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1

Zhang, Yuqi, and Michel F. Sanner. "AutoDock CrankPep: combining folding and docking to predict protein–peptide complexes." Bioinformatics 35, no. 24 (2019): 5121–27. http://dx.doi.org/10.1093/bioinformatics/btz459.

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Abstract Motivation Protein–peptide interactions mediate a wide variety of cellular and biological functions. Methods for predicting these interactions have garnered a lot of interest over the past few years, as witnessed by the rapidly growing number of peptide-based therapeutic molecules currently in clinical trials. The size and flexibility of peptides has shown to be challenging for existing automated docking software programs. Results Here we present AutoDock CrankPep or ADCP in short, a novel approach to dock flexible peptides into rigid receptors. ADCP folds a peptide in the potential f
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2

Blaszczyk, Maciej, Maciej Pawel Ciemny, Andrzej Kolinski, Mateusz Kurcinski, and Sebastian Kmiecik. "Protein–peptide docking using CABS-dock and contact information." Briefings in Bioinformatics 20, no. 6 (2018): 2299–305. http://dx.doi.org/10.1093/bib/bby080.

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Abstract CABS-dock is a computational method for protein–peptide molecular docking that does not require predefinition of the binding site. The peptide is treated as fully flexible, while the protein backbone undergoes small fluctuations and, optionally, large-scale rearrangements. Here, we present a specific CABS-dock protocol that enhances the docking procedure using fragmentary information about protein–peptide contacts. The contact information is used to narrow down the search for the binding peptide pose to the proximity of the binding site. We used information on a single-chosen and rand
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3

Hamasaki, Naotaka, Hiroyuki Kuma, Kazuhisa Ota, Masao Sakaguchi, and Katsuyoshi Mihara. "A new concept in polytopic membrane proteins following from the study of band 3 protein." Biochemistry and Cell Biology 76, no. 5 (1998): 729–33. http://dx.doi.org/10.1139/o98-085.

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In the present communication, we introduce a novel concept in multispanning polytopic membrane proteins revealed by the study of the band 3 protein. The transmembrane domain of such proteins can be divided into three categories, that is, hydrophilic loops connecting transmembrane peptides (category 1), portions embedded by peptide-peptide interactions (category 2), and portions embedded by peptide-lipid interactions (category 3). Category 2 peptides of polytopic membrane proteins were found to stably reside in the lipid bilayer without peptide-lipid interactions that had been thought to be ess
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Kosugi, Takatsugu, and Masahito Ohue. "Design of Cyclic Peptides Targeting Protein–Protein Interactions Using AlphaFold." International Journal of Molecular Sciences 24, no. 17 (2023): 13257. http://dx.doi.org/10.3390/ijms241713257.

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More than 930,000 protein–protein interactions (PPIs) have been identified in recent years, but their physicochemical properties differ from conventional drug targets, complicating the use of conventional small molecules as modalities. Cyclic peptides are a promising modality for targeting PPIs, but it is difficult to predict the structure of a target protein–cyclic peptide complex or to design a cyclic peptide sequence that binds to the target protein using computational methods. Recently, AlphaFold with a cyclic offset has enabled predicting the structure of cyclic peptides, thereby enabling
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Lin, Wen-Wei, Yu-Jen Wang, Cheng-Wen Ko, Tain-Lu Cheng, and Yeng-Tseng Wang. "Cyclic Peptide Inhibitors of the Tsg101 UEV Protein Interactions Refined through Global Docking and Gaussian Accelerated Molecular Dynamics Simulations." Polymers 12, no. 10 (2020): 2235. http://dx.doi.org/10.3390/polym12102235.

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Tsg101 UEV domain proteins are potential targets for virus infection therapy, especially for HIV and Ebola viruses. Peptides are key in curbing virus transmission, and cyclic peptides have a greater survival time than their linear peptides. To date, the accurate prediction of cyclic peptide-protein receptors binding conformations still is challenging because of high peptide flexibility. Here, a useful approach combined the global peptide docking, Gaussian accelerated molecular dynamics (GaMD), two-dimensional (2D) potential of mean force (PMF), normal molecular dynamics (cMD), and solvated int
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6

Meyer, Katrina, and Matthias Selbach. "Peptide-based Interaction Proteomics." Molecular & Cellular Proteomics 19, no. 7 (2020): 1070–75. http://dx.doi.org/10.1074/mcp.r120.002034.

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Protein-protein interactions are often mediated by short linear motifs (SLiMs) that are located in intrinsically disordered regions (IDRs) of proteins. Interactions mediated by SLiMs are notoriously difficult to study, and many functionally relevant interactions likely remain to be uncovered. Recently, pull-downs with synthetic peptides in combination with quantitative mass spectrometry emerged as a powerful screening approach to study protein-protein interactions mediated by SLiMs. Specifically, arrays of synthetic peptides immobilized on cellulose membranes provide a scalable means to identi
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7

Li, Chun-Mei, Minna Haapalainen, Justin Lee, Thorsten Nürnberger, Martin Romantschuk, and Suvi Taira. "Harpin of Pseudomonas syringae pv. phaseolicola Harbors a Protein Binding Site." Molecular Plant-Microbe Interactions® 18, no. 1 (2005): 60–66. http://dx.doi.org/10.1094/mpmi-18-0060.

