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Book
Marine Enzymes : Sources, Biochemistry and Bioprocesses for Marine Biotechnology
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Year: 2020 Publisher: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute

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Abstract

This book presents contributions from scientists who are directly involved in the potential of marine enzymes as useful tools in biocatalysis; the results of enzymatic bioprospecting in gross marine environments are acknowledged, including two review articles on general enzymatic processes and microalgal enzymes. In addition, studies on structural characterizations, biological functions and aspects related to the complexity of marine enzyme-based bioprocesses are discussed. Prominent conclusions by many scientists in the field of marine biotechnology emphasize that, due to marine biological diversity and the specificity of biological marine metabolisms, the study of biocatalysts on a global scale from this environment is just starting, and possesses huge potential for the development of applications with industrial benefits.

Keywords

Research & information: general --- Biology, life sciences --- metalloprotease --- adsorption analysis --- molecular docking --- affinity purification --- aminophenylboronic acid --- alginate degradation --- 4-deoxy-l-erythro-5-hexoseulose uronic acid (DEH) metabolism --- Bacteroidetes --- Proteobacteria --- Flavobacterium --- 2-keto-3-deoxy-d-gluconate (KDG) kinase --- 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase --- alginate-derived products --- marine enzymes --- biocatalysts --- bioprocesses --- biorefinery --- seafood --- marine biomarkers --- collagenase --- fermentation optimization --- collagen --- Pseudoalteromonas --- antioxidant peptides --- microcystin-degrading bacteria --- mycotoxin --- protease --- esterase --- inhibitor --- marine agent --- Catenovulum --- alkaline and cold-adapted dextranase --- isomaltoogligosaccharides --- biofilm --- dental caries --- growing cells --- resting cells --- asymmetric reduction --- marine fungi --- chiral alcohols --- alginate lyase --- marine bacterium --- Bacillus sp. Alg07 --- purification --- alginate oligosaccharides --- Vibrio weizhoudaoensis --- PL7 family --- salt-activated enzyme --- Serratia marcescens --- polyM-specific --- oligosaccharides --- Isoptericola halotolerans --- bifunctional alginate lyase --- α-d-galactosidase --- homology model --- GH 36 family --- mutation --- transglycosylation --- marine bacteria --- Pseudoalteromonas sp. KMM 701 --- leucine dehydrogenase --- cold-adapted --- Antarctic bacterium --- sea-ice --- homology modeling --- fucoidan --- endo-fucoidanase --- galactofucan --- molecular stabilisation --- Sargassum mcclurei --- Turbinaria ornata --- Alteromonas --- deep sea --- cold-adapted enzyme --- β-galactosidase --- lactose-free milk --- chitosanases --- chitin deacetylase --- deacetylation patterns --- chitooligosaccharides --- separating --- detecting --- expression --- deep-sea enzyme --- pCold vector --- Ascophyllum nodosum --- algal cell wall degrading enzymes --- enzyme-assisted extraction --- ichip device --- quorum quenching enzyme --- error prone PCR --- high-throughput screening --- site-directed mutagenesis --- catalytic ability --- Pectobacterium carotovorum subsp. carotovorum (Pcc) --- Alginate lyase --- Thermo-tolerant --- pH-stability --- Endo-manner --- Vibrio sp. SY01 --- polysaccharide lyase of family 6 --- characterization --- degradation pattern --- microalgae --- enzymes --- marine biotechnology --- -omics technologies --- heterologous expression --- homologous expression


Book
Novel Enzyme and Whole-Cell Biocatalysts
Authors: ---
Year: 2020 Publisher: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute

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Abstract

The concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for “green” synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and environmentally-responsible bio-based chemicals. Recent advances in synthetic biology, computational tools, and metabolic engineering have supported the discovery of new enzymes and the rational design of whole-cell biocatalysts. In this book, we highlight these current advances in the field of biocatalysis, with special emphasis on novel enzymes and whole-cell biocatalysts for applications in several industrial biotechnological applications.

Keywords

Technology: general issues --- 2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals


Book
Novel Enzyme and Whole-Cell Biocatalysts
Authors: ---
Year: 2020 Publisher: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute

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Abstract

The concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for “green” synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and environmentally-responsible bio-based chemicals. Recent advances in synthetic biology, computational tools, and metabolic engineering have supported the discovery of new enzymes and the rational design of whole-cell biocatalysts. In this book, we highlight these current advances in the field of biocatalysis, with special emphasis on novel enzymes and whole-cell biocatalysts for applications in several industrial biotechnological applications.

