Log in

Relevant bibliographies by topics / Enzymatic modifications / Journal articles

Journal articles on the topic 'Enzymatic modifications'

To see the other types of publications on this topic, follow the link: Enzymatic modifications.

Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Enzymatic modifications.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Bensaad, Dhiya Eddine, Mohammed Saleh, Khalid Ismail, and Youngseung Lee. "Recent Advances in Physical, Enzymatic, and Genetic Modifications of Starches." Jordan Journal of Agricultural Sciences 18, no. 3 (September 1, 2022): 245–58. http://dx.doi.org/10.35516/jjas.v18i3.474.

Full text

Abstract:

The current review presents the potential physical modification devised into thermal which includes pre-gelatinization and hydrothermal processing (i.e., annealing (ANN) and heat-moisture treatment (HMT)) and nonthermal modifications (i.e., high-pressure processing (HPP), micronization, ultrasonication, and pulsed electric field (PEF)). Rather than physical modification; enzymatic modification by single enzyme treatment, debranching enzymes, and multienzyme synergetic treatment was discussed. Genetic modification was also discussed as a potential starch modification for better utilization of starch.

APA, Harvard, Vancouver, ISO, and other styles

2

Das, Rakha Hari, Rajesh Ahirwar, Saroj Kumar, and Pradip Nahar. "Microwave-mediated enzymatic modifications of DNA." Analytical Biochemistry 471 (February 2015): 26–28. http://dx.doi.org/10.1016/j.ab.2014.11.003.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Bensaad, Dhiya Eddine, Mohammed Saleh, Khalid Ismail, Youngseung Lee, and George Ondier. "Chemical Modifications of Starch; A Prospective for Sweet Potato Starch." Jordan Journal of Agricultural Sciences 18, no. 4 (December 1, 2022): 293–308. http://dx.doi.org/10.35516/jjas.v18i4.802.

Full text

Abstract:

The current review presents the potential chemical modifications and applications of sweet potato starch in food and non-food industries. Native starch in general and particularly sweet potato starch characteristics have several functional features and applications in biomedicine as well as in the food industry. Modified starch is expected to enhance such characteristics as discussed in this review. For instance, due to the polymeric and branching nature of starch; the starch is usually less soluble, absorbs less water and oil, and shows a strong ability to bind to iodine. Also, native starches have significantly lower digestibility values under enzymatic treatment. Starch modifications, therefore are designed to enhance one or more of the above-mentioned limitations; thereby, modification of starch can alter the physicochemical characteristics of the native starch to improve its functional characteristic. Starches can be modified using physical methods (annealing, heat moisture treatment, pre-gelatinization, and other non-thermal processes), chemical methods (etherification, acetylation, acid modification, cationic linking, esterification, cross-linking, and oxidation), enzymatic modification methods, genetic alteration process or combination of them.

APA, Harvard, Vancouver, ISO, and other styles

4

Pourmohammadi, Kiana, and Elahe Abedi. "Enzymatic modifications of gluten protein: Oxidative enzymes." Food Chemistry 356 (September 2021): 129679. http://dx.doi.org/10.1016/j.foodchem.2021.129679.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Kondo, Shinichi, and Kunimoto Hotta. "Semisynthetic aminoglycoside antibiotics: Development and enzymatic modifications." Journal of Infection and Chemotherapy 5, no. 1 (1999): 1–9. http://dx.doi.org/10.1007/s101560050001.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Yamamoto, Yasuhiko, and Hiroshi Yamamoto. "Enzymatic and non‐enzymatic post‐translational modifications linking diabetes and heart disease." Journal of Diabetes Investigation 6, no. 1 (June 24, 2014): 16–17. http://dx.doi.org/10.1111/jdi.12248.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Treffon, Patrick, and Elizabeth Vierling. "Focus on Nitric Oxide Homeostasis: Direct and Indirect Enzymatic Regulation of Protein Denitrosation Reactions in Plants." Antioxidants 11, no. 7 (July 21, 2022): 1411. http://dx.doi.org/10.3390/antiox11071411.

Full text

Abstract:

Protein cysteines (Cys) undergo a multitude of different reactive oxygen species (ROS), reactive sulfur species (RSS), and/or reactive nitrogen species (RNS)-derived modifications. S-nitrosation (also referred to as nitrosylation), the addition of a nitric oxide (NO) group to reactive Cys thiols, can alter protein stability and activity and can result in changes of protein subcellular localization. Although it is clear that this nitrosative posttranslational modification (PTM) regulates multiple signal transduction pathways in plants, the enzymatic systems that catalyze the reverse S-denitrosation reaction are poorly understood. This review provides an overview of the biochemistry and regulation of nitro-oxidative modifications of protein Cys residues with a focus on NO production and S-nitrosation. In addition, the importance and recent advances in defining enzymatic systems proposed to be involved in regulating S-denitrosation are addressed, specifically cytosolic thioredoxins (TRX) and the newly identified aldo-keto reductases (AKR).

APA, Harvard, Vancouver, ISO, and other styles

8

Romero, Elvira, Bethan S. Jones, Bethany N. Hogg, Arnau Rué Casamajo, Martin A. Hayes, Sabine L. Flitsch, Nicholas J. Turner, and Christian Schnepel. "Enzymatic Late‐Stage Modifications: Better Late Than Never." Angewandte Chemie International Edition 60, no. 31 (March 8, 2021): 16824–55. http://dx.doi.org/10.1002/anie.202014931.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Castellani, Oscar F., E. Nora Martínez, and M. Cristina Añón. "Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis." Journal of Agricultural and Food Chemistry 48, no. 11 (November 2000): 5624–29. http://dx.doi.org/10.1021/jf000624o.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Jung, Guenther. "Smart peptide libraries are accessible via enzymatic modifications." Letters in Peptide Science 8, no. 3-5 (May 2001): 259–65. http://dx.doi.org/10.1007/bf02446526.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Roy, Anjana, Rajarshi Sil, and Abhay Sankar Chakraborti. "Non-enzymatic glycation induces structural modifications of myoglobin." Molecular and Cellular Biochemistry 338, no. 1-2 (November 29, 2009): 105–14. http://dx.doi.org/10.1007/s11010-009-0343-7.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Mahanta, Nilkamal, Andi Liu, Shihui Dong, Satish K. Nair, and Douglas A. Mitchell. "Enzymatic reconstitution of ribosomal peptide backbone thioamidation." Proceedings of the National Academy of Sciences 115, no. 12 (March 5, 2018): 3030–35. http://dx.doi.org/10.1073/pnas.1722324115.

