Acta Veterinaria Scandinavica, ISSN 0044-605X, 01/2019, Volume 61, Issue 1, pp. 3 - 8
BackgroundHand-sewn intestinal anastomoses are a fundamental procedure in both open and laparoscopic intestinal surgery. Self-retaining barbed suture devices...
Pigs | Jejunojejunal | Barbed suture | End-to-end anastomosis | IN-VIVO ASSESSMENT | CLOSURE DEVICE | VETERINARY SCIENCES | EXPERIENCE | ADHESION FORMATION | Usage | Neovascularization | Comparative analysis | Penicillin G | Anastomosis | Systematic review | Laparoscopy | Adhesion | Vascularization | Abdomen | Animals | Histopathology | Intestine | Swine | Collagen | Surgery | Bursting pressure | Sutures | Horses | Gastrointestinal surgery | Bursting
Pigs | Jejunojejunal | Barbed suture | End-to-end anastomosis | IN-VIVO ASSESSMENT | CLOSURE DEVICE | VETERINARY SCIENCES | EXPERIENCE | ADHESION FORMATION | Usage | Neovascularization | Comparative analysis | Penicillin G | Anastomosis | Systematic review | Laparoscopy | Adhesion | Vascularization | Abdomen | Animals | Histopathology | Intestine | Swine | Collagen | Surgery | Bursting pressure | Sutures | Horses | Gastrointestinal surgery | Bursting
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 10/2011, Volume 286, Issue 40, pp. 35119 - 35128
IQGAP1 is a large modular protein that displays multiple partnership and is thought to act as a scaffold in coupling cell signaling to the actin and...
ACTOMYOSIN RING | SHIGELLA-FLEXNERI | F-ACTIN | HOMOLOGY DOMAIN | STRUCTURAL BASIS | ENTEROPATHOGENIC ESCHERICHIA-COLI | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | N-WASP | PEDESTAL FORMATION | INTEGRATES CA2+/CALMODULIN | Protein Structure, Tertiary | ras GTPase-Activating Proteins - metabolism | Calmodulin - metabolism | Signal Transduction | Humans | Actins - metabolism | Solubility | Recombinant Proteins - chemistry | cdc42 GTP-Binding Protein - metabolism | Adenosine Diphosphate - chemistry | Point Mutation | Protein Binding | Kinetics | Wiskott-Aldrich Syndrome Protein, Neuronal - metabolism | DNA, Complementary - metabolism | Cell Movement | Actin | Cell Motility | Barbed End Capping | IQGAP1 | Enzymology | Calmodulin | Cdc42
ACTOMYOSIN RING | SHIGELLA-FLEXNERI | F-ACTIN | HOMOLOGY DOMAIN | STRUCTURAL BASIS | ENTEROPATHOGENIC ESCHERICHIA-COLI | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | N-WASP | PEDESTAL FORMATION | INTEGRATES CA2+/CALMODULIN | Protein Structure, Tertiary | ras GTPase-Activating Proteins - metabolism | Calmodulin - metabolism | Signal Transduction | Humans | Actins - metabolism | Solubility | Recombinant Proteins - chemistry | cdc42 GTP-Binding Protein - metabolism | Adenosine Diphosphate - chemistry | Point Mutation | Protein Binding | Kinetics | Wiskott-Aldrich Syndrome Protein, Neuronal - metabolism | DNA, Complementary - metabolism | Cell Movement | Actin | Cell Motility | Barbed End Capping | IQGAP1 | Enzymology | Calmodulin | Cdc42
Journal Article
Journal of Cell Science, ISSN 0021-9533, 2016, Volume 129, Issue 6, pp. 1085 - 1091
Cells respond to external stimuli by rapidly remodeling their actin cytoskeleton. At the heart of this function lies the intricately controlled regulation of...