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Harpin HrpZ of plant-pathogenic bacterium Pseudomonas syringae elicits a hypersensitive response (HR) in some nonhost plants, but its function in the pathogenesis process is still obscure. HrpZ-interacting proteins were identified by screening a phage-display library of random peptides. HrpZ of the bean pathogen P. syringae pv. Phaseolicola (HrpZPph) shows affinity to peptides with a consensus amino acid motif W(L)ARWLL(G/L). To localize the peptide-binding site, the hrpZPph gene was mutagenized with randomly placed 15-bp insertions, and the mutant proteins were screened for the peptide-bindin
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8

TOOMIK, Reet, and Pia EK. "A potent and highly selective peptide substrate for protein kinase C assay." Biochemical Journal 322, no. 2 (1997): 455–60. http://dx.doi.org/10.1042/bj3220455.

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Protein kinases exhibit substrate specificities that are often primarily determined by the amino acids around the phosphorylation sites. Peptides corresponding to protein kinase C phosphorylation sites in several different proteins were synthesized on SPOTs membrane which has recently been found to be applicable for studies of protein kinase specificity. After phosphorylation with protein kinase C, we chose the best phosphorylated peptides for the investigation of the importance of amino acids immediately adjacent to the phosphorylation site. The selectivity of the best protein kinase C substr
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9

Schork, Karin, Michael Turewicz, Julian Uszkoreit, Jörg Rahnenführer, and Martin Eisenacher. "Characterization of peptide-protein relationships in protein ambiguity groups via bipartite graphs." PLOS ONE 17, no. 10 (2022): e0276401. http://dx.doi.org/10.1371/journal.pone.0276401.

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In bottom-up proteomics, proteins are enzymatically digested into peptides before measurement with mass spectrometry. The relationship between proteins and their corresponding peptides can be represented by bipartite graphs. We conduct a comprehensive analysis of bipartite graphs using quantified peptides from measured data sets as well as theoretical peptides from an in silico digestion of the corresponding complete taxonomic protein sequence databases. The aim of this study is to characterize and structure the different types of graphs that occur and to compare them between data sets. We obs
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10

Levin, E. R. "Natriuretic peptide C-receptor: more than a clearance receptor." American Journal of Physiology-Endocrinology and Metabolism 264, no. 4 (1993): E483—E489. http://dx.doi.org/10.1152/ajpendo.1993.264.4.e483.

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The natriuretic peptide family of proteins acts through two distinct classes of receptors that signal through entirely different mechanisms. The elucidation of the structure of the guanylate cyclase-containing receptor proteins has provided a better understanding of the mechanisms by which the natriuretic peptides regulate diverse functions of salt and water balance, in conjunction with other vasoactive peptides. A second receptor class was named for the originally described function of this protein to clear the natriuretic peptides from plasma. The mechanism of signaling for the natriuretic p
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11

Anusha, G., and M. Monisha. "Molecular modeling and screening of antiviral peptides for Influenza A virus Polymerase basic protein 2(PB2) protein using Hpepdock software for the therapy of Influenza A." CARDIOMETRY, no. 25 (February 14, 2023): 1693–701. http://dx.doi.org/10.18137/cardiometry.2022.25.16931701.

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Aim: To determine the binding affinity (kcal/mol) for various antiviral peptides to target Influenza A virus PB2 protein using Hpepdock software and comparison with the Macrocyclic iHA100 peptide (Reference peptide). Materials and methods: The three-dimensional (3D) coordinates for PB2 protein were retrieved from Protein Data Bank (PDB ID 4P1U). The structures of 16 antiviral peptides were modeled using HPEPDOCK. The Molecular docking analysis of PB2 protein with derived antiviral peptides was performed using Hpepdock software. This software employs an algorithm that generates the output compl
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12

Anupam, Saha, Bhattachajee Sunirmal, and Mukherjee Susmita. "Research and Review: Drugs and Drugs Development Based on Protein Drug Delivery System." Research and Advances in Pharmacy and Life Sciences 1, no. 1 (2018): 1–13. https://doi.org/10.5281/zenodo.1493707.

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Protein Drug Delivery System is raising pharmaceuticals in the Health Care Systems and Allied Health Sciences in bearing of better treatment. A noteworthy test defying pharmaceutical researchers later on will be to plan fruitful measurement shapes for the up and coming age of medications. Protein and Peptide sedate conveyance framework are the Novel medication Delivery System. Protein and peptide upgrade the effectively conveyance of the medication to the coveted site of activity. Proteins and peptides are the richest segments of natural cells. They exist working, for example, compounds, hormo
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13

Zuo, Lingyan, Weiqian Li, Jifang Shi, Yingzhen Su, Hongyan Shuai, and Xin Yu. "SynB3 Conjugated QBP1 Passes Blood-Brain Barrier Models and Inhibits PolyQ Protein Aggregation." Protein & Peptide Letters 29, no. 1 (2022): 110–20. http://dx.doi.org/10.2174/0929866529666211221163930.