Full text

Abstract:

Methyl-coenzyme M reductase (MCR) is an essential enzyme found strictly in methanogenic and methanotrophic archaea. MCR catalyzes a reversible reaction involved in the production and consumption of the potent greenhouse gas methane. The α-subunit of this enzyme (McrA) contains several unusual posttranslational modifications, including the only known naturally occurring example of protein thioamidation. We have recently demonstrated by genetic deletion and mass spectrometry that the tfuA and ycaO genes of Methanosarcina acetivorans are involved in thioamidation of Gly465 in the MCR active site. Modification to thioGly has been postulated to stabilize the active site structure of MCR. Herein, we report the in vitro reconstitution of ribosomal peptide thioamidation using heterologously expressed and purified YcaO and TfuA proteins from M. acetivorans. Like other reported YcaO proteins, this reaction is ATP-dependent but requires an external sulfide source. We also reconstitute the thioamidation activity of two TfuA-independent YcaOs from the hyperthermophilic methanogenic archaea Methanopyrus kandleri and Methanocaldococcus jannaschii. Using these proteins, we demonstrate the basis for substrate recognition and regioselectivity of thioamide formation based on extensive mutagenesis, biochemical, and binding studies. Finally, we report nucleotide-free and nucleotide-bound crystal structures for the YcaO proteins from M. kandleri. Sequence and structure-guided mutagenesis with subsequent biochemical evaluation have allowed us to assign roles for residues involved in thioamidation and confirm that the reaction proceeds via backbone O-phosphorylation. These data assign a new biochemical reaction to the YcaO superfamily and paves the way for further characterization of additional peptide backbone posttranslational modifications.

APA, Harvard, Vancouver, ISO, and other styles

13

Muneeruddin, K., C. E. Bobst, R. Frenkel, D. Houde, I. Turyan, Z. Sosic, and I. A. Kaltashov. "Characterization of a PEGylated protein therapeutic by ion exchange chromatography with on-line detection by native ESI MS and MS/MS." Analyst 142, no. 2 (2017): 336–44. http://dx.doi.org/10.1039/c6an02041k.

Full text

Abstract:

Detailed profiling of both enzymatic (e.g., glycosylation) and non-enzymatic (e.g., oxidation and deamidation) post-translational modifications (PTMs) is frequently required for the quality assessment of protein-based drugs.

APA, Harvard, Vancouver, ISO, and other styles

14

Deponte, Marcel, and Christopher Horst Lillig. "Enzymatic control of cysteinyl thiol switches in proteins." Biological Chemistry 396, no. 5 (May 1, 2015): 401–13. http://dx.doi.org/10.1515/hsz-2014-0280.

Full text

Abstract:

Abstract The spatiotemporal modification of specific cysteinyl residues in proteins has emerged as a novel concept in signal transduction. Such modifications alter the redox state of the cysteinyl thiol group, with implications for the structure and biological function of the protein. Regulatory cysteines are therefore classified as ‘thiol switches’. In this review we emphasize the relevance of enzymes for specific and efficient redox sensing, evaluate prerequisites and general properties of redox switches, and highlight mechanistic principles for toggling thiol switches. Moreover, we provide an overview of potential mechanisms for the initial formation of regulatory disulfide bonds. In brief, we address the three basic questions (i) what defines a thiol switch, (ii) which parameters confer signal specificity, and (iii) how are thiol switches oxidized?

APA, Harvard, Vancouver, ISO, and other styles

15

Laurent, M., and A. Fleury. "Hysteretic behavior and differential apparent stability properties of microtubule species emerge from the regulation of post-translational modifications of microtubules." Journal of Cell Science 109, no. 2 (February 1, 1996): 419–28. http://dx.doi.org/10.1242/jcs.109.2.419.

Full text

Abstract:

At the epigenetic level, microtubule diversity is generated by several mechanisms of reversible post-translational modifications of tubulin subunits. In most cases, modification enzymes preferentially act on the tubulin subunits of microtubules, whereas the substrate of the enzymes which ensure the reverse reaction is preferentially the alpha beta-dimer of nonpolymerized tubulin. Most modifications identified to date appear to be nearly ubiquitous within the animal kingdom. Moreover, modifications are generally not mutually exclusive, so that cellular microtubules often bear several distinct biochemical alterations whose biological role is yet unknown. Post-translational modifications often (but not always) occur on microtubule species with low turnover rate. However, in vitro comparison of the polymerization and depolymerization rates of modified or unmodified forms of tubulin did not reveal any significant difference between molecular species. Thus, post-translational modifications are thought to be the result rather than the cause of microtubule stability. We re-examine this contention in the light of a regulated kinetic scheme for multiple and non-exclusive enzymatic modifications of microtubules. This study shows that different apparent stability properties of microtubule species emerge under such a kinetic regulation, although all the species were assumed to have identical intrinsic stability properties. This model can be used to reinterpret the results of well-known studies bearing on the relationship between microtubule stability and post-translational modifications. Another important finding is that the existence of a regulation loop in one of the multiple pathways of enzymatic differentiation of microtubules endows the system with hysteretic properties. These properties may be viewed, under restrictive conditions, as a buffering mechanism for the transitions between microtubule growing and shrinking phases during fluctuations in the regulation of centrosomal nucleating activity.

APA, Harvard, Vancouver, ISO, and other styles

16

Stanic-Vucinic, Dragana, and Tanja Cirkovic-Velickovic. "The modifications of bovine β-lactoglobulin: Effects on its structural and functional properties." Journal of the Serbian Chemical Society 78, no. 3 (2013): 445–61. http://dx.doi.org/10.2298/jsc120810155s.

