physico-Chimica Sinica 10, no. 10 (1994): 867–69. http://dx.doi.org/10.3866/pku.whxb19941001.

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12

Mishra, Pramod Kumar. "Effect of geometrical constraint on conformational properties of a polymer chain." Phase Transitions 84, no. 3 (March 2011): 291–98. http://dx.doi.org/10.1080/01411594.2010.534657.

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13

Gilon, Chaim, David Halle, Michael Chorev, Zvi Selincer, and Gerardo Byk. "Backbone cyclization: A new method for conferring conformational constraint on peptides." Biopolymers 31, no. 6 (May 1991): 745–50. http://dx.doi.org/10.1002/bip.360310619.

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14

Wang, Hongshuang, Robert S. Dawber, Peiyu Zhang, Martin Walko, Andrew J. Wilson, and Xiaohui Wang. "Peptide-based inhibitors of protein–protein interactions: biophysical, structural and cellular consequences of introducing a constraint." Chemical Science 12, no. 17 (2021): 5977–93. http://dx.doi.org/10.1039/d1sc00165e.

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15

Humphries, M. J. "Monoclonal antibodies as probes of integrin priming and activation." Biochemical Society Transactions 32, no. 3 (June 1, 2004): 407–11. http://dx.doi.org/10.1042/bst0320407.

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Анотація:
Integrins are a family of heterodimeric, transmembrane receptors that mediate a range of cell–cell and cell–extracellular matrix interactions in an array of physiological and pathophysiological situations. Integrin-mediated cell adhesion is dynamically regulated in vivo to facilitate cell anchorage and movement, but prevents aberrant trafficking and aggregation. Following ligand engagement, integrin signalling imposes a spatial constraint on the assembly of signalling complexes and controls the transduction of mechanical force to the cytoskeleton. This transmembrane passage of signals via integrins is achieved both by clustering of receptors, which makes the ligand and effector engagement more favourable kinetically, and by induction of conformational changes, that theoretically creates ligand and effector binding sites de novo. Clustering and conformational changes can be triggered both from the inside of the cell (resulting in acquisition of ligand-competent conformers) and from the outside (ligand-induced signalling). In this paper, these processes will be described and distinguished by the terms priming and activation, respectively. Although both clustering and conformation are important for integrin function, the latter will be the main focus of this article; in particular, the importance of monoclonal antibodies for the study of integrin shape changes.
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16

Udugamasooriya, D. Gomika, and Mark R. Spaller. "Conformational constraint in protein ligand design and the inconsistency of binding entropy." Biopolymers 89, no. 8 (August 2008): 653–67. http://dx.doi.org/10.1002/bip.20983.

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17

Lee, Ji Hyang, Hae Sook Park та Young Kee Kang. "Conformational preferences of β-sheet structures in cyclopropane-containing γ-peptides". New Journal of Chemistry 39, № 6 (2015): 4640–46. http://dx.doi.org/10.1039/c5nj00545k.

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Анотація:
Oligo-γ-peptides based on 2-(aminomethyl)cyclopropanecarboxylic acid (γAmc3) with a cyclopropane constraint on the Cα–Cβ bond preferentially formed parallel β-sheets rather than antiparallel β-sheets due to the stronger N–H⋯O H-bonds in the parallel conformation.
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18

Hills, Ivory D., M. Katharine Holloway, Pablo de León, Ashley Nomland, Hong Zhu, Hemaka Rajapakse, Tim J. Allison та ін. "A conformational constraint improves a β-secretase inhibitor but for an unexpected reason". Bioorganic & Medicinal Chemistry Letters 19, № 17 (вересень 2009): 4993–95. http://dx.doi.org/10.1016/j.bmcl.2009.07.071.

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19

Farrell, Daniel W., Tatyana Mamonova, Maria Kurnikova, and Michael F. Thorpe. "Generating Pathways for Free Energy Calculations in Proteins Using Constraint-Based Conformational Sampling." Biophysical Journal 96, no. 3 (February 2009): 407a. http://dx.doi.org/10.1016/j.bpj.2008.12.2072.

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20

Tuthill, Paul A., Pamela R. Seida, William Barker, Joel A. Cassel, Serge Belanger, Robert N. DeHaven, Michael Koblish та ін. "Azepinone as a conformational constraint in the design of κ-opioid receptor agonists". Bioorganic & Medicinal Chemistry Letters 14, № 22 (листопад 2004): 5693–97. http://dx.doi.org/10.1016/j.bmcl.2004.08.041.