Keywords

2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals


Book
Marine Enzymes : Sources, Biochemistry and Bioprocesses for Marine Biotechnology
Author:
Year: 2020 Publisher: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute

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Abstract

This book presents contributions from scientists who are directly involved in the potential of marine enzymes as useful tools in biocatalysis; the results of enzymatic bioprospecting in gross marine environments are acknowledged, including two review articles on general enzymatic processes and microalgal enzymes. In addition, studies on structural characterizations, biological functions and aspects related to the complexity of marine enzyme-based bioprocesses are discussed. Prominent conclusions by many scientists in the field of marine biotechnology emphasize that, due to marine biological diversity and the specificity of biological marine metabolisms, the study of biocatalysts on a global scale from this environment is just starting, and possesses huge potential for the development of applications with industrial benefits.

Keywords

metalloprotease --- adsorption analysis --- molecular docking --- affinity purification --- aminophenylboronic acid --- alginate degradation --- 4-deoxy-l-erythro-5-hexoseulose uronic acid (DEH) metabolism --- Bacteroidetes --- Proteobacteria --- Flavobacterium --- 2-keto-3-deoxy-d-gluconate (KDG) kinase --- 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase --- alginate-derived products --- marine enzymes --- biocatalysts --- bioprocesses --- biorefinery --- seafood --- marine biomarkers --- collagenase --- fermentation optimization --- collagen --- Pseudoalteromonas --- antioxidant peptides --- microcystin-degrading bacteria --- mycotoxin --- protease --- esterase --- inhibitor --- marine agent --- Catenovulum --- alkaline and cold-adapted dextranase --- isomaltoogligosaccharides --- biofilm --- dental caries --- growing cells --- resting cells --- asymmetric reduction --- marine fungi --- chiral alcohols --- alginate lyase --- marine bacterium --- Bacillus sp. Alg07 --- purification --- alginate oligosaccharides --- Vibrio weizhoudaoensis --- PL7 family --- salt-activated enzyme --- Serratia marcescens --- polyM-specific --- oligosaccharides --- Isoptericola halotolerans --- bifunctional alginate lyase --- α-d-galactosidase --- homology model --- GH 36 family --- mutation --- transglycosylation --- marine bacteria --- Pseudoalteromonas sp. KMM 701 --- leucine dehydrogenase --- cold-adapted --- Antarctic bacterium --- sea-ice --- homology modeling --- fucoidan --- endo-fucoidanase --- galactofucan --- molecular stabilisation --- Sargassum mcclurei --- Turbinaria ornata --- Alteromonas --- deep sea --- cold-adapted enzyme --- β-galactosidase --- lactose-free milk --- chitosanases --- chitin deacetylase --- deacetylation patterns --- chitooligosaccharides --- separating --- detecting --- expression --- deep-sea enzyme --- pCold vector --- Ascophyllum nodosum --- algal cell wall degrading enzymes --- enzyme-assisted extraction --- ichip device --- quorum quenching enzyme --- error prone PCR --- high-throughput screening --- site-directed mutagenesis --- catalytic ability --- Pectobacterium carotovorum subsp. carotovorum (Pcc) --- Alginate lyase --- Thermo-tolerant --- pH-stability --- Endo-manner --- Vibrio sp. SY01 --- polysaccharide lyase of family 6 --- characterization --- degradation pattern --- microalgae --- enzymes --- marine biotechnology --- -omics technologies --- heterologous expression --- homologous expression


Book
Novel Enzyme and Whole-Cell Biocatalysts
Authors: ---
Year: 2020 Publisher: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute

Loading...
Export citation

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Bookmark

Abstract

The concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for “green” synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and environmentally-responsible bio-based chemicals. Recent advances in synthetic biology, computational tools, and metabolic engineering have supported the discovery of new enzymes and the rational design of whole-cell biocatalysts. In this book, we highlight these current advances in the field of biocatalysis, with special emphasis on novel enzymes and whole-cell biocatalysts for applications in several industrial biotechnological applications.