Full text

Abstract:

Beta-lactoglobulin (BLG) is the main whey protein and it is frequently used additive in wide range of food products due to its excellent techno-functional properties, high nutritional value and low cost. It is also considered as acid-resistant drug carrier for delivery of pharmaceutical and nutraceutical agents. However, BLG is the main allergen of milk. A variety of methods have been explored for modification of BLG in attempt to improve its functional properties and to decrease its allergenicity. Due to its compact globular structure BLG is relatively resistant to modifications, especially under mild conditions. BLG can be modified by physical, chemical and enzymatic treatments. Although chemical modifications offer efficient way of alteration of protein structural and functional properties, they are associated with safety concern. In the last decade there is a tendency for application of novel non-thermal physical processing methods, as well as enzymes in order to obtain BLG with desirable properties. The objective of this review is to overview chemical, physical and enzymatic processing techniques utilized to modify BLG and their effects on structure and functional properties of BLG.

APA, Harvard, Vancouver, ISO, and other styles

17

Chorfa, Nasima, Hervé Nlandu, Khaled Belkacemi, and Safia Hamoudi. "Physical and Enzymatic Hydrolysis Modifications of Potato Starch Granules." Polymers 14, no. 10 (May 16, 2022): 2027. http://dx.doi.org/10.3390/polym14102027.

Full text

Abstract:

In this work, a valorization of the starch stemming from downgraded potatoes was approached through the preparation of starch nanoparticles using different physical methods, namely liquid and supercritical carbon dioxide, high energy ball milling (HEBM), and ultrasonication on the one hand and enzymatic hydrolysis on the other hand. Starch nanoparticles are beneficial as a reinforcement in food packaging technology as they enhance the mechanical and water vapor resistance of polymers. Also, starch nanoparticles are appropriate for medical applications as carriers for the delivery of bioactive or therapeutic agents. The obtained materials were characterized using X-ray diffraction as well as scanning and transmission electron microscopies (SEM and TEM), whereas the hydrolysates were analyzed using size exclusion chromatography coupled with pulsed amperometric detection (SEC-PAD). The acquired results revealed that the physical modification methods led to moderate alterations of the potato starch granules’ size and crystallinity. However, enzymatic hydrolysis conducted using Pullulanase enzyme followed by nanoprecipitation of the hydrolysates allowed us to obtain very tiny starch nanoparticles sized between 20 and 50 nm, much smaller than the native starch granules, which have an average size of 10 μm. The effects of enzyme concentration, temperature, and reaction medium pH on the extent of hydrolysis in terms of the polymer carbohydrates’ fractions were investigated. The most promising results were obtained with a Pullulanase enzyme concentration of 160 npun/g of starch, at a temperature of 60 °C in a pH 4 phosphate buffer solution resulting in the production of hydrolysates containing starch polymers with low molecular weights corresponding mainly to P-10, P-5, and fractions with molecular weights lower than P-5 Pullulan standards.

APA, Harvard, Vancouver, ISO, and other styles

18

Harmel, Robert, and Dorothea Fiedler. "Features and regulation of non-enzymatic post-translational modifications." Nature Chemical Biology 14, no. 3 (February 14, 2018): 244–52. http://dx.doi.org/10.1038/nchembio.2575.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Punia, Sneh. "Barley starch modifications: Physical, chemical and enzymatic - A review." International Journal of Biological Macromolecules 144 (February 2020): 578–85. http://dx.doi.org/10.1016/j.ijbiomac.2019.12.088.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Schwarzenbolz, Uwe, and Thomas Henle. "Non-enzymatic modifications of proteins under high-pressure treatment." High Pressure Research 30, no. 4 (December 2010): 458–65. http://dx.doi.org/10.1080/08957959.2010.523893.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Piñol-Ripoll, Gerard, Anton Kichev, Ekaterina V. Ilieva, Petar Podlesniy, Isidre Ferrer, Manuel Portero-Otin, Reinald Pamplona, Francisco Purroy, and Carme Espinet. "P2-261: Non-enzymatic modifications increase in Alzheimer's disease." Alzheimer's & Dementia 6 (July 2010): S390—S391. http://dx.doi.org/10.1016/j.jalz.2010.05.1311.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Ravikiran, Boddepalli, and Radhakrishnan Mahalakshmi. "Unusual post-translational protein modifications: the benefits of sophistication." RSC Adv. 4, no. 64 (2014): 33958–74. http://dx.doi.org/10.1039/c4ra04694c.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Kazuhito, Tomizawa, and Fan-Yan Wei. "Posttranscriptional modifications in mitochondrial tRNA and its implication in mitochondrial translation and disease." Journal of Biochemistry 168, no. 5 (August 20, 2020): 435–44. http://dx.doi.org/10.1093/jb/mvaa098.

Full text

Abstract:

Abstract A fundamental aspect of mitochondria is that they possess DNA and protein translation machinery. Mitochondrial DNA encodes 22 tRNAs that translate mitochondrial mRNAs to 13 polypeptides of respiratory complexes. Various chemical modifications have been identified in mitochondrial tRNAs via complex enzymatic processes. A growing body of evidence has demonstrated that these modifications are essential for translation by regulating tRNA stability, structure and mRNA binding, and can be dynamically regulated by the metabolic environment. Importantly, the hypomodification of mitochondrial tRNA due to pathogenic mutations in mitochondrial tRNA genes or nuclear genes encoding modifying enzymes can result in life-threatening mitochondrial diseases in humans. Thus, the mitochondrial tRNA modification is a fundamental mechanism underlying the tight regulation of mitochondrial translation and is essential for life. In this review, we focus on recent findings on the physiological roles of 5-taurinomethyl modification (herein referred as taurine modification) in mitochondrial tRNAs. We summarize the findings in human patients and animal models with a deficiency of taurine modifications and provide pathogenic links to mitochondrial diseases. We anticipate that this review will help understand the complexity of mitochondrial biology and disease.

APA, Harvard, Vancouver, ISO, and other styles

24

Yamauchi, Mitsuo, and Marnisa Sricholpech. "Lysine post-translational modifications of collagen." Essays in Biochemistry 52 (May 25, 2012): 113–33. http://dx.doi.org/10.1042/bse0520113.