Motility | Filament barbed end | Profilin | Actin assembly | Formin | Capping protein | WH2 DOMAINS | ARP2/3 COMPLEX | CELL BIOLOGY | CAPPING PROTEIN FUNCTION | CELL-MIGRATION | IN-VIVO | DYNAMICS | NUCLEATION | FORMIN MDIA1 | Actin Cytoskeleton - metabolism | Animals | Humans | Actins - metabolism | Cytoskeleton - genetics | Cytoskeleton - metabolism | Actin Cytoskeleton - genetics | Actins - genetics | Life Sciences
Motility | Filament barbed end | Profilin | Actin assembly | Formin | Capping protein | WH2 DOMAINS | ARP2/3 COMPLEX | CELL BIOLOGY | CAPPING PROTEIN FUNCTION | CELL-MIGRATION | IN-VIVO | DYNAMICS | NUCLEATION | FORMIN MDIA1 | Actin Cytoskeleton - metabolism | Animals | Humans | Actins - metabolism | Cytoskeleton - genetics | Cytoskeleton - metabolism | Actin Cytoskeleton - genetics | Actins - genetics | Life Sciences
Journal Article
Current Biology, ISSN 0960-9822, 07/2017, Volume 27, Issue 13, pp. 1956 - 1967.e7
Actin-depolymerizing factor (ADF)/cofilins contribute to cytoskeletal dynamics by promoting rapid actin filament disassembly. In the classical view,...
non-muscle actin | actin-depolymerizing factor | cofilin | barbed-end depolymerization | actin dynamics | capping protein | microfluidics | single filaments | F-ACTIN | SKELETAL-MUSCLE | NETWORK | TURNOVER | CELL MOTILITY | BARBED ENDS | BIOCHEMISTRY & MOLECULAR BIOLOGY | COFILIN INCREASES | PROFILIN | ARP2/3 COMPLEX | CAPPING PROTEIN | CELL BIOLOGY | Rabbits | Actin Cytoskeleton - metabolism | Humans | Actins - metabolism | Polymerization | Cofilin 1 - genetics | Cofilin 2 - metabolism | Animals | Cofilin 1 - metabolism | Cattle | Cofilin 2 - genetics | Destrin - genetics | Destrin - metabolism | Muscles | Muscle proteins | Actin | Microfluidics
non-muscle actin | actin-depolymerizing factor | cofilin | barbed-end depolymerization | actin dynamics | capping protein | microfluidics | single filaments | F-ACTIN | SKELETAL-MUSCLE | NETWORK | TURNOVER | CELL MOTILITY | BARBED ENDS | BIOCHEMISTRY & MOLECULAR BIOLOGY | COFILIN INCREASES | PROFILIN | ARP2/3 COMPLEX | CAPPING PROTEIN | CELL BIOLOGY | Rabbits | Actin Cytoskeleton - metabolism | Humans | Actins - metabolism | Polymerization | Cofilin 1 - genetics | Cofilin 2 - metabolism | Animals | Cofilin 1 - metabolism | Cattle | Cofilin 2 - genetics | Destrin - genetics | Destrin - metabolism | Muscles | Muscle proteins | Actin | Microfluidics
Journal Article
Experimental Cell Research, ISSN 0014-4827, 08/2017, Volume 357, Issue 2, pp. 163 - 169
Formins are multi domain proteins present ubiquitously in all eukaryotes from lower fungi to higher vertebrates. Formins are characterized by the presence of...
Delphilin | Expression | Formin | Actin and barbed end capping | MECHANISM | FH2 DOMAIN | PROFILIN | ARP2/3 COMPLEX | POLYMERIZATION | BNI1 | BINDING PROTEIN | CELL BIOLOGY | WASP/SCAR PROTEINS | ONCOLOGY | NUCLEATION | ASSOCIATION | Nerve Tissue Proteins - metabolism | Protein Structure, Tertiary | Actin Cytoskeleton - metabolism | Animals | Humans | Actins - metabolism | Nuclear Proteins - metabolism | Fetal Proteins - metabolism | Mice | Microfilament Proteins - metabolism | CapZ Actin Capping Protein - metabolism | Muscle proteins | Actin | Sciences education
Delphilin | Expression | Formin | Actin and barbed end capping | MECHANISM | FH2 DOMAIN | PROFILIN | ARP2/3 COMPLEX | POLYMERIZATION | BNI1 | BINDING PROTEIN | CELL BIOLOGY | WASP/SCAR PROTEINS | ONCOLOGY | NUCLEATION | ASSOCIATION | Nerve Tissue Proteins - metabolism | Protein Structure, Tertiary | Actin Cytoskeleton - metabolism | Animals | Humans | Actins - metabolism | Nuclear Proteins - metabolism | Fetal Proteins - metabolism | Mice | Microfilament Proteins - metabolism | CapZ Actin Capping Protein - metabolism | Muscle proteins | Actin | Sciences education
Journal Article
Biophysical Journal, ISSN 0006-3495, 2004, Volume 87, Issue 4, pp. 2838 - 2854
Force generation in several types of cell motility is driven by rapidly elongating cytoskeletal filaments that are persistently tethered at their polymerizing...