Keywords

Technology: general issues --- 2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals --- 2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals


Book
Targeting STAT3 and STAT5 in Cancer
Authors: --- ---
Year: 2020 Publisher: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute

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Abstract

Every minute, 34 new patients are diagnosed with cancer globally. Although over the past 50 years treatments have improved and survival rates have increased dramatically for several types of cancers, many remain incurable. Several aggressive types of blood and solid cancers form when mutations occur in a critical cellular signaling pathway, the JAK-STAT pathway; (Janus Kinase-Signal Transducer and Activator of Transcription). Currently, there are no clinically available drugs that target the oncogenic STAT3/5 proteins in particular or their Gain of Function hyperactive mutant products. Here, we summarize targeting approaches on STAT3/5, as the field moves towards clinical applications as well as we illuminate on upstream or downstream JAK-STAT pathway interference with kinase inhibitors, heat shock protein blockers or changing nuclear import/export processes. We cover the design paradigms and medicinal chemistry approaches to illuminate progress and challenges in understanding the pleiotropic role of STAT3 and STAT5 in oncogenesis, the microenvironment, the immune system in particular, all culminating in a complex interplay towards cancer progression.

Keywords

Research & information: general --- Biology, life sciences --- multiple myeloma --- STAT3 --- S3I-1757 --- nanoparticle --- CD38 --- siRNA/RNAi --- polyethylenimine --- PEI --- lipopolyplex --- siRNA delivery --- glioma --- glioblastoma --- STAT5 --- AKT --- ERK1/2 --- prolactin --- androgens --- prostate cancer --- knockout --- escape mechanisms --- stem/progenitor cells --- cell hierarchy --- cancer --- CD4+ T cells --- CD8+ T cells --- myeloid cells --- immune check point --- hepatitis C virus (HCV) --- cirrhosis --- hepatocellular carcinoma (HCC) --- endoplasmic reticulum (ER) stress --- oxidative stress (OS) --- unfolded protein response (UPR) --- microRNA-122 (miR-122) --- nuclear factor erythroid 2-related factor 2 (NRF2) --- signal transducer and activator of transcription 3 (STAT3) --- hepatocyte nuclear factor 4 alpha (HNF4A) --- solid cancers --- cell cycle --- apoptosis --- inflammation --- mitochondria --- stemness --- tumor suppression --- melanoma --- autoimmune disease --- immunotherapy --- tumor-immune cell interactions --- breast cancer --- PD-L1 --- M2 macrophages --- NK cells --- STAT3 inhibitor XIII --- hedging --- transaction costs --- dynamic programming --- risk management --- post-decision state variable --- cancer progression --- cancer-stem cell --- cytokine --- therapy resistance --- metastasis --- immunosuppression --- tumor microenvironment --- proliferation --- tyrosine kinase 2 --- JAK family of protein tyrosine kinases --- signal transducer and activator of transcription --- cytokine receptor signaling --- gain-of-function mutation --- tumorigenesis --- ADAM17 --- interleukin-6 --- trans-signaling --- epidermal growth factor receptor (EGF-R) --- shedding --- metalloprotease --- tumor necrosis factor alpha (TNFα) --- inflammation associated cancer --- colon cancer --- lung cancer --- SH2 domain --- mutations --- autosomal-dominant hyper IgE syndrome --- inflammatory hepatocellular adenomas --- T-cell large granular lymphocytic leukemia --- T-cell prolymphocytic leukemia --- growth hormone insensitivity syndrome --- nuclear pore complex --- nuclear transport receptors --- nucleocytoplasmic shuttling --- targeting --- tumor-associated macrophages --- adoptive T cell therapy --- immune suppression --- STAT transcription factors --- JAK --- STAT --- T-PLL --- T-cell leukemia --- meta-analysis --- STAT5B signaling --- small-molecule inhibitors --- cancer models --- companion animals --- comparative oncology --- pharmacological inhibitor --- STAT5 signaling --- chemotherapy resistance --- myeloid leukemia --- heat shock proteins --- chaperones --- stabilization --- targeted therapy --- ovarian cancer --- hematopoietic cancers --- therapeutic targeting --- pharmacological inhibitors --- mTOR --- Bone Marrow Failure Syndromes --- lymphocytes --- lymphoma --- T-cells --- RHOA --- NGS --- MPN --- JAK2 V617F --- neoplastic stem cells --- multiple myeloma --- STAT3 --- S3I-1757 --- nanoparticle --- CD38 --- siRNA/RNAi --- polyethylenimine --- PEI --- lipopolyplex --- siRNA delivery --- glioma --- glioblastoma --- STAT5 --- AKT --- ERK1/2 --- prolactin --- androgens --- prostate cancer --- knockout --- escape mechanisms --- stem/progenitor cells --- cell hierarchy --- cancer --- CD4+ T cells --- CD8+ T cells --- myeloid cells --- immune check point --- hepatitis C virus (HCV) --- cirrhosis --- hepatocellular carcinoma (HCC) --- endoplasmic reticulum (ER) stress --- oxidative stress (OS) --- unfolded protein response (UPR) --- microRNA-122 (miR-122) --- nuclear factor erythroid 2-related factor 2 (NRF2) --- signal transducer and activator of transcription 3 (STAT3) --- hepatocyte nuclear factor 4 alpha (HNF4A) --- solid cancers --- cell cycle --- apoptosis --- inflammation --- mitochondria --- stemness --- tumor suppression --- melanoma --- autoimmune disease --- immunotherapy --- tumor-immune cell interactions --- breast cancer --- PD-L1 --- M2 macrophages --- NK cells --- STAT3 inhibitor XIII --- hedging --- transaction costs --- dynamic programming --- risk management --- post-decision state variable --- cancer progression --- cancer-stem cell --- cytokine --- therapy resistance --- metastasis --- immunosuppression --- tumor microenvironment --- proliferation --- tyrosine kinase 2 --- JAK family of protein tyrosine kinases --- signal transducer and activator of transcription --- cytokine receptor signaling --- gain-of-function mutation --- tumorigenesis --- ADAM17 --- interleukin-6 --- trans-signaling --- epidermal growth factor receptor (EGF-R) --- shedding --- metalloprotease --- tumor necrosis factor alpha (TNFα) --- inflammation associated cancer --- colon cancer --- lung cancer --- SH2 domain --- mutations --- autosomal-dominant hyper IgE syndrome --- inflammatory hepatocellular adenomas --- T-cell large granular lymphocytic leukemia --- T-cell prolymphocytic leukemia --- growth hormone insensitivity syndrome --- nuclear pore complex --- nuclear transport receptors --- nucleocytoplasmic shuttling --- targeting --- tumor-associated macrophages --- adoptive T cell therapy --- immune suppression --- STAT transcription factors --- JAK --- STAT --- T-PLL --- T-cell leukemia --- meta-analysis --- STAT5B signaling --- small-molecule inhibitors --- cancer models --- companion animals --- comparative oncology --- pharmacological inhibitor --- STAT5 signaling --- chemotherapy resistance --- myeloid leukemia --- heat shock proteins --- chaperones --- stabilization --- targeted therapy --- ovarian cancer --- hematopoietic cancers --- therapeutic targeting --- pharmacological inhibitors --- mTOR --- Bone Marrow Failure Syndromes --- lymphocytes --- lymphoma --- T-cells --- RHOA --- NGS --- MPN --- JAK2 V617F --- neoplastic stem cells


