Costameres: STRIATED MUSCLE cell components which anchor the MYOFIBRILS from the Z-bands to the SARCOLEMMA and EXTRACELLULAR MATRIX. Costameric proteins include the proteins of FOCAL ADHESIONS.Rodenticides: Substances used to destroy or inhibit the action of rats, mice, or other rodents.Rodent Control: The reduction or regulation of the population of noxious, destructive, or dangerous rodents through chemical, biological, or other means.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Rodent Diseases: Diseases of rodents of the order RODENTIA. This term includes diseases of Sciuridae (squirrels), Geomyidae (gophers), Heteromyidae (pouched mice), Castoridae (beavers), Cricetidae (rats and mice), Muridae (Old World rats and mice), Erethizontidae (porcupines), and Caviidae (guinea pigs).Ankyrin Repeat: Protein motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating sequence of 33-amino acids was discovered in ANKYRIN where it is involved in interaction with the anion exchanger (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE). Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions.4-Hydroxycoumarins: Substances found in many plants, containing the 4-hydroxycoumarin radical. They interfere with vitamin K and the blood clotting mechanism, are tightly protein-bound, inhibit mitochondrial and microsomal enzymes, and are used as oral anticoagulants.Ankyrins: A family of membrane-associated proteins responsible for the attachment of the cytoskeleton. Erythrocyte-related isoforms of ankyrin attach the SPECTRIN cytoskeleton to a transmembrane protein (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE) in the erythrocyte plasma membrane. Brain-related isoforms of ankyrin also exist.Cell Polarity: Orientation of intracellular structures especially with respect to the apical and basolateral domains of the plasma membrane. Polarized cells must direct proteins from the Golgi apparatus to the appropriate domain since tight junctions prevent proteins from diffusing between the two domains.Cytoskeleton: The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.Dictionaries, MedicalAnkyrin Repeat: Protein motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating sequence of 33-amino acids was discovered in ANKYRIN where it is involved in interaction with the anion exchanger (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE). Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions.Dictionaries as Topic: Lists of words, usually in alphabetical order, giving information about form, pronunciation, etymology, grammar, and meaning.Ankyrins: A family of membrane-associated proteins responsible for the attachment of the cytoskeleton. Erythrocyte-related isoforms of ankyrin attach the SPECTRIN cytoskeleton to a transmembrane protein (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE) in the erythrocyte plasma membrane. Brain-related isoforms of ankyrin also exist.Anion Exchange Protein 1, Erythrocyte: A major integral transmembrane protein of the ERYTHROCYTE MEMBRANE. It is the anion exchanger responsible for electroneutral transporting in CHLORIDE IONS in exchange of BICARBONATE IONS allowing CO2 uptake and transport from tissues to lungs by the red blood cells. Genetic mutations that result in a loss of the protein function have been associated with type 4 HEREDITARY SPHEROCYTOSIS.SLC4A Proteins: Bicarbonate transporters that move BICARBONATE IONS in exchange of CHLORIDE IONS or SODIUM IONS across membranes. They regulate acid-base HOMEOSTASIS, cell volume and intracellular pH. Members include CHLORIDE-BICARBONATE ANTIPORTERS (SLC4A1, 2, 3, and 9); SODIUM-COUPLED BICARBONATE TRANSPORTERS (SLC4A4 and 5, 7, 8 and 10); and a sodium borate cotransporter (SLC4A11 protein).Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Anion Transport Proteins: Membrane proteins whose primary function is to facilitate the transport of negatively charged molecules (anions) across a biological membrane.Antiporters: Membrane transporters that co-transport two or more dissimilar molecules in the opposite direction across a membrane. Usually the transport of one ion or molecule is against its electrochemical gradient and is "powered" by the movement of another ion or molecule with its electrochemical gradient.Ankyrin Repeat: Protein motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating sequence of 33-amino acids was discovered in ANKYRIN where it is involved in interaction with the anion exchanger (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE). Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions.Bryopsida: A class of plants within the Bryophyta comprising the mosses, which are found in both damp (including freshwater) and drier situations. Mosses possess erect or prostrate leafless stems, which give rise to leafless stalks bearing capsules. Spores formed in the capsules are released and grow to produce new plants. (Concise Dictionary of Biology, 1990). Many small plants bearing the name moss are in fact not mosses. The "moss" found on the north side of trees is actually a green alga (CHLOROPHYTA). Irish moss is really a red alga (RHODOPHYTA). Beard lichen (beard moss), Iceland moss, oak moss, and reindeer moss are actually LICHENS. Spanish moss is a common name for both LICHENS and an air plant (TILLANDSIA usneoides) of the pineapple family. Club moss is an evergreen herb of the family LYCOPODIACEAE.Periodicals as Topic: A publication issued at stated, more or less regular, intervals.Access to Information: Individual's rights to obtain and use information collected or generated by others.Journal Impact Factor: A quantitative measure of the frequency on average with which articles in a journal have been cited in a given period of time.Bibliometrics: The use of statistical methods in the analysis of a body of literature to reveal the historical development of subject fields and patterns of authorship, publication, and use. Formerly called statistical bibliography. (from The ALA Glossary of Library and Information Science, 1983)Publishing: "The business or profession of the commercial production and issuance of literature" (Webster's 3d). It includes the publisher, publication processes, editing and editors. Production may be by conventional printing methods or by electronic publishing.Ankyrins: A family of membrane-associated proteins responsible for the attachment of the cytoskeleton. Erythrocyte-related isoforms of ankyrin attach the SPECTRIN cytoskeleton to a transmembrane protein (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE) in the erythrocyte plasma membrane. Brain-related isoforms of ankyrin also exist.Peer Review, Research: The evaluation by experts of the quality and pertinence of research or research proposals of other experts in the same field. Peer review is used by editors in deciding which submissions warrant publication, by granting agencies to determine which proposals should be funded, and by academic institutions in tenure decisions.Bryophyta: A division of the plant kingdom. Bryophyta contains the subdivision, Musci, which contains the classes: Andreaeopsida, BRYOPSIDA, and SPHAGNOPSIDA.Ankyrin Repeat: Protein motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating sequence of 33-amino acids was discovered in ANKYRIN where it is involved in interaction with the anion exchanger (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE). Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions.Ankyrins: A family of membrane-associated proteins responsible for the attachment of the cytoskeleton. Erythrocyte-related isoforms of ankyrin attach the SPECTRIN cytoskeleton to a transmembrane protein (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE) in the erythrocyte plasma membrane. Brain-related isoforms of ankyrin also exist.