LISTERIA-MONOCYTOGENES | BARBED-END | COMET TAILS | BIOPHYSICS | APC PROTEIN | MICROTUBULES | ENA/VASP FAMILY | LIPID VESICLES | PROFILIN | ACTIN-BASED MOTILITY | POLYMERIZATION | Models, Chemical | Humans | Stress, Mechanical | Molecular Motor Proteins - chemistry | Adenosine Diphosphate - physiology | Cell Movement - physiology | Molecular Motor Proteins - physiology | Hydrolysis | Animals | Energy Transfer - physiology | Models, Biological | Computer Simulation | Actins - chemistry | Cytoskeleton - physiology | Adenosine Triphosphate - physiology | Actins - physiology | Cytoskeleton - chemistry | Proteins | Thermodynamics | Analysis | Polymerization | Parameter estimation | Biochemistry | Kinetics | Cell Biophysics
LISTERIA-MONOCYTOGENES | BARBED-END | COMET TAILS | BIOPHYSICS | APC PROTEIN | MICROTUBULES | ENA/VASP FAMILY | LIPID VESICLES | PROFILIN | ACTIN-BASED MOTILITY | POLYMERIZATION | Models, Chemical | Humans | Stress, Mechanical | Molecular Motor Proteins - chemistry | Adenosine Diphosphate - physiology | Cell Movement - physiology | Molecular Motor Proteins - physiology | Hydrolysis | Animals | Energy Transfer - physiology | Models, Biological | Computer Simulation | Actins - chemistry | Cytoskeleton - physiology | Adenosine Triphosphate - physiology | Actins - physiology | Cytoskeleton - chemistry | Proteins | Thermodynamics | Analysis | Polymerization | Parameter estimation | Biochemistry | Kinetics | Cell Biophysics
Journal Article
Current Biology, ISSN 0960-9822, 12/2014, Volume 24, Issue 23, pp. 2749 - 2757
Depolymerization of actin filaments is vital for the morphogenesis of dynamic cytoskeletal arrays and actin-dependent cell motility. Cofilin is necessary for...
INTERACTING PROTEIN-1 UNC-78 | F-ACTIN | BARBED-END | TURNOVER | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | ADF/COFILIN | POLYMERIZATION | DEPOLYMERIZING FACTOR/COFILIN | FRAGMENTATION | BINDING | CELL BIOLOGY | Actin Depolymerizing Factors - pharmacology | Actin Cytoskeleton - metabolism | Actin Depolymerizing Factors - genetics | Humans | Tissue Extracts - pharmacology | CapZ Actin Capping Protein - pharmacology | Actin Depolymerizing Factors - metabolism | Thymus Gland - chemistry | Animals | Actin Cytoskeleton - drug effects | Cattle | Fluorescence Resonance Energy Transfer | Cytosol - metabolism | Thymocytes - cytology | Muscle proteins | Actin
INTERACTING PROTEIN-1 UNC-78 | F-ACTIN | BARBED-END | TURNOVER | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | ADF/COFILIN | POLYMERIZATION | DEPOLYMERIZING FACTOR/COFILIN | FRAGMENTATION | BINDING | CELL BIOLOGY | Actin Depolymerizing Factors - pharmacology | Actin Cytoskeleton - metabolism | Actin Depolymerizing Factors - genetics | Humans | Tissue Extracts - pharmacology | CapZ Actin Capping Protein - pharmacology | Actin Depolymerizing Factors - metabolism | Thymus Gland - chemistry | Animals | Actin Cytoskeleton - drug effects | Cattle | Fluorescence Resonance Energy Transfer | Cytosol - metabolism | Thymocytes - cytology | Muscle proteins | Actin
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 09/2001, Volume 312, Issue 4, pp. 721 - 730
We investigated the effect of actin filament length and capping protein on the rate of end-to-end annealing of actin filaments. Long filaments were fragmented...
