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Cellular and Molecular Life Sciences, ISSN 1420-682X, 1/2011, Volume 68, Issue 2, pp. 169 - 184
Spider dragline silk is an outstanding material made up of unique proteins—spidroins. Analysis of the amino acid sequences of full-length spidroins reveals a... 
Life Sciences | Biochemistry, general | Recombinant protein production | Protein self-assembly | Life Sciences, general | Spidroin | Biocompatibility | Biomaterial | Protein structure | Biomedicine general | Cell Biology | MAJOR AMPULLATE SILK | BIOCHEMISTRY & MOLECULAR BIOLOGY | BLACK-WIDOW SPIDER | MECHANICAL-PROPERTIES | CELL BIOLOGY | FIBROIN GENE FAMILY | CLAVIPES DRAGLINE SILK | FIBER FORMATION | LATRODECTUS-HESPERUS | NEPHILA-CLAVIPES | CONSERVED C-TERMINI | EGG CASE SILK | Protein Structure, Tertiary | Amino Acid Sequence | Fibroins - chemistry | Humans | Recombinant Fusion Proteins - physiology | Fibroins - genetics | Molecular Sequence Data | Structure-Activity Relationship | Recombinant Fusion Proteins - chemistry | Regenerative Medicine | Fibroins - physiology | Animals | Spiders | Plants, Genetically Modified | Recombinant Fusion Proteins - genetics | Biocompatible Materials | Sequence Analysis | Physiological aspects | Biological products | Glycine | Recombinant proteins | Polyamides | Biomedical engineering | Proteins | Biomedical materials | Molecular biology | Crystal structure | Biological Sciences | Tertiary | Plants | Protein Structure | Recombinant Fusion Proteins/chemistry/genetics/physiology | Naturvetenskap | Genetically Modified | Biokemi och molekylärbiologi | Biologiska vetenskaper | Fibroins/chemistry/genetics/physiology | Biochemistry and Molecular Biology | Natural Sciences
Journal Article
Chemical Communications, ISSN 1359-7345, 2009, Issue 43, pp. 6515 - 6529
Journal Article
Biomacromolecules, ISSN 1525-7797, 07/2018, Volume 19, Issue 7, pp. 2825 - 2833
Journal Article
Biotechnology Advances, ISSN 0734-9750, 09/2019, Volume 37, Issue 5, pp. 642 - 666
Materials science and genetic engineering have joined forces over the last three decades in the development of so-called protein-based polymers. These are... 
Silk | Self-assembly | Proteolysis | Gelatin | Collagen | Elastin | Protein expression | Pichia pastoris | Protein-based polymers | Block copolymers | ALPHA-FACTOR | SELF-ASSEMBLING PEPTIDES | RECOMBINANT SPIDER SILK | RECURSIVE DIRECTIONAL LIGATION | SACCHAROMYCES-CEREVISIAE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | NONCANONICAL AMINO-ACIDS | HETEROLOGOUS PROTEINS | ELASTIN-LIKE RECOMBINAMERS | CELL-WALL POROSITY | INVERSE TEMPERATURE TRANSITION | Recombinant Proteins - metabolism | Silk - genetics | Pichia - metabolism | Protein Engineering - methods | Pichia - genetics | Silk - metabolism | Industrial Microbiology - methods | Recombinant Proteins - genetics | Phosphates | Oxidases | Medical research | Usage | Phosphatases | Peptides | Escherichia coli | Amino acids | Genetically modified organisms | Medicine, Experimental | Genetic engineering | Protein binding | Self assembly | Bioprocessing | Yeast | Materials science | Nanomaterials | Biosynthesis | Physical properties | Functional materials | Proteins | Biomedical materials | E coli | Bioreactors | Polymers | Deoxyribonucleic acid--DNA | Recombinant | ELP, elastin-like polypeptide | BiP, immunoglobulin-binding protein | ppαF, Saccharomyces cerevisiae α-factor mating pheromone prepro peptide | ECM, extracellular matrix | MaSp1, major ampullate spidroin 1 | DPAPase A, dipeptidyl aminopeptidase A | AOX1, alcohol oxidase 1 | GRAS, generally recognized as safe | PDI, protein disulfide isomerase | MaSp2, major ampullate spidroin 2 | UPR, unfolded protein response | ERAD, ER-associated degradation | Pho1, acid phosphatase | P4H, peptidyl-prolyl-4-hydroxylase | OD600, optical density at 600 nm | EBP, elastin-binding protein | ITC, inverse transition cycling | FDA, food and drug administration | his4, histidinol dehydrogenase | LCST, lower critical solution temperature | GAP, glyceraldehyde-3-phosphate dehydrogenase
Journal Article