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21

Kukol, Andreas. "Site‒specific IR spectroscopy and molecular modelling combined towards solving transmembrane protein structure." Spectroscopy 19, no. 1 (2005): 1–16. http://dx.doi.org/10.1155/2005/297098.

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Membrane protein structures are underrepresented in structural databases despite their abundance and biomedical importance. This review focuses on the novel method of site-specific infrared dichroism (SSID) combined with constraint molecular dynamics simulation, which has recently emerged as a powerful method to obtain structures of transmembrane α-helical bundles. The theory of SSID including its latest developments is reviewed with the aim to encourage widespread application of this method. This is followed by an outline of the conformational search using experimentally constraint molecular dynamics simulations. Finally a critical evaluation of recent applications, namely the Influenza M2 proton channel, the vpu ion channel of HIV-1 and the MHC-class II associated invariant chain, is conducted.
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22

KODAMA, Hiroaki, and Yasuyuki SHIMOHIGASHI. "Synthesis of Cyclopropane Amino Acids and Their Incorporation into Bioactive Peptides as Conformational Constraint." Journal of Synthetic Organic Chemistry, Japan 52, no. 3 (1994): 180–91. http://dx.doi.org/10.5059/yukigoseikyokaishi.52.180.

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23

Davies, John S., Malgosia Stelmach-Diddams, Regis Fromentin, Alun Howells та Ron Cotton. "The synthesis and conformational aspects of a novel dioxopiperazine—a possible β-turn constraint". Journal of the Chemical Society, Perkin Transactions 1, № 2 (2000): 239–43. http://dx.doi.org/10.1039/a904943f.

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24

Jung, Sejin, Asuka Inoue, Sho Nakamura, Takayuki Kishi, Akiharu Uwamizu, Misa Sayama, Masaya Ikubo, et al. "Conformational Constraint of the Glycerol Moiety of Lysophosphatidylserine Affords Compounds with Receptor Subtype Selectivity." Journal of Medicinal Chemistry 59, no. 8 (April 14, 2016): 3750–76. http://dx.doi.org/10.1021/acs.jmedchem.5b01925.

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25

Kemp, D. S., and Jeffrey H. Rothman. "Synthesis and analysis of a macrocyclic triproline-derived template containing a local conformational constraint." Tetrahedron Letters 36, no. 23 (June 1995): 4019–22. http://dx.doi.org/10.1016/0040-4039(95)00706-i.

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26

Zhu, Peng-Wei, and Luguang Chen. "Conformational collapse of spherical poly(N-isopropylacrylamide) brushes under the constraint of bound micelles." Physical Chemistry Chemical Physics 19, no. 46 (2017): 31362–76. http://dx.doi.org/10.1039/c7cp06406c.

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27

ZHANG, MING, LIQUN WANG, and RONALD GOLDMAN. "BÉZIER SUBDIVISION FOR INVERSE MOLECULAR KINEMATICS." International Journal of Computational Geometry & Applications 16, no. 05n06 (December 2006): 513–32. http://dx.doi.org/10.1142/s0218195906002166.

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Conformational searching is a core task in inverse molecular kinematics. Algorithmic improvements affecting either the speed or quality of conformational searching will have a profound impact on applications including ligand-receptor docking, ab initio prediction of protein structure, and protein folding. In this paper, we investigate a specific geometry-constrained conformational searching problem, where some feature atoms have pre-specified target positions. Using Bézier subdivision, we present a method to locate and approximate the solutions of the equations derived from constraints on the feature atoms. The conformations corresponding to these solutions are all the conformations satisfying the target constraints. Three implementations of the subdivision method taking advantage of the sparsity of the coefficients of the polynomial equations are presented and the results are compared and contrasted.
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28

Borics, Attila, Katarzyna Gach, Jakub Fichna, Dariusz Sobolewski, Géza Toth, and Anna Janecka. "Structural comparison of endomorphin-2 and its conformationally restricted analog." Open Chemistry 10, no. 1 (February 1, 2012): 172–79. http://dx.doi.org/10.2478/s11532-011-0119-2.

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AbstractIn the present study, the effect of a conformational constraint introduced into the endomorphin-2 (Tyr-Pro-Phe-Phe-NH2, EM-2) structure was studied using computational analysis and radioligand binding assay. EM-2 was modified by connecting nitrogen atoms of both phenylalanine residues by a methylene bridge. The obtained analog did not bind to the µ- or δ-opioid receptors in the in vitro studies. The computational analysis of this analog showed twisted, type IV turns and the absence of canonical β-turns typical for the EM-2 structure, which can be explained by the lack of hydrogen bonds involving Phe4. Our results show that the introduction of chemical constraint in the EM-2 structure has a significant effect on opioid receptor affinity and in vitro bioactivity.
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29

Mandal, Mihirbaran, Zhaoning Zhu, Jared N. Cumming, Xiaoxiang Liu, Corey Strickland, Robert D. Mazzola, John P. Caldwell, et al. "Design and Validation of Bicyclic Iminopyrimidinones As Beta Amyloid Cleaving Enzyme-1 (BACE1) Inhibitors: Conformational Constraint to Favor a Bioactive Conformation." Journal of Medicinal Chemistry 55, no. 21 (October 2012): 9331–45. http://dx.doi.org/10.1021/jm301039c.