actin | capping protein | polymer dynamics | annealing | Polymer dynamics | Annealing | Actin | Capping protein | F-ACTIN | COMPLEX | BARBED ENDS | BIOCHEMISTRY & MOLECULAR BIOLOGY | LENGTH | POLYMERIZATION | ADP-ACTIN | ADF/COFILIN | ATP | BINDING | Biopolymers - chemistry | Rabbits | Actin Cytoskeleton - metabolism | Actins - metabolism | Actin Cytoskeleton - chemistry | Actin Depolymerizing Factors | Fluorometry | Biopolymers - metabolism | Animals | Microscopy | Protein Structure, Quaternary | Actins - chemistry | Protein Binding | Destrin | Microfilament Proteins - metabolism | Kinetics
actin | capping protein | polymer dynamics | annealing | Polymer dynamics | Annealing | Actin | Capping protein | F-ACTIN | COMPLEX | BARBED ENDS | BIOCHEMISTRY & MOLECULAR BIOLOGY | LENGTH | POLYMERIZATION | ADP-ACTIN | ADF/COFILIN | ATP | BINDING | Biopolymers - chemistry | Rabbits | Actin Cytoskeleton - metabolism | Actins - metabolism | Actin Cytoskeleton - chemistry | Actin Depolymerizing Factors | Fluorometry | Biopolymers - metabolism | Animals | Microscopy | Protein Structure, Quaternary | Actins - chemistry | Protein Binding | Destrin | Microfilament Proteins - metabolism | Kinetics
Journal Article
The EMBO Journal, ISSN 0261-4189, 04/2011, Volume 30, Issue 7, pp. 1230 - 1237
The actin filament has clear polarity where one end, the pointed end, has a much slower polymerization and depolymerization rate than the other end, the barbed...
cryo‐electron microscopy | single particle analysis | cytoskeleton | motor protein | actin filament | cryo-electron microscopy | SYSTEM | BARBED-END | COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | LAMELLIPODIA | POLYMERIZATION | MICROSCOPY | CELL BIOLOGY | ATP HYDROLYSIS | ADP-ACTIN | CAPZ | Cryoelectron Microscopy | Rabbits | Actin Cytoskeleton - metabolism | Animals | Protein Multimerization | Actin Cytoskeleton - chemistry | Models, Molecular | Kinetics | Actin Cytoskeleton - ultrastructure | Polymerization | Cells
cryo‐electron microscopy | single particle analysis | cytoskeleton | motor protein | actin filament | cryo-electron microscopy | SYSTEM | BARBED-END | COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | LAMELLIPODIA | POLYMERIZATION | MICROSCOPY | CELL BIOLOGY | ATP HYDROLYSIS | ADP-ACTIN | CAPZ | Cryoelectron Microscopy | Rabbits | Actin Cytoskeleton - metabolism | Animals | Protein Multimerization | Actin Cytoskeleton - chemistry | Models, Molecular | Kinetics | Actin Cytoskeleton - ultrastructure | Polymerization | Cells
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Tropomyosin Regulates Elongation by Formin at the Fast-Growing End of the Actin Filament
Biochemistry, ISSN 0006-2960, 07/2007, Volume 46, Issue 27, pp. 8146 - 8155
The balance between dynamic and stable actin filaments is essential for the regulation of cellular functions including the determination of cell shape and...