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Background: Polyglutamine diseases are degenerative diseases in the central nervous system caused by CAG trinucleotide repeat expansion which encodes polyglutamine tracts, leading to the misfolding of pathological proteins. Small peptides can be designed to prevent polyglutamine diseases by inhibiting the polyglutamine protein aggregation, for example, polyglutamine binding peptide 1(QBP1). However, the transportation capability of polyglutamine binding peptide 1 across the blood-brain barrier is less efficient. We hypothesized whether its therapeutic effect could be improved by increasing the
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14

Geetha, C., S. G. Venkatesh, L. Bingle, C. D. Bingle, and S. U. Gorr. "Design and Validation of Anti-inflammatory Peptides from Human Parotid Secretory Protein." Journal of Dental Research 84, no. 2 (2005): 149–53. http://dx.doi.org/10.1177/154405910508400208.

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Parotid secretory protein (PSP) and palate-lung-nasal epithelium clone (PLUNC) are novel secretory proteins that are expressed in the oral cavity and upper airways. Both proteins are related to bactericidal/permeability increasing protein (BPI). Cationic peptides derived from BPI exhibit anti-inflammatory activity. To test if PSP (C20orf70 gene product) also contains anti-inflammatory peptides, we designed 3 cationic peptides based on the predicted structure of PSP and known active regions of BPI. Each peptide inhibited the lipopolysaccharide (LPS)-stimulated secretion of TNFα from RAW 264.7 m
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15

Curran, T., C. Van Beveren, and I. M. Verma. "Viral and cellular fos proteins are complexed with a 39,000-dalton cellular protein." Molecular and Cellular Biology 5, no. 1 (1985): 167–72. http://dx.doi.org/10.1128/mcb.5.1.167-172.1985.

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The structure of viral and cellular fos gene products and their association with a 39,000-dalton cellular protein (p39) were investigated by using antisera raised against synthetic peptides. The first peptide, termed M, corresponded to amino acids 127 to 152 of the v-fos sequence, a region which is identical in c-fos. The second peptide, termed V, corresponded to the nine C-terminal amino acids of v-fos; this region is not present in c-fos. Rabbit antisera were purified by affinity chromatography against their respective peptides before being used for immunoprecipitation. M peptide antisera pr
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16

Curran, T., C. Van Beveren, and I. M. Verma. "Viral and cellular fos proteins are complexed with a 39,000-dalton cellular protein." Molecular and Cellular Biology 5, no. 1 (1985): 167–72. http://dx.doi.org/10.1128/mcb.5.1.167.

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The structure of viral and cellular fos gene products and their association with a 39,000-dalton cellular protein (p39) were investigated by using antisera raised against synthetic peptides. The first peptide, termed M, corresponded to amino acids 127 to 152 of the v-fos sequence, a region which is identical in c-fos. The second peptide, termed V, corresponded to the nine C-terminal amino acids of v-fos; this region is not present in c-fos. Rabbit antisera were purified by affinity chromatography against their respective peptides before being used for immunoprecipitation. M peptide antisera pr
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17

Hernandez, Daniel Perez, and Gunnar Dittmar. "Peptide array–based interactomics." Analytical and Bioanalytical Chemistry 413, no. 22 (2021): 5561–66. http://dx.doi.org/10.1007/s00216-021-03367-8.

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AbstractThe analysis of protein-protein interactions (PPIs) is essential for the understanding of cellular signaling. Besides probing PPIs with immunoprecipitation-based techniques, peptide pull-downs are an alternative tool specifically useful to study interactome changes induced by post-translational modifications. Peptides for pull-downs can be chemically synthesized and thus offer the possibility to include amino acid exchanges and post-translational modifications (PTMs) in the pull-down reaction. The combination of peptide pull-down and analysis of the binding partners with mass spectrome
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18

Piiper, A., D. Stryjek-Kaminska, R. Jahn, and S. Zeuzem. "Stimulation of inositol 1,4,5-trisphosphate production by peptides corresponding to the effector domain of different Rab3 isoforms and cross-linking of an effector domain peptide target." Biochemical Journal 309, no. 2 (1995): 621–27. http://dx.doi.org/10.1042/bj3090621.

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Rab3 proteins are localized on secretory vesicles and appear to be involved in regulated exocytosis. We have previously shown that a modified peptide corresponding to the effector domain of the small molecular mass GTP-binding protein Rab3A, Rab3AAL, stimulates inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] production and amylase release in digitonin-permeabilized pancreatic acini. Experiments using monoclonal antibodies reveal that the Rab3-like protein present in pancreatic acini is not the Rab3A isoform. However, since the putative effector domains of the four as yet known Rab3 proteins (A, B,
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19

Li, R. H., and J. O. Thomas. "Identification of a human protein that interacts with nuclear localization signals." Journal of Cell Biology 109, no. 6 (1989): 2623–32. http://dx.doi.org/10.1083/jcb.109.6.2623.

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Through a series of label transfer experiments, we have identified a HeLa cell nuclear protein that interacts with nuclear localization signals (NLSs). The protein has a molecular weight of 66,000 and an isoelectric point of approximately 6. It associates with a synthetic peptide that contains the SV-40 T antigen NLS peptide but not with an analogous peptide in which an asparagine is substituted for an essential lysine (un-NLS peptide). In addition to these peptides, several proteins have been tested as label donors. With the proteins, there is a correlation between nuclear localization (assay
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Wittmann-Liebold, Brigitte, Monika Ühlein, Henning Urlaub, Eva-Christina Müller, Albrecht Otto, and Oliver Bischof. "Structural and functional implications in the eubacterial ribosome as revealed by protein–rRNA and antibiotic contact sites." Biochemistry and Cell Biology 73, no. 11-12 (1995): 1187–97. http://dx.doi.org/10.1139/o95-128.