Full text

Abstract:

Type I collagen is the most abundant structural protein in vertebrates. It is a heterotrimeric molecule composed of two α1 chains and one α2 chain, forming a long uninterrupted triple helical structure with short non-triple helical telopeptides at both the N- and C-termini. During biosynthesis, collagen acquires a number of post-translational modifications, including lysine modifications, that are critical to the structure and biological functions of this protein. Lysine modifications of collagen are highly complicated sequential processes catalysed by several groups of enzymes leading to the final step of biosynthesis, covalent intermolecular cross-linking. In the cell, specific lysine residues are hydroxylated to form hydroxylysine. Then specific hydroxylysine residues located in the helical domain of the molecule are glycosylated by the addition of galactose or glucose-galactose. Outside the cell, lysine and hydroxylysine residues in the N- and C-telopeptides can be oxidatively deaminated to produce reactive aldehydes that undergo a series of non-enzymatic condensation reactions to form covalent intra- and inter-molecular cross-links. Owing to the recent advances in molecular and cellular biology, and analytical technologies, the biological significance and molecular mechanisms of these modifications have been gradually elucidated. This chapter provides an overview on these enzymatic lysine modifications and subsequent cross-linking.

APA, Harvard, Vancouver, ISO, and other styles

25

Clemen, Ramona, and Sander Bekeschus. "Oxidatively Modified Proteins: Cause and Control of Diseases." Applied Sciences 10, no. 18 (September 15, 2020): 6419. http://dx.doi.org/10.3390/app10186419.

Full text

Abstract:

Proteins succumb to numerous post-translational modifications (PTMs). These relate to enzymatic or non-enzymatic reactions taking place in either the intracellular or extracellular compartment. While intracellular oxidative changes are mainly due to redox stress, extracellular PTMs may be induced in an inflammatory micro milieu that is rich in reactive species. The increasing recognition of oxidative modifications as a causing agent or side-effect of pathophysiological states and diseases puts oxidative PTMS (oxPTMs) into the spotlight of inflammation research. Pathological hyper-modification of proteins can lead to accumulation, aggregation, cell stress, altered antigenic peptides, and damage-associated molecular pattern (DAMP)-like recognition by host immunity. Such processes are linked to cardiovascular disease and autoinflammation. At the same time, a detailed understanding of the mechanisms governing inflammatory responses to oxPTMs may capitalize on new therapeutic routes for enhancing adaptive immune responses as needed, for instance, in oncology. We here summarize some of the latest developments of oxPTMs in disease diagnosis and therapy. Potential target proteins and upcoming technologies, such as gas plasmas, are outlined for future research that may aid in identifying the molecular basis of immunogenic vs. tolerogenic oxPTMs.

APA, Harvard, Vancouver, ISO, and other styles

26

Srivastava, Rakesh, and Niraj Lodhi. "DNA Methylation Malleability and Dysregulation in Cancer Progression: Understanding the Role of PARP1." Biomolecules 12, no. 3 (March 8, 2022): 417. http://dx.doi.org/10.3390/biom12030417.

Full text

Abstract:

Mammalian genomic DNA methylation represents a key epigenetic modification and its dynamic regulation that fine-tunes the gene expression of multiple pathways during development. It maintains the gene expression of one generation of cells; particularly, the mitotic inheritance of gene-expression patterns makes it the key governing mechanism of epigenetic change to the next generation of cells. Convincing evidence from recent discoveries suggests that the dynamic regulation of DNA methylation is accomplished by the enzymatic action of TET dioxygenase, which oxidizes the methyl group of cytosine and activates transcription. As a result of aberrant DNA modifications, genes are improperly activated or inhibited in the inappropriate cellular context, contributing to a plethora of inheritable diseases, including cancer. We outline recent advancements in understanding how DNA modifications contribute to tumor suppressor gene silencing or oncogenic-gene stimulation, as well as dysregulation of DNA methylation in cancer progression. In addition, we emphasize the function of PARP1 enzymatic activity or inhibition in the maintenance of DNA methylation dysregulation. In the context of cancer remediation, the impact of DNA methylation and PARP1 pharmacological inhibitors, and their relevance as a combination therapy are highlighted.

APA, Harvard, Vancouver, ISO, and other styles

27

Summerhill, Grechko, Yet, Sobenin, and Orekhov. "The Atherogenic Role of Circulating Modified Lipids in Atherosclerosis." International Journal of Molecular Sciences 20, no. 14 (July 20, 2019): 3561. http://dx.doi.org/10.3390/ijms20143561.

Full text

Abstract:

Lipid accumulation in the arterial wall is a crucial event in the development of atherosclerotic lesions. Circulating low-density lipoprotein (LDL) is the major source of lipids that accumulate in the atherosclerotic plaques. It was discovered that not all LDL is atherogenic. In the blood plasma of atherosclerotic patients, LDL particles are the subject of multiple enzymatic and non-enzymatic modifications that determine their atherogenicity. Desialylation is the primary and the most important atherogenic LDL modification followed by a cascade of other modifications that also increase blood atherogenicity. The enzyme trans-sialidase is responsible for the desialylation of LDL, therefore, its activity plays an important role in atherosclerosis development. Moreover, circulating modified LDL is associated with immune complexes that also have a strong atherogenic potential. Moreover, it was shown that antibodies to modified LDL are also atherogenic. The properties of modified LDL were described, and the strong evidence indicating that it is capable of inducing intracellular accumulation of lipids was presented. The accumulated evidence indicated that the molecular properties of modified LDL, including LDL-containing immune complexes can serve as the prognostic/diagnostic biomarkers and molecular targets for the development of anti-atherosclerotic drugs.

APA, Harvard, Vancouver, ISO, and other styles

28

Mordhorst, Silja, and Jennifer N. Andexer. "Round, round we go – strategies for enzymatic cofactor regeneration." Natural Product Reports 37, no. 10 (2020): 1316–33. http://dx.doi.org/10.1039/d0np00004c.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Motorin, Yuri, and Virginie Marchand. "Analysis of RNA Modifications by Second- and Third-Generation Deep Sequencing: 2020 Update." Genes 12, no. 2 (February 16, 2021): 278. http://dx.doi.org/10.3390/genes12020278.