Book
Marine Enzymes : Sources, Biochemistry and Bioprocesses for Marine Biotechnology
Author:
Year: 2020 Publisher: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute

Loading...
Export citation

Choose an application

Bookmark

Abstract

This book presents contributions from scientists who are directly involved in the potential of marine enzymes as useful tools in biocatalysis; the results of enzymatic bioprospecting in gross marine environments are acknowledged, including two review articles on general enzymatic processes and microalgal enzymes. In addition, studies on structural characterizations, biological functions and aspects related to the complexity of marine enzyme-based bioprocesses are discussed. Prominent conclusions by many scientists in the field of marine biotechnology emphasize that, due to marine biological diversity and the specificity of biological marine metabolisms, the study of biocatalysts on a global scale from this environment is just starting, and possesses huge potential for the development of applications with industrial benefits.

Keywords

Research & information: general --- Biology, life sciences --- metalloprotease --- adsorption analysis --- molecular docking --- affinity purification --- aminophenylboronic acid --- alginate degradation --- 4-deoxy-l-erythro-5-hexoseulose uronic acid (DEH) metabolism --- Bacteroidetes --- Proteobacteria --- Flavobacterium --- 2-keto-3-deoxy-d-gluconate (KDG) kinase --- 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase --- alginate-derived products --- marine enzymes --- biocatalysts --- bioprocesses --- biorefinery --- seafood --- marine biomarkers --- collagenase --- fermentation optimization --- collagen --- Pseudoalteromonas --- antioxidant peptides --- microcystin-degrading bacteria --- mycotoxin --- protease --- esterase --- inhibitor --- marine agent --- Catenovulum --- alkaline and cold-adapted dextranase --- isomaltoogligosaccharides --- biofilm --- dental caries --- growing cells --- resting cells --- asymmetric reduction --- marine fungi --- chiral alcohols --- alginate lyase --- marine bacterium --- Bacillus sp. Alg07 --- purification --- alginate oligosaccharides --- Vibrio weizhoudaoensis --- PL7 family --- salt-activated enzyme --- Serratia marcescens --- polyM-specific --- oligosaccharides --- Isoptericola halotolerans --- bifunctional alginate lyase --- α-d-galactosidase --- homology model --- GH 36 family --- mutation --- transglycosylation --- marine bacteria --- Pseudoalteromonas sp. KMM 701 --- leucine dehydrogenase --- cold-adapted --- Antarctic bacterium --- sea-ice --- homology modeling --- fucoidan --- endo-fucoidanase --- galactofucan --- molecular stabilisation --- Sargassum mcclurei --- Turbinaria ornata --- Alteromonas --- deep sea --- cold-adapted enzyme --- β-galactosidase --- lactose-free milk --- chitosanases --- chitin deacetylase --- deacetylation patterns --- chitooligosaccharides --- separating --- detecting --- expression --- deep-sea enzyme --- pCold vector --- Ascophyllum nodosum --- algal cell wall degrading enzymes --- enzyme-assisted extraction --- ichip device --- quorum quenching enzyme --- error prone PCR --- high-throughput screening --- site-directed mutagenesis --- catalytic ability --- Pectobacterium carotovorum subsp. carotovorum (Pcc) --- Alginate lyase --- Thermo-tolerant --- pH-stability --- Endo-manner --- Vibrio sp. SY01 --- polysaccharide lyase of family 6 --- characterization --- degradation pattern --- microalgae --- enzymes --- marine biotechnology --- -omics technologies --- heterologous expression --- homologous expression --- metalloprotease --- adsorption analysis --- molecular docking --- affinity purification --- aminophenylboronic acid --- alginate degradation --- 4-deoxy-l-erythro-5-hexoseulose uronic acid (DEH) metabolism --- Bacteroidetes --- Proteobacteria --- Flavobacterium --- 2-keto-3-deoxy-d-gluconate (KDG) kinase --- 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase --- alginate-derived products --- marine enzymes --- biocatalysts --- bioprocesses --- biorefinery --- seafood --- marine biomarkers --- collagenase --- fermentation optimization --- collagen --- Pseudoalteromonas --- antioxidant peptides --- microcystin-degrading bacteria --- mycotoxin --- protease --- esterase --- inhibitor --- marine agent --- Catenovulum --- alkaline and cold-adapted dextranase --- isomaltoogligosaccharides --- biofilm --- dental caries --- growing cells --- resting cells --- asymmetric reduction --- marine fungi --- chiral alcohols --- alginate lyase --- marine bacterium --- Bacillus sp. Alg07 --- purification --- alginate oligosaccharides --- Vibrio weizhoudaoensis --- PL7 family --- salt-activated enzyme --- Serratia marcescens --- polyM-specific --- oligosaccharides --- Isoptericola halotolerans --- bifunctional alginate lyase --- α-d-galactosidase --- homology model --- GH 36 family --- mutation --- transglycosylation --- marine bacteria --- Pseudoalteromonas sp. KMM 701 --- leucine dehydrogenase --- cold-adapted --- Antarctic bacterium --- sea-ice --- homology modeling --- fucoidan --- endo-fucoidanase --- galactofucan --- molecular stabilisation --- Sargassum mcclurei --- Turbinaria ornata --- Alteromonas --- deep sea --- cold-adapted enzyme --- β-galactosidase --- lactose-free milk --- chitosanases --- chitin deacetylase --- deacetylation patterns --- chitooligosaccharides --- separating --- detecting --- expression --- deep-sea enzyme --- pCold vector --- Ascophyllum nodosum --- algal cell wall degrading enzymes --- enzyme-assisted extraction --- ichip device --- quorum quenching enzyme --- error prone PCR --- high-throughput screening --- site-directed mutagenesis --- catalytic ability --- Pectobacterium carotovorum subsp. carotovorum (Pcc) --- Alginate lyase --- Thermo-tolerant --- pH-stability --- Endo-manner --- Vibrio sp. SY01 --- polysaccharide lyase of family 6 --- characterization --- degradation pattern --- microalgae --- enzymes --- marine biotechnology --- -omics technologies --- heterologous expression --- homologous expression