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Contact sites between protein and rRNA in 30S and 50S ribosomal subunits of Escherichia coli and Bacillus stearothermophilus were investigated at the molecular level using UV and 2–iminothiolane as cross-linkers. Thirteen ribosomal proteins (S3, S4, S7, S14, S17, L2, L4, L6, L14, L27, L28, L29, andL36) from these organisms were cross-linked in direct contact with the RNAs, and the peptide stretches as well as amino acids involved were identified. Further, the binding sites of puromycin and spiramycin were established at die peptide level in several proteins that were found to constitute me ant
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Benson, R. Edward, Elizabeth B. Gottlin, Dale J. Christensen, and Paul T. Hamilton. "Intracellular Expression of Peptide Fusions for Demonstration of Protein Essentiality in Bacteria." Antimicrobial Agents and Chemotherapy 47, no. 9 (2003): 2875–81. http://dx.doi.org/10.1128/aac.47.9.2875-2881.2003.

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ABSTRACT We describe a “protein knockout” technique that can be used to identify essential proteins in bacteria. This technique uses phage display to select peptides that bind specifically to purified target proteins. The peptides are expressed intracellularly and cause inhibition of growth when the protein is essential. In this study, peptides that each specifically bind to one of seven essential proteins were identified by phage display and then expressed as fusions to glutathione S-transferase in Escherichia coli. Expression of peptide fusions directed against E. coli DnaN, LpxA, RpoD, ProR
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Clément, B., B. Segui-Real, P. Savagner, H. K. Kleinman, and Y. Yamada. "Hepatocyte attachment to laminin is mediated through multiple receptors." Journal of Cell Biology 110, no. 1 (1990): 185–92. http://dx.doi.org/10.1083/jcb.110.1.185.

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The interaction of hepatocytes with the basement membrane glycoprotein laminin was studied using synthetic peptides derived from laminin sequences. Rat hepatocytes bind to laminin and three different sites within the A and B1 chains of laminin were identified. Active laminin peptides include the PA22-2 peptide (close to the carboxyl end of the long arm in the A chain), the RGD-containing peptide, PA21 (in the short arm of the A chain) and the pentapeptide YIGSR (in the short arm of the B1 chain). PA22-2 was the most potent peptide, whereas the other two peptides had somewhat lower activity. Fu
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23

Doytchinova, Irini, Mariyana Atanasova, Antonio Fernandez, F. Javier Moreno, Frits Koning, and Ivan Dimitrov. "Modeling Peptide–Protein Interactions by a Logo-Based Method: Application in Peptide–HLA Binding Predictions." Molecules 29, no. 2 (2024): 284. http://dx.doi.org/10.3390/molecules29020284.

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Peptide–protein interactions form a cornerstone in molecular biology, governing cellular signaling, structure, and enzymatic activities in living organisms. Improving computational models and experimental techniques to describe and predict these interactions remains an ongoing area of research. Here, we present a computational method for peptide–protein interactions’ description and prediction based on leveraged amino acid frequencies within specific binding cores. Utilizing normalized frequencies, we construct quantitative matrices (QMs), termed ‘logo models’ derived from sequence logos. The
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Anusha, G., and M. Monisha. "Molecular Modeling and Screening of Antiviral peptides for HIV-Glycoprotein (gp41) using Hpepdock software for the therapy of AIDS (Acquired ImmunoDeficiency Syndrome)." CARDIOMETRY, no. 25 (February 14, 2023): 1702–10. http://dx.doi.org/10.18137/cardiometry.2022.25.17021710.

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Aim: To determine the binding affinity (Kcal/mol) for various antiviral peptides to target AIDS (Acquired Immunodeficiency Syndrome) gp41 protein. Materials and methods: The three-dimensional coordinates of gp41 protein were retrieved from Protein data bank(PDB ID 3VIE). The structures of 16 antiviral peptides were modeled using Hpepdock software. The Hpepdock software was used to perform a molecular docking investigation of gp41 with antiviral peptides. This software uses an algorithm to produce output complexes based on peptide conformations and orientations.The power calculation was done by
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25

Panwar, Khushboo, Satyabrat Dutta, Richa Sarkar, et al. "Peptide Phage Display Technology Advancement and Uses in Biomedicine." International Journal of Current Microbiology and Applied Sciences 12, no. 1 (2023): 261–74. http://dx.doi.org/10.20546/ijcmas.2023.1201.029.

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A potent research tool for high-throughput protein interaction screening is a combinatorial phage library. Phage display has established itself as the most widely used molecular display technology. It is possible to find peptides that can bind target molecules and control their function by screening phage- displayed random peptide libraries. B-cell and T-cell epitope mapping, selecting bioactive peptides bound to receptors or proteins, disease-specific antigen mimics, peptides bound to non-protein targets, cell- or organ-specific peptides, and developing peptide-mediated drug delivery systems
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Nikcevich, K. M., D. Kopielski, and A. Finnegan. "Interference with the binding of a naturally processed peptide to class II alters the immunodominance of T cell epitopes in vivo." Journal of Immunology 153, no. 3 (1994): 1015–26. http://dx.doi.org/10.4049/jimmunol.153.3.1015.