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Muridae: A family of the order Rodentia containing 250 genera including the two genera Mus (MICE) and Rattus (RATS), from which the laboratory inbred strains are developed. The fifteen subfamilies are SIGMODONTINAE (New World mice and rats), CRICETINAE, Spalacinae, Myospalacinae, Lophiomyinae, ARVICOLINAE, Platacanthomyinae, Nesomyinae, Otomyinae, Rhizomyinae, GERBILLINAE, Dendromurinae, Cricetomyinae, MURINAE (Old World mice and rats), and Hydromyinae.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Histone-Lysine N-Methyltransferase: An enzyme that catalyzes the methylation of the epsilon-amino group of lysine residues in proteins to yield epsilon mono-, di-, and trimethyllysine. EC 2.1.1.43.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Molecular Sequence Annotation: The addition of descriptive information about the function or structure of a molecular sequence to its MOLECULAR SEQUENCE DATA record.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Ankyrins: A family of membrane-associated proteins responsible for the attachment of the cytoskeleton. Erythrocyte-related isoforms of ankyrin attach the SPECTRIN cytoskeleton to a transmembrane protein (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE) in the erythrocyte plasma membrane. Brain-related isoforms of ankyrin also exist.Spectrin: A high molecular weight (220-250 kDa) water-soluble protein which can be extracted from erythrocyte ghosts in low ionic strength buffers. The protein contains no lipids or carbohydrates, is the predominant species of peripheral erythrocyte membrane proteins, and exists as a fibrous coating on the inner, cytoplasmic surface of the membrane.Spherocytosis, Hereditary: A group of familial congenital hemolytic anemias characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. The erythrocytes have increased osmotic fragility and are abnormally permeable to sodium ions.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Cytoskeleton: The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Protein Splicing: The excision of in-frame internal protein sequences (INTEINS) of a precursor protein, coupled with ligation of the flanking sequences (EXTEINS). Protein splicing is an autocatalytic reaction and results in the production of two proteins from a single primary translation product: the intein and the mature protein.Erythrocyte Membrane: The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.Ankyrin Repeat: Protein motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating sequence of 33-amino acids was discovered in ANKYRIN where it is involved in interaction with the anion exchanger (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE). Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions.Tankyrases: A group of telomere associated proteins that interact with TRF1 PROTEIN, contain ANKYRIN REPEATS and have poly(ADP-ribose) polymerase activity.Amino Acid Motifs: Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Monomeric GTP-Binding Proteins: A class of monomeric, low molecular weight (20-25 kDa) GTP-binding proteins that regulate a variety of intracellular processes. The GTP bound form of the protein is active and limited by its inherent GTPase activity, which is controlled by an array of GTPase activators, GDP dissociation inhibitors, and guanine nucleotide exchange factors. This enzyme was formerly listed as EC 3.6.1.47Ankyrins: A family of membrane-associated proteins responsible for the attachment of the cytoskeleton. Erythrocyte-related isoforms of ankyrin attach the SPECTRIN cytoskeleton to a transmembrane protein (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE) in the erythrocyte plasma membrane. Brain-related isoforms of ankyrin also exist.Armadillo Domain Proteins: A family of proteins that contain several 42-amino acid repeat domains and are homologous to the Drosophila armadillo protein. They bind to other proteins through their armadillo domains and play a variety of roles in the CELL including SIGNAL TRANSDUCTION, regulation of DESMOSOME assembly, and CELL ADHESION.Receptor, EphA8: An eph family receptor found exclusively in BRAIN. EphA8 receptors may play a role in the axonal guidance of a subset of tectal commissural NEURONS.Ankyrin Repeat: Protein motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating sequence of 33-amino acids was discovered in ANKYRIN where it is involved in interaction with the anion exchanger (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE). Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions.Ankyrins: A family of membrane-associated proteins responsible for the attachment of the cytoskeleton. Erythrocyte-related isoforms of ankyrin attach the SPECTRIN cytoskeleton to a transmembrane protein (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE) in the erythrocyte plasma membrane. Brain-related isoforms of ankyrin also exist.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.I-kappa B Proteins: A family of inhibitory proteins which bind to the REL PROTO-ONCOGENE PROTEINS and modulate their activity. In the CYTOPLASM, I-kappa B proteins bind to the transcription factor NF-KAPPA B. Cell stimulation causes its dissociation and translocation of active NF-kappa B to the nucleus.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.NF-kappa B p50 Subunit: A component of NF-kappa B transcription factor. It is proteolytically processed from NF-kappa B p105 precursor protein and is capable of forming dimeric complexes with itself or with TRANSCRIPTION FACTOR RELA. It regulates expression of GENES involved in immune and inflammatory responses.TRPV Cation Channels: A subgroup of TRP cation channels named after vanilloid receptor. They are very sensitive to TEMPERATURE and hot spicy food and CAPSAICIN. They have the TRP domain and ANKYRIN repeats. Selectivity for CALCIUM over SODIUM ranges from 3 to 100 fold.Spectrin: A high molecular weight (220-250 kDa) water-soluble protein which can be extracted from erythrocyte ghosts in low ionic strength buffers. The protein contains no lipids or carbohydrates, is the predominant species of peripheral erythrocyte membrane proteins, and exists as a fibrous coating on the inner, cytoplasmic surface of the membrane.Ankyrins: A family of membrane-associated proteins responsible for the attachment of the cytoskeleton. Erythrocyte-related isoforms of ankyrin attach the SPECTRIN cytoskeleton to a transmembrane protein (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE) in the erythrocyte plasma membrane. Brain-related isoforms of ankyrin also exist.Vaccinium: A plant genus of the family ERICACEAE known for species with edible fruits.Biological Science Disciplines: All of the divisions of the natural sciences dealing with the various aspects of the phenomena of life and vital processes. The concept includes anatomy and physiology, biochemistry and biophysics, and the biology of animals, plants, and microorganisms. It should be differentiated from BIOLOGY, one of its subdivisions, concerned specifically with the origin and life processes of living organisms.Botany: The study of the origin, structure, development, growth, function, genetics, and reproduction of plants.Ankyrin Repeat: Protein motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating sequence of 33-amino acids was discovered in ANKYRIN where it is involved in interaction with the anion exchanger (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE). Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions.Faculty, Medical: The teaching staff and members of the administrative staff having academic rank in a medical school.Newspapers: Publications printed and distributed daily, weekly, or at some other regular and usually short interval, containing news, articles of opinion (as editorials and letters), features, advertising, and announcements of current interest. (Webster's 3d ed)Natural Science Disciplines: The sciences dealing with processes observable in nature.Plant Leaves: Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)

