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536 results on '"Rosengren, K. Johan"'

153. Structural Properties of Relaxin Chimeras NMR Characterization of the R3/I5 Relaxin Peptide

Author

Haugaard-Jonsson, Linda M., Hossain, Mohammed Akhter, Daly, Norelle L., Bathgate, Ross A. D., Wade, John D., Craik, David J., Rosengren, K. Johan, Kedström, Linda Maria Haugaard, Haugaard-Jonsson, Linda M., Hossain, Mohammed Akhter, Daly, Norelle L., Bathgate, Ross A. D., Wade, John D., Craik, David J., Rosengren, K. Johan, and Kedström, Linda Maria Haugaard

Published
2009

154. Structure of the R3/I5 chimeric relaxin peptide, a selective GPCR135 and GPCR142 agonist

Author

Haugaard-Jonsson, Linda M., Hossain, Mohammed Akhter, Daly, Norelle L., Bathgate, Ross A. D., Wade, John D., Craik, David J., Rosengren, K. Johan, Kedström, Linda Maria Haugaard, Haugaard-Jonsson, Linda M., Hossain, Mohammed Akhter, Daly, Norelle L., Bathgate, Ross A. D., Wade, John D., Craik, David J., Rosengren, K. Johan, and Kedström, Linda Maria Haugaard

Published
2008

155. The A-chain of human relaxin family peptides has distinct roles in the binding and activation of the different relaxin family peptide receptors

Author

Hossain, Mohammed Akhter, Rosengren, K. Johan, Haugaard-Joensson, Linda M., Zhang, Soude, Layfield, Sharon, Ferraro, Tania, Daly, Norelle L., Tregear, Geoffrey W., Wade, John D., Bathgate, Ross A. D., Kedström, Linda Maria Haugaard, Hossain, Mohammed Akhter, Rosengren, K. Johan, Haugaard-Joensson, Linda M., Zhang, Soude, Layfield, Sharon, Ferraro, Tania, Daly, Norelle L., Tregear, Geoffrey W., Wade, John D., Bathgate, Ross A. D., and Kedström, Linda Maria Haugaard

Published
2008

156. Synthesis, conformation, and activity of human insulin-like peptide 5 (INSL5)

Author

Hossain, Mohammed Akhter, Bathgate, Ross A. D., Kong, Chze K., Shabanpoor, Fazel, Zhang, Suode, Haugaard-Jonsson, Linda M., Rosengren, K. Johan, Tregear, Geoffrey W., Wade, John D., Kedström, Linda Maria Haugaard, Hossain, Mohammed Akhter, Bathgate, Ross A. D., Kong, Chze K., Shabanpoor, Fazel, Zhang, Suode, Haugaard-Jonsson, Linda M., Rosengren, K. Johan, Tregear, Geoffrey W., Wade, John D., and Kedström, Linda Maria Haugaard

Published
2008

162. Structural and functional characterization of the conserved salt bridge in mammalian paneth cell alpha-defensins:solution structures of mouse CRYPTDIN-4 and (E15D)-CRYPTDIN-4

Author

Rosengren, K Johan, Daly, Norelle L, Fornander, Liselotte M, Jönsson, Linda M H, Shirafuji, Yoshinori, Qu, Xiaoqing, Vogel, Hans J, Ouellette, Andre J, Craik, David J, Kedström, Linda Maria Haugaard, Rosengren, K Johan, Daly, Norelle L, Fornander, Liselotte M, Jönsson, Linda M H, Shirafuji, Yoshinori, Qu, Xiaoqing, Vogel, Hans J, Ouellette, Andre J, Craik, David J, and Kedström, Linda Maria Haugaard

Abstract

alpha-Defensins are mediators of mammalian innate immunity, and knowledge of their structure-function relationships is essential for understanding their mechanisms of action. We report here the NMR solution structures of the mouse Paneth cell alpha-defensin cryptdin-4 (Crp4) and a mutant (E15D)-Crp4 peptide, in which a conserved Glu(15) residue was replaced by Asp. Structural analysis of the two peptides confirms the involvement of this Glu in a conserved salt bridge that is removed in the mutant because of the shortened side chain. Despite disruption of this structural feature, the peptide variant retains a well defined native fold because of a rearrangement of side chains, which result in compensating favorable interactions. Furthermore, salt bridge-deficient Crp4 mutants were tested for bactericidal effects and resistance to proteolytic degradation, and all of the variants had similar bactericidal activities and stability to proteolysis. These findings support the conclusion that the function of the conserved salt bridge in Crp4 is not linked to bactericidal activity or proteolytic stability of the mature peptide.