BARBED-END | F-ACTIN | SKELETAL-MUSCLE | CIRCULAR-DICHROISM | CAPPING-PROTEIN-BETA | STRUCTURAL BASIS | MUSCLE ALPHA-TROPOMYOSIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | HOMOLOGY-2 DOMAIN | ENA/VASP PROTEINS | CARBOXYL-TERMINUS | Tropomyosin - physiology | Animals | Chickens | Fetal Proteins - physiology | Microfilament Proteins - physiology | Nuclear Proteins - physiology | Actins - physiology | Circular Dichroism
BARBED-END | F-ACTIN | SKELETAL-MUSCLE | CIRCULAR-DICHROISM | CAPPING-PROTEIN-BETA | STRUCTURAL BASIS | MUSCLE ALPHA-TROPOMYOSIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | HOMOLOGY-2 DOMAIN | ENA/VASP PROTEINS | CARBOXYL-TERMINUS | Tropomyosin - physiology | Animals | Chickens | Fetal Proteins - physiology | Microfilament Proteins - physiology | Nuclear Proteins - physiology | Actins - physiology | Circular Dichroism
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/1998, Volume 95, Issue 11, pp. 6181 - 6186
The Arp2/3 complex is a stable assembly of seven protein subunits including two actin-related proteins (Arp2 and Arp3) and five novel proteins. Previous work...
Nuclear models | Cell motility | Nucleation | Microfilaments | Actins | Polymerization | Dimers | Kinetics | Monomers | Cells | ACANTHAMOEBA-CASTELLANII | PROTEIN | CYTOSKELETON | BARBED ENDS | KINETICS | ELONGATION | MULTIDISCIPLINARY SCIENCES | RATE CONSTANTS | PURIFICATION | PROFILIN | POLYMERIZATION | Usage | Cytoplasmic filaments | Actin | Analysis | Research | Electron microscopy | Arp2/3 protein
Nuclear models | Cell motility | Nucleation | Microfilaments | Actins | Polymerization | Dimers | Kinetics | Monomers | Cells | ACANTHAMOEBA-CASTELLANII | PROTEIN | CYTOSKELETON | BARBED ENDS | KINETICS | ELONGATION | MULTIDISCIPLINARY SCIENCES | RATE CONSTANTS | PURIFICATION | PROFILIN | POLYMERIZATION | Usage | Cytoplasmic filaments | Actin | Analysis | Research | Electron microscopy | Arp2/3 protein
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12.
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The availability of filament ends modulates actin stochastic dynamics in live plant cells
Molecular Biology of the Cell, ISSN 1059-1524, 04/2014, Volume 25, Issue 8, pp. 1263 - 1275
A network of individual filaments that undergoes incessant remodeling through a process known as stochastic dynamics comprises the cortical actin cytoskeleton...
LATRUNCULIN B | F-ACTIN | ARABIDOPSIS-THALIANA | CELLULOSE SYNTHASE | BARBED ENDS | PHOSPHATIDIC-ACID | PHYSCOMITRELLA-PATENS | CAPPING PROTEIN | PLASMA-MEMBRANE | CORTICAL ARRAY | CELL BIOLOGY | Actin Cytoskeleton - metabolism | Plant Roots - metabolism | Arabidopsis - growth & development | Hypocotyl - cytology | Plant Roots - cytology | Actin Capping Proteins - genetics | Plant Cells | Plant Epidermis - metabolism | Arabidopsis - metabolism | Actin Capping Proteins - biosynthesis | Image Processing, Computer-Assisted | Stochastic Processes | Plant Epidermis - cytology | Microfilament Proteins - metabolism | Life Sciences | Cellular Biology
LATRUNCULIN B | F-ACTIN | ARABIDOPSIS-THALIANA | CELLULOSE SYNTHASE | BARBED ENDS | PHOSPHATIDIC-ACID | PHYSCOMITRELLA-PATENS | CAPPING PROTEIN | PLASMA-MEMBRANE | CORTICAL ARRAY | CELL BIOLOGY | Actin Cytoskeleton - metabolism | Plant Roots - metabolism | Arabidopsis - growth & development | Hypocotyl - cytology | Plant Roots - cytology | Actin Capping Proteins - genetics | Plant Cells | Plant Epidermis - metabolism | Arabidopsis - metabolism | Actin Capping Proteins - biosynthesis | Image Processing, Computer-Assisted | Stochastic Processes | Plant Epidermis - cytology | Microfilament Proteins - metabolism | Life Sciences | Cellular Biology
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Molecular basis for barbed end uncapping by CARMIL homology domain 3 of mouse CARMIL-1
Journal of Biological Chemistry, ISSN 0021-9258, 09/2010, Volume 285, Issue 37, pp. 29014 - 29026
Capping protein (CP) is a ubiquitously expressed, 62-kDa heterodimer that binds the barbed end of the actin filament with similar to 0.1 nM affinity to prevent...