Full text

Abstract:

The precise mapping and quantification of the numerous RNA modifications that are present in tRNAs, rRNAs, ncRNAs/miRNAs, and mRNAs remain a major challenge and a top priority of the epitranscriptomics field. After the keystone discoveries of massive m6A methylation in mRNAs, dozens of deep sequencing-based methods and protocols were proposed for the analysis of various RNA modifications, allowing us to considerably extend the list of detectable modified residues. Many of the currently used methods rely on the particular reverse transcription signatures left by RNA modifications in cDNA; these signatures may be naturally present or induced by an appropriate enzymatic or chemical treatment. The newest approaches also include labeling at RNA abasic sites that result from the selective removal of RNA modification or the enhanced cleavage of the RNA ribose-phosphate chain (perhaps also protection from cleavage), followed by specific adapter ligation. Classical affinity/immunoprecipitation-based protocols use either antibodies against modified RNA bases or proteins/enzymes, recognizing RNA modifications. In this survey, we review the most recent achievements in this highly dynamic field, including promising attempts to map RNA modifications by the direct single-molecule sequencing of RNA by nanopores.

APA, Harvard, Vancouver, ISO, and other styles

30

Camera, E., S. Lisby, M. L. Dell'Anna, B. Santucci, R. Paganelli, O. Baadsgaard, and M. Picardo. "Levels of Enzymatic Antioxidants Activities in Mononuclear Cells and Skin Reactivity to Sodium Dodecyl Sulphate." International Journal of Immunopathology and Pharmacology 16, no. 1 (January 2003): 49–54. http://dx.doi.org/10.1177/039463200301600107.

Full text

Abstract:

Chemical irritants are able to produce several biological modifications of the skin, including the direct or indirect production of cytokines and reactive oxygen species leading to an inflammatory reaction. This report examines the existence of a possible correlation between the skin sensitivity to the irritant sodium dodecyl sulphate (SDS) and the activity of the enzymatic antioxidants. In twenty-three healthy subjects the evaluation of the epidermal and peripheral blood mononuclear cells (PBMCs) activities of superoxide Dismutase (SOD) and Catalase (Cat) demonstrate a significant correlation (r= 0,85 and p< 0,005 for SOD, and r= 0,87 and p< 0,0001 for Cat). Based on this result, on a further group of normal subjects (n=13) we studied the link between the threshold dose of skin reactivity to SDS and the activities of the enzymatic antioxidants in PBMCs. The degree of skin modification induced by SDS, applied at different concentrations for 24 hrs, was determined by means of Trans Epidermal Water Loss (TEWL), Erythemal Index or by Visual Score (VS). The minimal dose of the irritant capable of inducing skin modifications, was significantly correlated with SOD (r=0,77) and Cat (r=0,81) activities in PBMCs, and the modification of TEWL or EI were inversely correlated with levels of antioxidants in PBMCs (r=−0,62 for SOD and r=−0,66 for Cat). Our results indicate that the skin reactivity to irritants can be modulated by the levels of antioxidants, and suggest a possible therapeutical approach in preventing irritant contact dermatitis.

APA, Harvard, Vancouver, ISO, and other styles

31

Piersma, Bram, and Ruud A. Bank. "Collagen cross-linking mediated by lysyl hydroxylase 2: an enzymatic battlefield to combat fibrosis." Essays in Biochemistry 63, no. 3 (July 19, 2019): 377–87. http://dx.doi.org/10.1042/ebc20180051.

Full text

Abstract:

Abstract The hallmark of fibrosis is an excessive accumulation of collagen, ultimately leading to organ failure. It has become evident that the deposited collagen also exhibits qualitative modifications. A marked modification is the increased cross-linking, leading to a stabilization of the collagen network and limiting fibrosis reversibility. Not only the level of cross-linking is increased, but also the composition of cross-linking is altered: an increase is seen in hydroxyallysine-derived cross-links at the expense of allysine cross-links. This results in irreversible fibrosis, as collagen cross-linked by hydroxyallysine is more difficult to degrade. Hydroxyallysine is derived from a hydroxylysine in the telopeptides of collagen. The expression of lysyl hydroxylase (LH) 2 (LH2), the enzyme responsible for the formation of telopeptidyl hydroxylysine, is universally up-regulated in fibrosis. It is expected that inhibition of this enzyme will lead to reversible fibrosis without interfering with the normal repair process. In this review, we discuss the molecular basis of collagen modifications and cross-linking, with an emphasis on LH2-mediated hydroxyallysine cross-links, and their implications for the pathogenesis and treatment of fibrosis.

APA, Harvard, Vancouver, ISO, and other styles

32

YAMAMOTO, KAZUO, FUMIKO URAKI, SHUJI YONEI, and OSAMI YUKAWA. "Enzymatic Repair Mechanisms for Base Modifications Induced by Oxygen Radicals." Journal of Radiation Research 38, no. 1 (1997): 1–4. http://dx.doi.org/10.1269/jrr.38.1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Sonawane, Vijay Chintaman. "Enzymatic Modifications of Cephalosporins by Cephalosporin Acylase and Other Enzymes." Critical Reviews in Biotechnology 26, no. 2 (January 2006): 95–120. http://dx.doi.org/10.1080/07388550600718630.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Raynal-Ljutovac, K., Y. W. Park, F. Gaucheron, and S. Bouhallab. "Heat stability and enzymatic modifications of goat and sheep milk." Small Ruminant Research 68, no. 1-2 (March 2007): 207–20. http://dx.doi.org/10.1016/j.smallrumres.2006.09.006.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Lee, Mijoon, Dusan Hesek, Elena Lastochkin, David A. Dik, Bill Boggess, and Shahriar Mobashery. "Deciphering the Nature of Enzymatic Modifications of Bacterial Cell Walls." ChemBioChem 18, no. 17 (July 25, 2017): 1696–702. http://dx.doi.org/10.1002/cbic.201700293.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Sexton, Brittany S., Maggie Heider, Louise Williams, Bradley Langhorst, Eileen Dimalanta, and Lynne Apone. "Abstract 58: Novel enzymatic fragmentation for challenging samples and methods." Cancer Research 82, no. 12_Supplement (June 15, 2022): 58. http://dx.doi.org/10.1158/1538-7445.am2022-58.