Book
Targeting STAT3 and STAT5 in Cancer
Authors: --- ---
Year: 2020 Publisher: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute

Loading...
Export citation

Choose an application

Bookmark

Abstract

Every minute, 34 new patients are diagnosed with cancer globally. Although over the past 50 years treatments have improved and survival rates have increased dramatically for several types of cancers, many remain incurable. Several aggressive types of blood and solid cancers form when mutations occur in a critical cellular signaling pathway, the JAK-STAT pathway; (Janus Kinase-Signal Transducer and Activator of Transcription). Currently, there are no clinically available drugs that target the oncogenic STAT3/5 proteins in particular or their Gain of Function hyperactive mutant products. Here, we summarize targeting approaches on STAT3/5, as the field moves towards clinical applications as well as we illuminate on upstream or downstream JAK-STAT pathway interference with kinase inhibitors, heat shock protein blockers or changing nuclear import/export processes. We cover the design paradigms and medicinal chemistry approaches to illuminate progress and challenges in understanding the pleiotropic role of STAT3 and STAT5 in oncogenesis, the microenvironment, the immune system in particular, all culminating in a complex interplay towards cancer progression.

Keywords

multiple myeloma --- STAT3 --- S3I-1757 --- nanoparticle --- CD38 --- siRNA/RNAi --- polyethylenimine --- PEI --- lipopolyplex --- siRNA delivery --- glioma --- glioblastoma --- STAT5 --- AKT --- ERK1/2 --- prolactin --- androgens --- prostate cancer --- knockout --- escape mechanisms --- stem/progenitor cells --- cell hierarchy --- cancer --- CD4+ T cells --- CD8+ T cells --- myeloid cells --- immune check point --- hepatitis C virus (HCV) --- cirrhosis --- hepatocellular carcinoma (HCC) --- endoplasmic reticulum (ER) stress --- oxidative stress (OS) --- unfolded protein response (UPR) --- microRNA-122 (miR-122) --- nuclear factor erythroid 2-related factor 2 (NRF2) --- signal transducer and activator of transcription 3 (STAT3) --- hepatocyte nuclear factor 4 alpha (HNF4A) --- solid cancers --- cell cycle --- apoptosis --- inflammation --- mitochondria --- stemness --- tumor suppression --- melanoma --- autoimmune disease --- immunotherapy --- tumor–immune cell interactions --- breast cancer --- PD-L1 --- M2 macrophages --- NK cells --- STAT3 inhibitor XIII --- hedging --- transaction costs --- dynamic programming --- risk management --- post-decision state variable --- cancer progression --- cancer-stem cell --- cytokine --- therapy resistance --- metastasis --- immunosuppression --- tumor microenvironment --- proliferation --- tyrosine kinase 2 --- JAK family of protein tyrosine kinases --- signal transducer and activator of transcription --- cytokine receptor signaling --- gain-of-function mutation --- tumorigenesis --- ADAM17 --- interleukin-6 --- trans-signaling --- epidermal growth factor receptor (EGF-R) --- shedding --- metalloprotease --- tumor necrosis factor alpha (TNFα) --- inflammation associated cancer --- colon cancer --- lung cancer --- SH2 domain --- mutations --- autosomal-dominant hyper IgE syndrome --- inflammatory hepatocellular adenomas --- T-cell large granular lymphocytic leukemia --- T-cell prolymphocytic leukemia --- growth hormone insensitivity syndrome --- nuclear pore complex --- nuclear transport receptors --- nucleocytoplasmic shuttling --- targeting --- tumor-associated macrophages --- adoptive T cell therapy --- immune suppression --- STAT transcription factors --- JAK --- STAT --- T-PLL --- T-cell leukemia --- meta-analysis --- STAT5B signaling --- small-molecule inhibitors --- cancer models --- companion animals --- comparative oncology --- pharmacological inhibitor --- STAT5 signaling --- chemotherapy resistance --- myeloid leukemia --- heat shock proteins --- chaperones --- stabilization --- targeted therapy --- ovarian cancer --- hematopoietic cancers --- therapeutic targeting --- pharmacological inhibitors --- mTOR --- Bone Marrow Failure Syndromes --- lymphocytes --- lymphoma --- T-cells --- RHOA --- NGS --- MPN --- JAK2 V617F --- neoplastic stem cells --- n/a --- tumor-immune cell interactions

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