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30

Fairlie, David P., Giovanni Abbenante, and Darren R. March. "Macrocyclic Peptidomimetics Forcing Peptides into Bioactive Conformations." Current Medicinal Chemistry 2, no. 2 (August 1995): 654–86. http://dx.doi.org/10.2174/0929867302666220218001506.

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Abstract: Cyclic peptides that are potent regulators of biological processes are rapidly emerging as important mechanistic probes and drug leads. Nature clearly uses macrocycles to. constrain peptides into conformations that can selectively bind proteins or. small molecules. Therapeutic effects of such macrocycles, often containing additional conformational constraints that fine­ tune structure (e.g. D-amino acids, N-methyl substituents, aromatic rings, to name a few), have so far been mainly discovered by accident. However it is now becoming possible to rationally design synthetic macrocycles to selectively recognize and inhibit a specific protein. A receptor-binding struc­ ture is more easily adopted by macrocyclic peptidomimetics than more flexible acyclic peptides because the former have less conformational entropy. Macrocycles are often stable to hydrolysis by peptidases that degrade acyclic peptides and hydrophobic side chains can protect peptide bonds in macrocycles from hydrolysis, as well as enhance lipophilicity, cell permeability and bioavailability. Synthetic efforts to obtain bioactive conformations of short peptides have so far been substrate-based, guided by molecular modelling predictions and structure-activity data for modified amino acid sequences of substrates. However, dramatic advances in molecular biology, X-ray crystallography, NMR spectroscopy and computing are rapidly producing three dimensional structures of proteins, promising direct observation of protein-bound conformations of small molecules and receptor-based design of peptidomimetics with surface complementarity for proteins. This perspective review highlights examples of both natural and synthetic bioactive macrocyclic peptides containing constraints that fix conformation, and briefly illustrates the promise that receptor-based design holds for structural and functional mimicry of peptides by macrocycles.
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31

Jackler, G., A. Wittemann, M. Ballauff, and C. Czeslik. "Spherical polyelectrolyte brushes as carrier particles for proteins: An investigation of the structure of adsorbed and desorbed bovine serum albumin." Spectroscopy 18, no. 2 (2004): 289–99. http://dx.doi.org/10.1155/2004/526159.

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The change in the secondary and tertiary structure of bovine serum albumin (BSA) induced by the interaction with spherical polyelectrolyte brushes (SPB) has been investigated using fluorescence and circular dichroism (CD) spectroscopy. The SPB consist of poly(acrylic acid) chains grafted to a poly(styrene) core. The colloidal SPB represent a new substrate for protein immobilization because their protein binding capacity can be controlled by the ionic strength of the solution: SPB bind large amounts of BSA at low ionic strength (pH=6.1), but they are largely protein resistant at moderate salt concentrations of 500 mM. The conformation of BSA which was labeled with the environmentally sensitive dansyl fluorophore was studied before adsorption to the SPB, in the adsorbed state, and after desorption from the SPB. In the adsorbed state the obtained fluorescence spectrum is red-shifted which indicates a hydration of the dansyl fluorophores due to a distortion of the tertiary structure of BSA. Fluorescence and CD spectroscopic analysis of BSA that was desorbed from the SPB shows that the adsorption-induced conformational changes are largely reversible. Convex constraint analysis of the observed CD spectra of BSA yield α-helix fractions of 68% and 57% before adsorption to and after desorption from the SPB, respectively. In a general view, the results of this study demonstrate that spherical polyelectrolyte brushes are suitable for a controlled immobilization and release of proteins without major conformational changes.
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32

Corr, Michael J., Rodrigo A. Cormanich, Cortney N. von Hahmann, Michael Bühl, David B. Cordes, Alexandra M. Z. Slawin, and David O'Hagan. "Fluorine in fragrances: exploring the difluoromethylene (CF2) group as a conformational constraint in macrocyclic musk lactones." Organic & Biomolecular Chemistry 14, no. 1 (2016): 211–19. http://dx.doi.org/10.1039/c5ob02023a.