Published
2006

163. Engineering stable peptide toxins by means of backbone cyclization: stabilization of the α-conotoxin MII

Author

Clark, Richard J, Fischer, Harald, Dempster, Louise, Daly, Norelle L, Rosengren, K. . Johan, Nevin, Simon T, Meunier, Frederic A, Adams, David J, Craik, David J, Clark, Richard J, Fischer, Harald, Dempster, Louise, Daly, Norelle L, Rosengren, K. . Johan, Nevin, Simon T, Meunier, Frederic A, Adams, David J, and Craik, David J

Abstract

Conotoxins (CTXs), with their exquisite specificity and potency, have recently created much excitement as drug leads. However, like most peptides, their beneficial activities may potentially be undermined by susceptibility to proteolysis in vivo. By cyclizing the α-CTX MII by using a range of linkers, we have engineered peptides that preserve their full activity but have greatly improved resistance to proteolytic degradation. The cyclic MII analogue containing a seven-residue linker joining the N and C termini was as active and selective as the native peptide for native and recombinant neuronal nicotinic acetylcholine receptor subtypes present in bovine chromaffin cells and expressed in Xenopus oocytes, respectively. Furthermore, its resistance to proteolysis against a specific protease and in human plasma was significantly improved. More generally, to our knowledge, this report is the first on the cyclization of disulfide-rich toxins. Cyclization strategies represent an approach for stabilizing bioactive peptides while keeping their full potencies and should boost applications of peptide-based drugs in human medicine.

Published
2005

167. The Minimal Active Structure of Human Relaxin-2

Author

Hossain, Mohammed Akhter, primary, Rosengren, K. Johan, additional, Samuel, Chrishan S., additional, Shabanpoor, Fazel, additional, Chan, Linda J., additional, Bathgate, Ross A.D., additional, and Wade, John D., additional

Published
2011
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168. Decoding the Membrane Activity of the Cyclotide Kalata B1

Author

Henriques, Sónia Troeira, primary, Huang, Yen-Hua, additional, Rosengren, K. Johan, additional, Franquelim, Henri G., additional, Carvalho, Filomena A., additional, Johnson, Adam, additional, Sonza, Secondo, additional, Tachedjian, Gilda, additional, Castanho, Miguel A.R.B., additional, Daly, Norelle L., additional, and Craik, David J., additional

Published
2011
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174. Structural Properties of Relaxin Chimeras

Author

Haugaard‐Jönsson, Linda M., primary, Hossain, Mohammed Akhter, additional, Daly, Norelle L., additional, Bathgate, Ross A. D., additional, Wade, John D., additional, Craik, David J., additional, and Rosengren, K. Johan, additional

Published
2009
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175. Structural Insights into the Function of Relaxins

Author

Rosengren, K. Johan, primary, Bathgate, Ross A. D., additional, Craik, David J., additional, Daly, Norelle L., additional, Haugaard-Jönsson, Linda M., additional, Hossain, Mohammed Akhter, additional, and Wade, John D., additional

Published
2009
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176. Combined X-ray and NMR Analysis of the Stability of the Cyclotide Cystine Knot Fold That Underpins Its Insecticidal Activity and Potential Use as a Drug Scaffold

Author

Wang, Conan K., primary, Hu, Shu-Hong, additional, Martin, Jennifer L., additional, Sjögren, Tove, additional, Hajdu, Janos, additional, Bohlin, Lars, additional, Claeson, Per, additional, Göransson, Ulf, additional, Rosengren, K. Johan, additional, Tang, Jun, additional, Tan, Ning-Hua, additional, and Craik, David J., additional

Published
2009
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181. The A-chain of Human Relaxin Family Peptides Has Distinct Roles in the Binding and Activation of the Different Relaxin Family Peptide Receptors

Author

Hossain, Mohammed Akhter, primary, Rosengren, K. Johan, additional, Haugaard-Jönsson, Linda M., additional, Zhang, Soude, additional, Layfield, Sharon, additional, Ferraro, Tania, additional, Daly, Norelle L., additional, Tregear, Geoffrey W., additional, Wade, John D., additional, and Bathgate, Ross A.D., additional

Published
2008
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184. Identification, Characterization, and Three-Dimensional Structure of the Novel Circular Bacteriocin, Enterocin NKR-5-3B, from Enterococcus faecium.

Author

Kohei Himeno, Rosengren, K. Johan, Tomoko Inoue, Perez, Rodney H., Colgrave, Michelle L., Han Siean Lee, Chan, Lai Y., Henriques, Sónia Troeira, Koji Fujita, Naoki Ishibashi, Takeshi Zendo, Wilaipun, Pongtep, Jiro Nakayama, Leelawatcharamas, Vichien, Hiroyuki Jikuya, Craiky, David J., and Kenji Sonomoto

Subjects
*ENTEROCOCCUS faecalis, *BACTERIOCINS, *ANTIBACTERIAL agents, *ENTEROCINS, *POLYCYCLIC compounds
Abstract

Enterocin NKR-5-3B, one of the multiple bacteriodns produced by Enterococcus faecium NKR-5-3, is a 64-amino add novel drcular bacteriocin that displays broad-spectrum antimicrobial activity. Here we report the identification, characterization, and three-dimensional nuclear magnetic resonance solution structure determination of enterocin NKR-5-3B. Enterodn NKR-5-3B is characterized by four helical segments that enclose a compact hydrophobic core, which together with its circular backbone impart high stability and structural integrity. We also report the corresponding structural gene, enkB, that encodes an 87-amino add precursor peptide that undergoes a yet to be described enzymatic processing that involves adjacent cleavage and ligation of Leu24 and Trp87 to yield the mature (drcular) enterocin NKR-5-3B. [ABSTRACT FROM AUTHOR]

Published
2015
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185. Chapter Six - Structural Studies of Cyclotides.