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Abstract T lymphocytes elicited in response to an immunizing Ag usually recognize only one or a few immunodominant peptides. The mechanisms governing this process are poorly understood. This study examines the consequences of peptide competition on immunodominance. Immunization of B10.A mice with the native Staphylococcus aureus nuclease protein primes T cells to the dominant 86-100 peptide presented in association with I-Ek class II molecules. To render the 86-100 peptide incapable of binding to the class II molecule, single amino acid substitutions were introduced in the native Staphylococcu
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Akagi, Keiko, Taku Nagao та Tetsuro Urushidani. "Responsiveness of β-escin-permeabilized rabbit gastric gland model: effects of functional peptide fragments". American Journal of Physiology-Gastrointestinal and Liver Physiology 277, № 3 (1999): G736—G744. http://dx.doi.org/10.1152/ajpgi.1999.277.3.g736.

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We established a β-escin-permeabilized gland model with the use of rabbit isolated gastric glands. The glands retained an ability to secrete acid, monitored by [14C]aminopyrine accumulation, in response to cAMP, forskolin, and histamine. These responses were all inhibited by cAMP-dependent protein kinase inhibitory peptide. Myosin light-chain kinase inhibitory peptide also suppressed aminopyrine accumulation, whereas the inhibitory peptide of protein kinase C or that of calmodulin kinase II was without effect. Guanosine-5′- O-(3-thiotriphosphate) (GTPγS) abolished cAMP-stimulated acid secretio
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28

Tsybin, Youri O., Per Håkansson, Magnus Wetterhall, Karin E. Markides, and Jonas Bergquist. "Capillary Electrophoresis and Electron Capture Dissociation Fourier Transform Ion Cyclotron Resonance Mass Spectrometry for Peptide Mixture and Protein Digest Analysis." European Journal of Mass Spectrometry 8, no. 5 (2002): 389–95. http://dx.doi.org/10.1255/ejms.514.

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Recent advances in peptide fragmentation techniques and mass spectrometry have opened up the possibility of combining peptide separation techniques, such as capillary electrophoresis (CE) and capillary liquid chromatography, with Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) and electron capture dissociation (ECD) in order to characterize peptide mixtures and protein digests. The results presented in this study show that CE/ECD-FT-ICR MS can be employed for peptide characterization in mixtures of standard peptides and in peptides resulting from the enzymatic digestion
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Beachey, E. H., J. M. Seyer, and J. B. Dale. "Protective immunogenicity and T lymphocyte specificity of a trivalent hybrid peptide containing NH2-terminal sequences of types 5, 6, and 24 M proteins synthesized in tandem." Journal of Experimental Medicine 166, no. 3 (1987): 647–56. http://dx.doi.org/10.1084/jem.166.3.647.

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The protective immunogenicity of a hybrid peptide containing tandem copies of types 5, 6, and 24 M protein epitopes was investigated. An NH2-terminal peptide of type 24 M protein was chemically synthesized and then extended to include NH2-terminal peptides of types 6 and 5 M proteins yielding a 34-residue hybrid peptide containing a cysteine residue at its COOH-terminus. When conjugated via the cysteine residue to keyhole limpet hemocyanin (KLH), emulsified in CFA, and injected into rabbits, the synthetic hybrid evoked opsonic antibodies against types 5, 6, and 24 streptococci without stimulat
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Hauptmann, Judith, Daniel Schraivogel, Astrid Bruckmann, et al. "Biochemical isolation of Argonaute protein complexes by Ago-APP." Proceedings of the National Academy of Sciences 112, no. 38 (2015): 11841–45. http://dx.doi.org/10.1073/pnas.1506116112.

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During microRNA (miRNA)-guided gene silencing, Argonaute (Ago) proteins interact with a member of the TNRC6/GW protein family. Here we used a short GW protein-derived peptide fused to GST and demonstrate that it binds to Ago proteins with high affinity. This allows for the simultaneous isolation of all Ago protein complexes expressed in diverse species to identify associated proteins, small RNAs, or target mRNAs. We refer to our method as “Ago protein Affinity Purification by Peptides“ (Ago-APP). Furthermore, expression of this peptide competes for endogenous TNRC6 proteins, leading to global
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Santiago Vispo, Nelson. "Covalent Peptide Evolution: Redefining Protein–Protein Interaction Inhibition Through Phage Display." Bionatura Journal 2, no. 2 (2025): 1–5. https://doi.org/10.70099/bj/2025.02.02.16.

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Covalent cyclic peptides represent a transformative approach for targeting challenging protein-protein interactions (PPIs) characterized by flat, extensive binding surfaces. Recent advances in electrophilic phage display now enable the evolution of these peptides through integrating sulfur(VI) fluoride exchange (SuFEx) chemistry with functional selection strategies. This innovative platform combines genetic encoding with site-specific cyclization and warhead incorporation to generate high-affinity, irreversible binders. When targeting the SARS-CoV-2 Spike-ACE2 interface, the approach produced
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Young, John K., Donghui Li, Matthew C. Abramowitz, and Trudy G. Morrison. "Interaction of Peptides with Sequences from the Newcastle Disease Virus Fusion Protein Heptad Repeat Regions." Journal of Virology 73, no. 7 (1999): 5945–56. http://dx.doi.org/10.1128/jvi.73.7.5945-5956.1999.