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33

Liu, Yinghui, Chun Wan, Shailendra S. Rathore, Michael H. B. Stowell, Haijia Yu, and Jingshi Shen. "SNARE Zippering Is Suppressed by a Conformational Constraint that Is Removed by v-SNARE Splitting." Cell Reports 34, no. 2 (January 2021): 108611. http://dx.doi.org/10.1016/j.celrep.2020.108611.

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34

Yanagihara, Ryoji, Masaki Katoh, Masayuki Hanyuu, Toshifumi Miyazawa та Takashi Yamada. "Recognition of quaternary ammonium salts with tetrapeptides containing α-aminoisobutyric acid as a conformational constraint". Journal of the Chemical Society, Perkin Transactions 2, № 3 (2000): 551–56. http://dx.doi.org/10.1039/a906439g.

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35

Meyer, Falco-Magnus, James C. Collins, Brendan Borin, James Bradow, Spiros Liras, Chris Limberakis, Alan M. Mathiowetz, et al. "Biaryl-Bridged Macrocyclic Peptides: Conformational Constraint via Carbogenic Fusion of Natural Amino Acid Side Chains." Journal of Organic Chemistry 77, no. 7 (March 13, 2012): 3099–114. http://dx.doi.org/10.1021/jo202105v.

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36

Renslo, Adam R., Priyadarshini Jaishankar, Revathy Venkatachalam, Corinne Hackbarth, Sara Lopez, Dinesh V. Patel, and Mikhail F. Gordeev. "Conformational Constraint in Oxazolidinone Antibacterials. Synthesis and Structure−Activity Studies of (Azabicyclo[3.1.0]hexylphenyl)oxazolidinones." Journal of Medicinal Chemistry 48, no. 15 (July 2005): 5009–24. http://dx.doi.org/10.1021/jm058204j.

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37

Schütznerová, Eva, Allen G. Oliver, Greg A. Slough, and Viktor Krchňák. "Traceless Solid-Phase Synthesis of Fused Chiral Macrocycles via Conformational Constraint-Assisted Cyclic Iminium Formation." Chemistry - A European Journal 23, no. 52 (August 16, 2017): 12876–85. http://dx.doi.org/10.1002/chem.201702461.

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38

Megalathan, Anoja, Bobby D. Cox, Peter D. Wilkerson, Anisa Kaur, Kumar Sapkota, Joseph E. Reiner, and Soma Dhakal. "Single-molecule analysis of i-motif within self-assembled DNA duplexes and nanocircles." Nucleic Acids Research 47, no. 14 (July 9, 2019): 7199–212. http://dx.doi.org/10.1093/nar/gkz565.

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Анотація:
Abstract The cytosine (C)-rich sequences that can fold into tetraplex structures known as i-motif are prevalent in genomic DNA. Recent studies of i-motif–forming sequences have shown increasing evidence of their roles in gene regulation. However, most of these studies have been performed in short single-stranded oligonucleotides, far from the intracellular environment. In cells, i-motif–forming sequences are flanked by DNA duplexes and packed in the genome. Therefore, exploring the conformational dynamics and kinetics of i-motif under such topologically constrained environments is highly relevant in predicting their biological roles. Using single-molecule fluorescence analysis of self-assembled DNA duplexes and nanocircles, we show that the topological environments play a key role on i-motif stability and dynamics. While the human telomere sequence (C3TAA)3C3 assumes i-motif structure at pH 5.5 regardless of topological constraint, it undergoes conformational dynamics among unfolded, partially folded and fully folded states at pH 6.5. The lifetimes of i-motif and the partially folded state at pH 6.5 were determined to be 6 ± 2 and 31 ± 11 s, respectively. Consistent with the partially folded state observed in fluorescence analysis, interrogation of current versus time traces obtained from nanopore analysis at pH 6.5 shows long-lived shallow blockades with a mean lifetime of 25 ± 6 s. Such lifetimes are sufficient for the i-motif and partially folded states to interact with proteins to modulate cellular processes.
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39

Long, Ya-Qiu, Feng-Di T. Lung, and Peter P. Roller. "Global optimization of conformational constraint on non-phosphorylated cyclic peptide antagonists of the Grb2-SH2 domain." Bioorganic & Medicinal Chemistry 11, no. 18 (September 2003): 3929–36. http://dx.doi.org/10.1016/s0968-0896(03)00411-5.

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40

KODAMA, H., and Y. SHIMOHIGASHI. "ChemInform Abstract: Synthesis of Cyclopropane Amino Acids and Their Incorporation into Bioactive Peptides as Conformational Constraint." ChemInform 25, no. 30 (August 19, 2010): no. http://dx.doi.org/10.1002/chin.199430290.