Full text

Abstract:

Abstract Next Generation Sequencing (NGS) requires fragmentation of DNA molecules upstream of sequencing. Current methods for fragmentation include mechanical shearing and enzymatic fragmentation for NGS library preparation. Mechanical shearing requires costly instruments, can be difficult to automate for high throughput labs, and results in sample loss. In comparison, enzymatic fragmentation methods do not require expensive instruments and are automation friendly. However, current enzymatic fragmentation methods on the market can remove DNA modifications such as methylation, cement DNA damage resulting from formalin fixation in final libraries and can introduce sequencing artifacts or bias. Therefore, while many fragmentation methods are commercially available, challenges remain for sequencing samples such as FFPE DNA or for detecting DNA modification (e.g., 5-methylcytosine). We have developed a novel enzymatic fragmentation method that can be used upstream of library preparation for DNA methylation assessment or FFPE DNA. The novel enzymatic fragmentation method is quick and robust, taking as little as 20 minutes. It is automation-friendly and can be used to generate DNA fragments ranging from as small as 50 bp up to over 1000 bp. Here we demonstrate the use of the novel enzymatic fragmentation method upstream of 5mC library preparation methods. This fragmentation method maintained the methylation marks. These libraries showed improvements in GC bias, library yield, library complexity and other sequencing metrics over libraries generated with mechanically sheared DNA. The use of the novel enzymatic fragmentation method with FFPE DNA library preparation resulted in improvements in sequencing metrics (increased proper pairs, etc.). There was reduced FFPE-damage-derived mutations compared to mechanical shearing or other enzymatic fragmentation methods. Fragmenting DNA to defined sizes for diverse applications and sample types remains a challenging aspect of NGS library preparation. This new, robust enzymatic fragmentation method overcomes the limitations of some traditional mechanical and enzymatic fragmentation methods and improves the library preparation and sequencing for both DNA modification assessment studies and FFPE DNA. Citation Format: Brittany S. Sexton, Maggie Heider, Louise Williams, Bradley Langhorst, Eileen Dimalanta, Lynne Apone. Novel enzymatic fragmentation for challenging samples and methods [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2022; 2022 Apr 8-13. Philadelphia (PA): AACR; Cancer Res 2022;82(12_Suppl):Abstract nr 58.

APA, Harvard, Vancouver, ISO, and other styles

37

Härmä, Harri, Natalia Tong-Ochoa, Arjan J. van Adrichem, Ilian Jelesarov, Krister Wennerberg, and Kari Kopra. "Toward universal protein post-translational modification detection in high throughput format." Chemical Communications 54, no. 23 (2018): 2910–13. http://dx.doi.org/10.1039/c7cc09575a.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Vader, Gerben, René H. Medema, and Susanne M. A. Lens. "The chromosomal passenger complex: guiding Aurora-B through mitosis." Journal of Cell Biology 173, no. 6 (June 12, 2006): 833–37. http://dx.doi.org/10.1083/jcb.200604032.

Full text

Abstract:

During mitosis, the chromosomal passenger complex (CPC) orchestrates highly different processes, such as chromosome alignment, histone modification, and cytokinesis. Proper and timely localization of this complex is the key to precise control over the enzymatic core of the CPC, the Aurora-B kinase. We discuss the molecular mechanisms by which the CPC members direct the dynamic localization of the complex throughout cell division. Also, we summarize posttranslational modifications that occur on the CPC and discuss their roles in regulating localization and function of this mitotic complex.

APA, Harvard, Vancouver, ISO, and other styles

39

Nowakowski, Andrew B., William J. Wobig, and David H. Petering. "Native SDS-PAGE: high resolution electrophoretic separation of proteins with retention of native properties including bound metal ions." Metallomics 6, no. 5 (2014): 1068–78. http://dx.doi.org/10.1039/c4mt00033a.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Fu, Changkui, Andre Bongers, Ke Wang, Bin Yang, Yuan Zhao, Haibo Wu, Yen Wei, Hien T. T. Duong, Zhiming Wang, and Lei Tao. "Facile synthesis of a multifunctional copolymer via a concurrent RAFT-enzymatic system for theranostic applications." Polymer Chemistry 7, no. 3 (2016): 546–52. http://dx.doi.org/10.1039/c5py01652e.

Full text

Abstract:

Through a straightforward concurrent RAFT-enzymatic multicomponent polymerization system and subsequent post-polymerization modifications, a multi-functional copolymer for theranostic application has been efficiently prepared.

APA, Harvard, Vancouver, ISO, and other styles

41

Wang, Ke, Danzhu Wang, Kaili Ji, Weixuan Chen, Yueqin Zheng, Chaofeng Dai, and Binghe Wang. "Post-synthesis DNA modifications using a trans-cyclooctene click handle." Organic & Biomolecular Chemistry 13, no. 3 (2015): 909–15. http://dx.doi.org/10.1039/c4ob02031f.

Full text

Abstract:

Efficient enzymatic DNA incorporation of trans-cyclooctene thymidine triphosphate (TCO-TTP) is reported. The general handle of trans-cyclooctene can undergo a rapid bioorthogonal cycloaddition with tetrazine, which is suitable for further DNA labeling work.

APA, Harvard, Vancouver, ISO, and other styles

42

Staniszewska, Magdalena M., and Ram H. Nagaraj. "3-Hydroxykynurenine-mediated Modification of Human Lens Proteins." Journal of Biological Chemistry 280, no. 23 (April 6, 2005): 22154–64. http://dx.doi.org/10.1074/jbc.m501419200.