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ABSTRACT Typical of many viral fusion proteins, the sequence of the Newcastle disease virus (NDV) fusion protein has several heptad repeat regions. One, HR1, is located just carboxyl terminal to the fusion peptide, while the other, HR2, is located adjacent to the transmembrane domain. The structure and function of a synthetic peptide with a sequence from the region of the NDV HR1 region (amino acids 150 to 173) were characterized. The peptide inhibited fusion with a half-maximal concentration of approximately 2 μM; however, inhibition was observed only if the peptide was added prior to proteas
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Meier, U. T., and G. Blobel. "A nuclear localization signal binding protein in the nucleolus." Journal of Cell Biology 111, no. 6 (1990): 2235–45. http://dx.doi.org/10.1083/jcb.111.6.2235.

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We used functional wild-type and mutant synthetic nuclear localization signal peptides of SV-40 T antigen cross-linked to human serum albumin (peptide conjugates) to assay their binding to proteins of rat liver nuclei on Western blots. Proteins of 140 and 55 kD (p140 and p55) were exclusively recognized by wild-type peptide conjugates. Free wild-type peptides competed for the wild-type peptide conjugate binding to p140 and p55 whereas free mutant peptides, which differed by a single amino acid from the wild type, competed less efficiently. The two proteins were extractable from nuclei by eithe
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Hoofnagle, Andrew N., Jeffrey R. Whiteaker, Steven A. Carr, et al. "Recommendations for the Generation, Quantification, Storage, and Handling of Peptides Used for Mass Spectrometry–Based Assays." Clinical Chemistry 62, no. 1 (2016): 48–69. http://dx.doi.org/10.1373/clinchem.2015.250563.

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Abstract BACKGROUND For many years, basic and clinical researchers have taken advantage of the analytical sensitivity and specificity afforded by mass spectrometry in the measurement of proteins. Clinical laboratories are now beginning to deploy these work flows as well. For assays that use proteolysis to generate peptides for protein quantification and characterization, synthetic stable isotope–labeled internal standard peptides are of central importance. No general recommendations are currently available surrounding the use of peptides in protein mass spectrometric assays. CONTENT The Clinic
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Jin, Bo, Jiayue Wang, Xiangnan Liu, et al. "Ubiquitin-Mimicking Peptides Transfer Differentiates by E1 and E2 Enzymes." BioMed Research International 2018 (August 30, 2018): 1–8. http://dx.doi.org/10.1155/2018/6062520.

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Ubiquitin and ubiquitin like proteins (UBLs) play key roles in eukaryotes. These proteins are attached to their target proteins through an E1-E2-E3 cascade and modify the functions of these proteins. Since the discovery of ubiquitin, several UBLs have been identified, including Nedd8, SUMO, ISG15, and Atg8. Ubiquitin and UBLs share a similar three-dimensional structure: β-grasp fold and an X-X-[R/A/E/K]-X-X-[G/X]-G motif at the C-terminus. We have previously reported that ubiquitin, Nedd8, and SUMO mimicking peptides which all contain the conserved motif X-X-[R/A/E/K]-X-X-[G/X]-G still retaine
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Dahiya, Sunita, and Rajiv Dahiya. "BIOAVAILABILITY ENHANCEMENT AND LIPID NANOCARRIER BASED DELIVERY OF PEPTIDES AND PROTEINS." Bulletin of Pharmaceutical Research 10, no. 1-3 (2020): 1–10. http://dx.doi.org/10.21276/bpr.2020.10.3.

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Peptides and proteins are vital biomacromolecules that perform several bodily functions in various physiological and biological processes. Being biocompatible and biodegradable, these macromolecules are considered promising platforms for delivery of drugs and genes. However, peptides and proteins suffer from major limitations including enzymatic degradation, short circulation half-lives, and poor membrane permeability that leads to poor bioavailability, challenging their effective delivery. This article briefly discusses the inherent challenges in peptide and protein delivery along with strate
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Loftis, Alexander R., Genwei Zhang, Coralie Backlund, et al. "An in vivo selection-derived d-peptide for engineering erythrocyte-binding antigens that promote immune tolerance." Proceedings of the National Academy of Sciences 118, no. 34 (2021): e2101596118. http://dx.doi.org/10.1073/pnas.2101596118.

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When displayed on erythrocytes, peptides and proteins can drive antigen-specific immune tolerance. Here, we investigated a straightforward approach based on erythrocyte binding to promote antigen-specific tolerance to both peptides and proteins. We first identified a robust erythrocyte-binding ligand. A pool of one million fully d-chiral peptides was injected into mice, blood cells were isolated, and ligands enriched on these cells were identified using nano-liquid chromatography–tandem mass spectrometry. One round of selection yielded a murine erythrocyte-binding ligand with an 80 nM apparent
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Yang, Yanlian, and Chen Wang. "Single-molecule studies on individual peptides and peptide assemblies on surfaces." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 371, no. 2000 (2013): 20120311. http://dx.doi.org/10.1098/rsta.2012.0311.