The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells. (1/741)

PINCH is a widely expressed and evolutionarily conserved protein comprising primarily five LIM domains, which are cysteine-rich consensus sequences implicated in mediating protein-protein interactions. We report here that PINCH is a binding protein for integrin-linked kinase (ILK), an intracellular serine/threonine protein kinase that plays important roles in the cell adhesion, growth factor, and Wnt signaling pathways. The interaction between ILK and PINCH has been consistently observed under a variety of experimental conditions. They have interacted in yeast two-hybrid assays, in solution, and in solid-phase-based binding assays. Furthermore, ILK, but not vinculin or focal adhesion kinase, has been coisolated with PINCH from mammalian cells by immunoaffinity chromatography, indicating that PINCH and ILK associate with each other in vivo. The PINCH-ILK interaction is mediated by the N-terminal-most LIM domain (LIM1, residues 1 to 70) of PINCH and multiple ankyrin (ANK) repeats located within the N-terminal domain (residues 1 to 163) of ILK. Additionally, biochemical studies indicate that ILK, through the interaction with PINCH, is capable of forming a ternary complex with Nck-2, an SH2/SH3-containing adapter protein implicated in growth factor receptor kinase and small GTPase signaling pathways. Finally, we have found that PINCH is concentrated in peripheral ruffles of cells spreading on fibronectin and have detected clusters of PINCH that are colocalized with the alpha5beta1 integrins. These results demonstrate a specific protein recognition mechanism utilizing a specific LIM domain and multiple ANK repeats and suggest that PINCH functions as an adapter protein connecting ILK and the integrins with components of growth factor receptor kinase and small GTPase signaling pathways.  (+info)