Author

Daly, Norelle L. and Rosengren, K. Johan

Subjects
*PEPTIDES, *BIODEGRADATION, *CYSTINE, *CHEMICAL decomposition, *BIOENGINEERING
Abstract

Over the last two decades, the cyclotides have generated widespread interest both in the plant biology and peptide communities for a number of reasons, including their physiological roles in plants, evolution, and wide range of biological activities with potential therapeutic applications. But perhaps most of all it is their unique structure with a cyclic cystine knot motif that provide remarkable features such as resistance to chemical and biological degradation, which have caught researchers' attention. In this chapter, we summarize the key studies that have contributed to our understanding of the cyclotide fold, the structural features of these peptides, and the role and utilization of these features for native and engineered biological functions. [ABSTRACT FROM AUTHOR]

Published
2015
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186. Stabilization of the Cysteine-Rich Conotoxin MrIA by Using a 1,2,3-Triazole as a Disulfide Bond Mimetic.

Author

Gori, Alessandro, Wang, Ching‐I A., Harvey, Peta J., Rosengren, K. Johan, Bhola, Rebecca F., Gelmi, Maria L., Longhi, Renato, Christie, Macdonald J., Lewis, Richard J., Alewood, Paul F., and Brust, Andreas

Subjects
CYSTEINE, CONOTOXINS, TRIAZOLES, DISULFIDES, RING formation (Chemistry), PLASMA stability
Abstract

The design of disulfide bond mimetics is an important strategy for optimising cysteine-rich peptides in drug development. Mimetics of the drug lead conotoxin MrIA, in which one disulfide bond is selectively replaced of by a 1,4-disubstituted-1,2,3-triazole bridge, are described. Sequential copper-catalyzed azide-alkyne cycloaddition (CuAAC; click reaction) followed by disulfide formation resulted in the regioselective syntheses of triazole-disulfide hybrid MrIA analogues. Mimetics with a triazole replacing the Cys4-Cys13 disulfide bond retained tertiary structure and full in vitro and in vivo activity as norepinephrine reuptake inhibitors. Importantly, these mimetics are resistant to reduction in the presence of glutathione, thus resulting in improved plasma stability and increased suitability for drug development. [ABSTRACT FROM AUTHOR]

Published
2015
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187. Stabilisierung eines cysteinreichen Kegelschneckentoxins, MrIA, in Form eines 1,2,3-Triazol-Disulfidbrückenmimetikums.

Author

Gori, Alessandro, Wang, Ching ‐ I A., Harvey, Peta J., Rosengren, K. Johan, Bhola, Rebecca F., Gelmi, Maria L., Longhi, Renato, Christie, Macdonald J., Lewis, Richard J., Alewood, Paul F., and Brust, Andreas

Abstract

Copyright of Angewandte Chemie is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Published
2015
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194. Isolation, Solution Structure, and Insecticidal Activity of Kalata B2, a Circular Protein with a Twist: Do Möbius Strips Exist in Nature?,

Author

Jennings, Cameron V., primary, Rosengren, K. Johan, additional, Daly, Norelle L., additional, Plan, Manuel, additional, Stevens, Jackie, additional, Scanlon, Martin J., additional, Waine, Clement, additional, Norman, David G., additional, Anderson, Marilyn A., additional, and Craik, David J., additional

Published
2004
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200. Stretching Peptides to Generate Small Molecule β-Strand Mimics

Author

Adams, Zoë C., Silvestri, Anthony P., Chiorean, Sorina, Flood, Dillon T., Balo, Brian P., Shi, Yifan, Holcomb, Matthew, Walsh, Shawn I., Maillie, Colleen A., Pierens, Gregory K., Forli, Stefano, Rosengren, K. Johan, and Dawson, Philip E.

Abstract

Advances in the modulation of protein–protein interactions (PPIs) enable both characterization of PPI networks that govern diseases and design of therapeutics and probes. The shallow protein surfaces that dominate PPIs are challenging to target using standard methods, and approaches for accessing extended backbone structures are limited. Here, we incorporate a rigid, linear, diyne brace between side chains at the ito i+2 positions to generate a family of low-molecular-weight, extended-backbone peptide macrocycles. NMR and density functional theory studies show that these stretched peptides adopt stable, rigid conformations in solution and can be tuned to explore extended peptide conformational space. The diyne brace is formed in excellent conversions (>95%) and amenable to high-throughput synthesis. The minimalist structure-inducing tripeptide core (<300 Da) is amenable to further synthetic elaboration. Diyne-braced inhibitors of bacterial type 1 signal peptidase demonstrate the utility of the technique.

Published
2023
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