ACTIN-CAPPING PROTEIN | STRUCTURAL BASIS | CELL MORPHOLOGY | NMR CHEMICAL-SHIFTS | MYOSIN-I | BIOCHEMISTRY & MOLECULAR BIOLOGY | MULTIDIMENSIONAL NMR | ARP2/3 COMPLEX | IDENTIFICATION | BINDING SITE | FILAMENT NUCLEATION | Actin Capping Proteins - metabolism | Protein Structure, Tertiary | Mutagenesis, Site-Directed | Actin Capping Proteins - chemistry | Actin Capping Proteins - genetics | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Microfilament Proteins | Surface Properties | Protein Structure, Quaternary | Protein Binding | Carrier Proteins - chemistry | Mice | Index Medicus | NMR | CARMIL | Molecular Biophysics | Actin | Cytoskeleton | Biophysics | Barbed Ends | Capping Protein | Cell Biology | Protein-Protein Interactions
ACTIN-CAPPING PROTEIN | STRUCTURAL BASIS | CELL MORPHOLOGY | NMR CHEMICAL-SHIFTS | MYOSIN-I | BIOCHEMISTRY & MOLECULAR BIOLOGY | MULTIDIMENSIONAL NMR | ARP2/3 COMPLEX | IDENTIFICATION | BINDING SITE | FILAMENT NUCLEATION | Actin Capping Proteins - metabolism | Protein Structure, Tertiary | Mutagenesis, Site-Directed | Actin Capping Proteins - chemistry | Actin Capping Proteins - genetics | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Microfilament Proteins | Surface Properties | Protein Structure, Quaternary | Protein Binding | Carrier Proteins - chemistry | Mice | Index Medicus | NMR | CARMIL | Molecular Biophysics | Actin | Cytoskeleton | Biophysics | Barbed Ends | Capping Protein | Cell Biology | Protein-Protein Interactions
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 10/2003, Volume 278, Issue 41, pp. 40000 - 40009
Tropomodulin 1 (Tmod1) is a â¼40-kDa tropomyosin binding and actin filament pointed end-capping protein that regulates pointed end dynamics and controls thin...
TROPOMYOSIN-BINDING PROTEIN | SKELETAL-MUSCLE | THIN-FILAMENTS | STRUCTURAL BASIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RATE CONSTANTS | ADP-ACTIN | ISOFORM | IDENTIFICATION | BARBED END | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Rabbits | Peptide Fragments - metabolism | Gelsolin - metabolism | Actins - metabolism | Molecular Sequence Data | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Binding Sites - genetics | Carrier Proteins - genetics | Peptide Fragments - chemistry | Animals | Carrier Proteins - metabolism | Microfilament Proteins | Chickens | Actins - chemistry | Tropomodulin | Carrier Proteins - chemistry | Kinetics | In Vitro Techniques | Peptide Fragments - genetics | Tropomyosin - metabolism
TROPOMYOSIN-BINDING PROTEIN | SKELETAL-MUSCLE | THIN-FILAMENTS | STRUCTURAL BASIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RATE CONSTANTS | ADP-ACTIN | ISOFORM | IDENTIFICATION | BARBED END | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Rabbits | Peptide Fragments - metabolism | Gelsolin - metabolism | Actins - metabolism | Molecular Sequence Data | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Binding Sites - genetics | Carrier Proteins - genetics | Peptide Fragments - chemistry | Animals | Carrier Proteins - metabolism | Microfilament Proteins | Chickens | Actins - chemistry | Tropomodulin | Carrier Proteins - chemistry | Kinetics | In Vitro Techniques | Peptide Fragments - genetics | Tropomyosin - metabolism
Journal Article