Full text

Abstract:

Tryptophan can be oxidized in the eye lens by both enzymatic and non-enzymatic mechanisms. Oxidation products, such as kynurenines, react with proteins to form yellow-brown pigments and cause covalent cross-linking. We generated a monoclonal antibody against 3-hydroxykynurenine (3OHKYN)-modified keyhole limpet hemocyanin and characterized it using 3OHKYN-modified amino acids and proteins. This monoclonal antibody reacted with 3OHKYN-modified Nα-acetyl lysine, Nα-acetyl histidine, Nα-acetyl arginine, and Nα-acetyl cysteine. Among the several tryptophan oxidation products tested, 3OHKYN produced the highest concentration of antigen when reacted with human lens proteins. A major antigen from the reaction of 3OHKYN and Nα-acetyl lysine was purified by reversed phase high pressure liquid chromatography, which was characterized by spectroscopy and identified as 2-amino-3-hydroxyl-α-((5S)-5-acetamino-5-carboxypentyl amino)-γ-oxo-benzene butanoic acid. Enzyme-digested cataractous lens proteins displayed 3OHKYN-derived modifications. Immunohistochemistry revealed 3OHKYN modifications in proteins associated with the lens fiber cell plasma membrane. The low molecular products (<10,000 Da) isolated from normal lenses after reaction with glucosidase followed by incubation with proteins generated 3OHKYN-derived products. Human lens epithelial cells incubated with 3OHKYN showed intense immunoreactivity. We also investigated the effect of glycation on tryptophan oxidation and kynurenine-mediated modification of lens proteins. The results showed that glycation products failed to oxidize tryptophan or generate kynurenine modifications in proteins. Our studies indicate that 3OHKYN modifies lens proteins independent of glycation to form products that may contribute to protein aggregation and browning during cataract formation.

APA, Harvard, Vancouver, ISO, and other styles

43

Nazari, Simin, and Amira Abdelrasoul. "Impact of Membrane Modification and Surface Immobilization Techniques on the Hemocompatibility of Hemodialysis Membranes: A Critical Review." Membranes 12, no. 11 (October 28, 2022): 1063. http://dx.doi.org/10.3390/membranes12111063.

Full text

Abstract:

Despite significant research efforts, hemodialysis patients have poor survival rates and low quality of life. Ultrafiltration (UF) membranes are the core of hemodialysis treatment, acting as a barrier for metabolic waste removal and supplying vital nutrients. So, developing a durable and suitable membrane that may be employed for therapeutic purposes is crucial. Surface modificationis a useful solution to boostmembrane characteristics like roughness, charge neutrality, wettability, hemocompatibility, and functionality, which are important in dialysis efficiency. The modification techniques can be classified as follows: (i) physical modification techniques (thermal treatment, polishing and grinding, blending, and coating), (ii) chemical modification (chemical methods, ozone treatment, ultraviolet-induced grafting, plasma treatment, high energy radiation, and enzymatic treatment); and (iii) combination methods (physicochemical). Despite the fact that each strategy has its own set of benefits and drawbacks, all of these methods yielded noteworthy outcomes, even if quantifying the enhanced performance is difficult. A hemodialysis membrane with outstanding hydrophilicity and hemocompatibility can be achieved by employing the right surface modification and immobilization technique. Modified membranes pave the way for more advancement in hemodialysis membrane hemocompatibility. Therefore, this critical review focused on the impact of the modification method used on the hemocompatibility of dialysis membranes while covering some possible modifications and basic research beyond clinical applications.

APA, Harvard, Vancouver, ISO, and other styles

44

Paschinger, Katharina, and Iain B. H. Wilson. "Comparisons of N-glycans across invertebrate phyla." Parasitology 146, no. 14 (May 3, 2019): 1733–42. http://dx.doi.org/10.1017/s0031182019000398.

Full text

Abstract:

AbstractMany invertebrates are either parasites themselves or vectors involved in parasite transmission; thereby, the interactions of parasites with final or intermediate hosts are often mediated by glycans. Therefore, it is of interest to compare the glycan structures or motifs present across invertebrate species. While a typical vertebrate modification such as sialic acid is rare in lower animals, antennal and core modifications of N-glycans are highly varied and range from core fucose, galactosylated fucose, fucosylated galactose, methyl groups, glucuronic acid and sulphate through to addition of zwitterionic moieties (phosphorylcholine, phosphoethanolamine and aminoethylphosphonate). Only in some cases are the enzymatic bases and the biological function of these modifications known. We are indeed still in the phase of discovering invertebrate glycomes primarily using mass spectrometry, but molecular biology and microarraying techniques are complementary to the determination of novel glycan structures and their functions.

APA, Harvard, Vancouver, ISO, and other styles

45

Azevedo, Cristina, and Adolfo Saiardi. "The new world of inorganic polyphosphates." Biochemical Society Transactions 44, no. 1 (February 9, 2016): 13–17. http://dx.doi.org/10.1042/bst20150210.

Full text

Abstract:

Post-translational modifications (PTMs) add regulatory features to proteins that help establish the complex functional networks that make up higher organisms. Advances in analytical detection methods have led to the identification of more than 200 types of PTMs. However, some modifications are unstable under the present detection methods, anticipating the existence of further modifications and a much more complex map of PTMs. An example is the recently discovered protein modification polyphosphorylation. Polyphosphorylation is mediated by inorganic polyphosphate (polyP) and represents the covalent attachment of this linear polymer of orthophosphate to lysine residues in target proteins. This modification has eluded MS analysis as both polyP itself and the phosphoramidate bonds created upon its reaction with lysine residues are highly unstable in acidic conditions. Polyphosphorylation detection was only possible through extensive biochemical characterization. Two targets have been identified: nuclear signal recognition 1 (Nsr1) and its interacting partner, topoisomerase 1 (Top1). Polyphosphorylation occurs within a conserved N-terminal polyacidic serine (S) and lysine (K) rich (PASK) cluster. It negatively regulates Nsr1–Top1 interaction and impairs Top1 enzymatic activity, namely relaxing supercoiled DNA. Modulation of cellular levels of polyP regulates Top1 activity by modifying its polyphosphorylation status. Here we discuss the significance of the recently identified new role of inorganic polyP.