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This review is intended to reflect the recent progress in single-molecule studies of individual peptides and peptide assemblies on surfaces. The structures and the mechanism of peptide assembly are discussed in detail. The contents include the following topics: structural analysis of single peptide molecules, adsorption and assembly of peptides on surfaces, folding structures of the amyloid peptides, interaction between amyloid peptides and dye or drug molecules, and modulation of peptide assemblies by small molecules. The explorations of peptide adsorption and assembly will benefit the unders
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McNew, J. A., K. Sykes, and J. M. Goodman. "Specific cross-linking of the proline isomerase cyclophilin to a non-proline-containing peptide." Molecular Biology of the Cell 4, no. 2 (1993): 223–32. http://dx.doi.org/10.1091/mbc.4.2.223.

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A peptide corresponding to an efficient peroxisomal targeting sequence, the carboxy terminal 12 amino acids of PMP20 from Candida boidinii, was employed as an affinity ligand to search for a peroxisomal targeting receptor. Two proteins from yeast extracts with apparent molecular masses of 20 and 80 kDa were detected by chemical cross-linking to radioiodinated peptide. Both proteins were present in cytosolic supernatants. The 20-kDa species did not cross-link to a control peptide with reversed sequence, whereas the 80-kDa protein cross-linked to both peptides. The cross-linking assay was used t
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Neagu, Anca-Narcisa, Madhuri Jayathirtha, Emma Baxter, Mary Donnelly, Brindusa Alina Petre, and Costel C. Darie. "Applications of Tandem Mass Spectrometry (MS/MS) in Protein Analysis for Biomedical Research." Molecules 27, no. 8 (2022): 2411. http://dx.doi.org/10.3390/molecules27082411.

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Mass Spectrometry (MS) allows the analysis of proteins and peptides through a variety of methods, such as Electrospray Ionization-Mass Spectrometry (ESI-MS) or Matrix-Assisted Laser Desorption Ionization-Mass Spectrometry (MALDI-MS). These methods allow identification of the mass of a protein or a peptide as intact molecules or the identification of a protein through peptide-mass fingerprinting generated upon enzymatic digestion. Tandem mass spectrometry (MS/MS) allows the fragmentation of proteins and peptides to determine the amino acid sequence of proteins (top-down and middle-down proteomi
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Banta, Scott, Zaki Megeed, Monica Casali, Kaushal Rege, and Martin L. Yarmush. "Engineering Protein and Peptide Building Blocks for Nanotechnology." Journal of Nanoscience and Nanotechnology 7, no. 2 (2007): 387–401. http://dx.doi.org/10.1166/jnn.2007.153.

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The tremendous diversity in the structure and function of proteins has stimulated intense interest in using them for nanotechnology applications. In this review, we discuss recent developments in the engineering of proteins and peptides for the design and construction of functional and structural elements of nanodevices. We begin with a short discussion highlighting the differences between chemical and biological synthesis of proteins and peptides. Subsequently, we review recent applications of proteins and peptides as molecular motors, transducers, biosensors, and structural elements of nanod
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Prommajak, Trakul, Kamonlak Chailangka, Suwalee Fong-in, Paideang Khwanchai, and Patcharin Chaibarn. "Preparation of house cricket peptide by enzymatic hydrolysis and development of herbal peptide drink." Food Science and Preservation 31, no. 6 (2024): 847–56. https://doi.org/10.11002/fsp.2024.31.6.847.

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As environmental concerns drive a shift toward sustainable protein sources, insects have emerged as a promising alternative to conventional animal proteins. House crickets (Acheta domestica) are particularly notable for their high protein content and minimal ecological impact. However, the development of cricket peptide products faces a key challenge in enhancing sensory properties for consumer acceptance. This study compared the effects of two enzymes - papain and alkaline protease - on the quality of cricket peptides, focusing on peptide yield, degree of hydrolysis, and sensory attributes. A
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Hidayah, Nur, and Sandy Ardiansyah. "The Potential of Bioactive Peptides from Animal Protein Sources as a Mental Health Problems Prevention." AGRITROPICA : Journal of Agricultural Sciences 4, no. 2 (2021): 114–21. http://dx.doi.org/10.31186/j.agritropica.4.2.114-121.

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Protein is one of the substances of nutrition macro that is needed by the body are known to contain bioactive peptides. Protein sources can be from vegetables and animals, based on research an animal protein sources more complete, balanced, easily digested and absorbed than vegetable protein sources. Some sources of animal protein (milk, eggs, meat, and products derived and processed) were reported that contain of bioactive peptides. Bioactive peptide has effect as antimicrobial, antithrombotic, antihypertensive, opioid, immunomodulatory, binder minerals, antioxidants, and prevent mental healt
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Cao, Jiawen, Tiantian Fan, Yanlian Li, et al. "Phage-Display Based Discovery and Characterization of Peptide Ligands against WDR5." Molecules 26, no. 5 (2021): 1225. http://dx.doi.org/10.3390/molecules26051225.