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41

Dinsmore, Christopher J., and Ian M. Bell. "Inhibitors of Farnesyltransferase and Geranylgeranyltransferase-I for Antitumor Therapy: Substrate-Based Design, Conformational Constraint and Biological Activity." Frontiers in Medicinal Chemistry - Online 2, no. 1 (January 1, 2005): 331–55. http://dx.doi.org/10.2174/1567204052931023.

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42

Dinsmore, Christopher, and Ian Bell. "Inhibitors of Farnesyltransferase and Geranylgeranyltransferase-I for Antitumor Therapy: Substrate-Based Design, Conformational Constraint and Biological Activity." Current Topics in Medicinal Chemistry 3, no. 10 (May 1, 2003): 1075–93. http://dx.doi.org/10.2174/1568026033452113.

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43

Ely, Fernando, Rodrigo Cristiano, Ricardo L. Longo, Rafael Vergara‐Toloza, Eduardo Soto‐Bustamante, and Hugo Gallardo. "Conformational constraint in ferroelectric liquid crystals incorporating a pyrrolidine‐type ring: FLC materials comprising parallel dipolar moments." Liquid Crystals 34, no. 4 (April 2007): 431–40. http://dx.doi.org/10.1080/02678290601171642.

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44

Askarian, Mohammad, Reza Hasanzadeh Ghasemi та Majid Moavenian. "Investigating conformational changes of Prefoldin β1 as result of applying external mechanical force without any position constraint". IET Nanobiotechnology 14, № 6 (15 липня 2020): 491–500. http://dx.doi.org/10.1049/iet-nbt.2019.0265.

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45

Ho, Jason, Kelly S. MacDonald, and Brian H. Barber. "Construction of recombinant targeting immunogens incorporating an HIV-1 neutralizing epitope into sites of differing conformational constraint." Vaccine 20, no. 7-8 (January 2002): 1169–80. http://dx.doi.org/10.1016/s0264-410x(01)00441-8.

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46

Davies, John S., Malgosia Stelmach-Diddams, Regis Fromentin, Alun Howells та Ron Cotton. "ChemInform Abstract: The Synthesis and Conformational Aspects of a Novel Dioxopiperazine (VIII) - A Possible β-Turn Constraint." ChemInform 31, № 19 (8 червня 2010): no. http://dx.doi.org/10.1002/chin.200019133.

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47

KEMP, D. S., and J. H. ROTHMAN. "ChemInform Abstract: Synthesis and Analysis of a Macrocyclic Triproline-Derived Template (I) Containing a Local Conformational Constraint." ChemInform 26, no. 43 (August 17, 2010): no. http://dx.doi.org/10.1002/chin.199543231.

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48

Healy, Judith M., Mitsuru Haruki, and Masakazu Kikuchi. "Preferred Motif for Integrin Binding Identified Using a Library of Randomized RGD Peptides Displayed on Phage." Protein & Peptide Letters 3, no. 1 (February 1996): 23–30. http://dx.doi.org/10.2174/092986650301220608153153.

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Abstract: We have selected RGD peptides recognized efficiently by integrin av3 through randomization of amino acids flanking the RGD motif. Degenerate RGD peptides were displayed on phage as fusions to the N-terminus of major coat protein Vill of M13 using a specially constructed phagemid vector. Identification of an apparent consensus sequence among ligands preferred by av3 supports the view that amino acids in the vicinity of RGD can influence receptor recognition of phage-peptides. In addition, several phage isolates encoded a potentially cyclic peptide which bound to av3 with superior affinity. Binding assays with cyclic and linear forms of synthetic RGD peptides confirmed the capacity of conformational constraint of RGD to confer high-affinity integrin binding.
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49

Gómez-Monterrey, Isabel, Rosario González-Muñiz, Rosario Herranz, and M. a. Teresa Garcia-Gomez. "Stereospecific synthesis of (2R,3S)-3-amino-2-piperidineacetic acid derivatives for use as conformational constraint in peptides." Tetrahedron Letters 34, no. 22 (May 1993): 3593–94. http://dx.doi.org/10.1016/s0040-4039(00)73644-6.

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50

Weerapreeyakul, Natthida, R. Gary Hollenbeck, and Prashant J. Chikhale. "Stability of bioreductive drug delivery systems containing melphalan is influenced by conformational constraint and electronic properties of substituents." Bioorganic & Medicinal Chemistry Letters 10, no. 21 (November 2000): 2391–95. http://dx.doi.org/10.1016/s0960-894x(00)00496-0.

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