APA, Harvard, Vancouver, ISO, and other styles

46

Duan, Jicheng, Matthew J. Gaffrey, and Wei-Jun Qian. "Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines." Molecular BioSystems 13, no. 5 (2017): 816–29. http://dx.doi.org/10.1039/c6mb00861e.

Full text

Abstract:

Post-translational modifications on protein cysteines play a crucial role in redox signaling, in the regulation of enzymatic activity and protein function, and in maintaining redox homeostasis in living systems.

APA, Harvard, Vancouver, ISO, and other styles

47

Sibbersen, Christian, and Mogens Johannsen. "Dicarbonyl derived post-translational modifications: chemistry bridging biology and aging-related disease." Essays in Biochemistry 64, no. 1 (January 15, 2020): 97–110. http://dx.doi.org/10.1042/ebc20190057.

Full text

Abstract:

Abstract In living systems, nucleophilic amino acid residues are prone to non-enzymatic post-translational modification by electrophiles. α-Dicarbonyl compounds are a special type of electrophiles that can react irreversibly with lysine, arginine, and cysteine residues via complex mechanisms to form post-translational modifications known as advanced glycation end-products (AGEs). Glyoxal, methylglyoxal, and 3-deoxyglucosone are the major endogenous dicarbonyls, with methylglyoxal being the most well-studied. There are several routes that lead to the formation of dicarbonyl compounds, most originating from glucose and glucose metabolism, such as the non-enzymatic decomposition of glycolytic intermediates and fructosyl amines. Although dicarbonyls are removed continuously mainly via the glyoxalase system, several conditions lead to an increase in dicarbonyl concentration and thereby AGE formation. AGEs have been implicated in diabetes and aging-related diseases, and for this reason the elucidation of their structure as well as protein targets is of great interest. Though the dicarbonyls and reactive protein side chains are of relatively simple nature, the structures of the adducts as well as their mechanism of formation are not that trivial. Furthermore, detection of sites of modification can be demanding and current best practices rely on either direct mass spectrometry or various methods of enrichment based on antibodies or click chemistry followed by mass spectrometry. Future research into the structure of these adducts and protein targets of dicarbonyl compounds may improve the understanding of how the mechanisms of diabetes and aging-related physiological damage occur.

APA, Harvard, Vancouver, ISO, and other styles

48

Kim, Joohwan, and Gina Lee. "Metabolic Control of m6A RNA Modification." Metabolites 11, no. 2 (January 30, 2021): 80. http://dx.doi.org/10.3390/metabo11020080.

Full text

Abstract:

Nutrients and metabolic pathways regulate cell growth and cell fate decisions via epigenetic modification of DNA and histones. Another key genetic material, RNA, also contains diverse chemical modifications. Among these, N6-methyladenosine (m6A) is the most prevalent and evolutionarily conserved RNA modification. It functions in various aspects of developmental and disease states, by controlling RNA metabolism, such as stability and translation. Similar to other epigenetic processes, m6A modification is regulated by specific enzymes, including writers (methyltransferases), erasers (demethylases), and readers (m6A-binding proteins). As this is a reversible enzymatic process, metabolites can directly influence the flux of this reaction by serving as substrates and/or allosteric regulators. In this review, we will discuss recent understanding of the regulation of m6A RNA modification by metabolites, nutrients, and cellular metabolic pathways.

APA, Harvard, Vancouver, ISO, and other styles

49

Pflum, Mary Kay H., Jeffrey K. Tong, William S. Lane, and Stuart L. Schreiber. "Histone Deacetylase 1 Phosphorylation Promotes Enzymatic Activity and Complex Formation." Journal of Biological Chemistry 276, no. 50 (October 15, 2001): 47733–41. http://dx.doi.org/10.1074/jbc.m105590200.

Full text

Abstract:

Accessibility of the genome to DNA-binding transcription factors is regulated by proteins that control the acetylation of amino-terminal lysine residues on nucleosomal histones. Specifically, histone deacetylase (HDAC) proteins repress transcription by deacetylating histones. To date, the only known regulatory mechanism of HDAC1 function is via interaction with associated proteins. Although the control of HDAC1 function by protein interaction and recruitment is well precedented, we were interested in exploring HDAC1 regulation by post-translational modification. Human HDAC1 protein was analyzed by ion trap mass spectrometry, and two phosphorylated serine residues, Ser421and Ser423, were unambiguously identified. Loss of phosphorylation at Ser421and Ser423due to mutation to alanine or disruption of the casein kinase 2 consensus sequence directing phosphorylation reduced the enzymatic activity and complex formation of HDAC1. Deletion of the highly charged carboxyl-terminal region of HDAC1 also decreased its deacetylase activity and protein associations, revealing its requirement in maintaining HDAC1 function. Our results reinforce the importance of protein associations in modulating HDAC1 function and provide the first step toward characterizing the role of post-translational modifications in regulating HDAC activityin vivo.

APA, Harvard, Vancouver, ISO, and other styles

50

Sjögren, Jonathan, Rolf Lood, and Andreas Nägeli. "On enzymatic remodeling of IgG glycosylation; unique tools with broad applications." Glycobiology 30, no. 4 (October 16, 2019): 254–67. http://dx.doi.org/10.1093/glycob/cwz085.

Full text

Abstract:

Abstract The importance of IgG glycosylation has been known for many years not only by scientists in glycobiology but also by human pathogens that have evolved specific enzymes to modify these glycans with fundamental impact on IgG function. The rise of IgG as a major therapeutic scaffold for many cancer and immunological indications combined with the availability of unique enzymes acting specifically on IgG Fc-glycans have spurred a range of applications to study this important post-translational modification on IgG. This review article introduces why the IgG glycans are of distinguished interest, gives a background on the unique enzymatic tools available to study the IgG glycans and finally presents an overview of applications utilizing these enzymes for various modifications of the IgG glycans. The applications covered include site-specific glycan transglycosylation and conjugation, analytical workflows for monoclonal antibodies and serum diagnostics. Additionally, the review looks ahead and discusses the importance of O-glycosylation for IgG3, Fc-fusion proteins and other new formats of biopharmaceuticals.

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!