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WD40 is a ubiquitous domain presented in at least 361 human proteins and acts as scaffold to form protein complexes. Among them, WDR5 protein is an important mediator in several protein complexes to exert its functions in histone modification and chromatin remodeling. Therefore, it was considered as a promising epigenetic target involving in anti-cancer drug development. In view of the protein–protein interaction nature of WDR5, we initialized a campaign to discover new peptide-mimic inhibitors of WDR5. In current study, we utilized the phage display technique and screened with a disulfide-bas
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Talian, Ivan, Veronika Kováčová, Marián Petrovič, and Ján Sabo. "Impact of un-polymerized acrylamide monomer residues onto protein identification by MALDI TOF MS." Open Chemistry 10, no. 4 (2012): 1073–78. http://dx.doi.org/10.2478/s11532-012-0024-3.

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AbstractPolyacrylamide gel electrophoresis is a powerful tool for protein mixture separation frequently used in proteomic studies. This article describes the problems which can arise during the identification process of separated proteins by matrix assisted laser desorption/ionization mass spectrometry. Presence of residual acrylamide monomers in the peptide samples leads to a significant peptide signal suppression. In the case of protein prohibitin, isolated from the MCF 7 breast cancer cell line, the peptide signal suppression was observed in 50% of all detected peptides.
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Silva, Rúben D. M., João Franco Machado, Kyle Gonçalves, et al. "Ultrasonication Improves Solid Phase Synthesis of Peptides Specific for Fibroblast Growth Factor Receptor and for the Protein-Protein Interface RANK-TRAF6." Molecules 26, no. 23 (2021): 7349. http://dx.doi.org/10.3390/molecules26237349.

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Considering our interest in the use of peptides as potential target-specific drugs or as delivery vectors of metallodrugs for various biomedical applications, it is crucial to explore improved synthetic methodologies to accomplish the highest peptide crude purity in the shortest time possible. Therefore, we compared “classical” fluorenylmethoxycarbonyl (Fmoc)-solid phase peptide synthesis (SPPS) with ultrasound(US)-assisted SPPS based on the preparation of three peptides, namely the fibroblast growth factor receptor 3(FGFR3)-specific peptide Pep1 (VSPPLTLGQLLS-NH2) and the novel peptides Pep2
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Porotto, Matteo, Christine C. Yokoyama, Gianmarco Orefice, et al. "Kinetic Dependence of Paramyxovirus Entry Inhibition." Journal of Virology 83, no. 13 (2009): 6947–51. http://dx.doi.org/10.1128/jvi.00416-09.

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ABSTRACT Peptides derived from conserved heptad repeat (HR) regions of paramyxovirus fusion (F) proteins inhibit viral fusion by interfering with the formation of the fusogenic six-helix bundle structure. Peptide efficacy is affected by the strength of the peptide association with the target virus's complementary HR region. Here, we show that a second basis for peptide efficacy lies in the kinetics of F activation by the homotypic attachment protein: efficient F activation by the attachment protein shortens the period during which antiviral molecules targeting intermediate states of F may act,
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Tsuchiya, Keisuke, Takashi Kurohara, Kiyoshi Fukuhara, Takashi Misawa, and Yosuke Demizu. "Helical Foldamers and Stapled Peptides as New Modalities in Drug Discovery: Modulators of Protein-Protein Interactions." Processes 10, no. 5 (2022): 924. http://dx.doi.org/10.3390/pr10050924.

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A “foldamer” is an artificial oligomeric molecule with a regular secondary or tertiary structure consisting of various building blocks. A “stapled peptide” is a peptide with stabilized secondary structures, in particular, helical structures by intramolecular covalent side-chain cross-linking. Helical foldamers and stapled peptides are potential drug candidates that can target protein-protein interactions because they enable multipoint molecular recognition, which is difficult to achieve with low-molecular-weight compounds. This mini-review describes a variety of peptide-based foldamers and sta
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Hardy, Christopher M., Gavin Clydesdale, and Karen J. Mobbs. "Development of mouse-specific contraceptive vaccines: infertility in mice immunized with peptide and polyepitope antigens." Reproduction 128, no. 4 (2004): 395–407. http://dx.doi.org/10.1530/rep.1.00276.

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Mouse-specific immunocontraceptive peptides have been identified in mouse proteins with key roles in reproduction from sequence comparisons to other species and tested for efficacy as immunocontraceptive antigens. Peptides were derived from granulocyte-macrophage colony-stimulating factor (GMCSF), the placental 27 kDa heat-shock protein (HSP), leukemia inhibitory factor receptor (LIFR), oviduct glycoprotein (OGP), proliferin (PLF), prolactin (PRL), sperm protein SP56 and mouse zona pellucida subunits 1 and 3 (ZP1, ZP3). Fertility of female BALB/c mice was reduced after immunization with severa
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Friedrich, Michael G., Zhen Wang, Kevin L. Schey, and Roger J. W. Truscott. "Mechanism of protein cleavage at asparagine leading to protein–protein cross-links." Biochemical Journal 476, no. 24 (2019): 3817–34. http://dx.doi.org/10.1042/bcj20190743.

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Long-lived proteins (LLPs) are present in numerous tissues within the human body. With age, they deteriorate, often leading to the formation of irreversible modifications such as peptide bond cleavage and covalent cross-linking. Currently understanding of the mechanism of formation of these cross-links is limited. As part of an ongoing study, proteomics was used to characterise sites of novel covalent cross-linking in the human lens. In this process, Lys residues were found cross-linked to C-terminal aspartates that had been present in the original protein as Asn residues. Cross-links were ide
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