Characterization of Chlamydomonas reinhardtii zygote-specific cDNAs that encode novel proteins containing ankyrin repeats and WW domains. (2/741)

Genes that are expressed only in the young zygote are considered to be of great importance in the development of an isogamous green alga, Chlamydomonas reinhardtii. Clones representing the Zys3 gene were isolated from a cDNA library prepared using zygotes at 10 min after fertilization. Sequencing of Zys3 cDNA clones resulted in the isolation of two related molecular species. One of them encoded a protein that contained two kinds of protein-to-protein interaction motifs known as ankyrin repeats and WW domains. The other clone lacked the ankyrin repeats but was otherwise identical. These mRNA species began to accumulate simultaneously in cells beginning 10 min after fertilization, and reached maximum levels at about 4 h, after which time levels decreased markedly. Genomic DNA gel-blot analysis indicated that Zys3 was a single-copy gene. The Zys3 proteins exhibited parallel expression to the Zys3 mRNAs at first, appearing 2 h after mating, and reached maximum levels at more than 6 h, but persisted to at least 1 d. Immunocytochemical analysis revealed their localization in the endoplasmic reticulum, which suggests a role in the morphological changes of the endoplasmic reticulum or in the synthesis and transport of proteins to the Golgi apparatus or related vesicles.  (+info)

RFX-B is the gene responsible for the most common cause of the bare lymphocyte syndrome, an MHC class II immunodeficiency. (3/741)

The bare lymphocyte syndrome (BLS) is characterized by the absence of MHC class II transcription and humoral- and cellular-mediated immune responses to foreign antigens. Three of the four BLS genetic complementation groups have defects in the activity of the MHC class II transcription factor RFX. We have purified the RFX complex and sequenced its three subunits. The sequence of the smallest subunit describes a novel gene, termed RFX-B. RFX-B complements the predominant BLS complementation group (group B) and was found to be mutant in cell lines from this BLS group. The protein has no known DNA-binding domain but does contain three ankyrin repeats that are likely to be important in protein-protein interactions.  (+info)

Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling. (4/741)

Paxillin is a focal adhesion adaptor protein involved in the integration of growth factor- and adhesion-mediated signal transduction pathways. Repeats of a leucine-rich sequence named paxillin LD motifs (Brown M.C., M.S. Curtis, and C.E. Turner. 1998. Nature Struct. Biol. 5:677-678) have been implicated in paxillin binding to focal adhesion kinase (FAK) and vinculin. Here we demonstrate that the individual paxillin LD motifs function as discrete and selective protein binding interfaces. A novel scaffolding function is described for paxillin LD4 in the binding of a complex of proteins containing active p21 GTPase-activated kinase (PAK), Nck, and the guanine nucleotide exchange factor, PIX. The association of this complex with paxillin is mediated by a new 95-kD protein, p95PKL (paxillin-kinase linker), which binds directly to paxillin LD4 and PIX. This protein complex also binds to Hic-5, suggesting a conservation of LD function across the paxillin superfamily. Cloning of p95PKL revealed a multidomain protein containing an NH2-terminal ARF-GAP domain, three ankyrin-like repeats, a potential calcium-binding EF hand, calmodulin-binding IQ motifs, a myosin homology domain, and two paxillin-binding subdomains (PBS). Green fluorescent protein- (GFP-) tagged p95PKL localized to focal adhesions/complexes in CHO.K1 cells. Overexpression in neuroblastoma cells of a paxillin LD4 deletion mutant inhibited lamellipodia formation in response to insulin-like growth fac- tor-1. Microinjection of GST-LD4 into NIH3T3 cells significantly decreased cell migration into a wound. These data implicate paxillin as a mediator of p21 GTPase-regulated actin cytoskeletal reorganization through the recruitment to nascent focal adhesion structures of an active PAK/PIX complex potentially via interactions with p95PKL.  (+info)

Identification of a novel inhibitor of nuclear factor-kappaB, RelA-associated inhibitor. (5/741)

Here we report the identification and characterization of a novel protein, RelA-associated inhibitor (RAI), that binds to the NF-kappaB subunit p65 (RelA) and inhibits its transcriptional activity. RAI gene was isolated in a yeast two-hybrid screen using the central region of p65 as bait. We confirmed the physical interaction in vitro using recombinant proteins as well as in vivo by immunoprecipitation/Western blot assay. RAI gene encodes a protein with homology to the C-terminal region of 53BP2 containing four consecutive ankyrin repeats and an Src homology 3 domain. RAI mRNA was preferentially expressed in human heart, placenta, and prostate. Despite its similarity to 53BP2, RAI did not interact with p53 in a yeast two-hybrid assay. RAI inhibited the action of NF-kappaB p65 but not that of p53 in transient luciferase gene expression assays. Similarly, RAI inhibited the endogenous NF-kappaB activity induced by tumor necrosis factor-alpha. RAI specifically inhibited the DNA binding activity of p65 when co-transfected in 293 cells. RAI protein appeared to be located in the nucleus and colocalized with NF-kappaB p65 that was activated by TNF-alpha. These observations indicate that RAI is another inhibitor of NF-kappaB in addition to IkappaB proteins and may confer an alternative mechanism of regulation.  (+info)

INK4 cell cycle inhibitors direct transcriptional inactivation of NF-kappaB. (6/741)

The nuclear factor kappaB, a transcription factor regulating the expression of multiple genes including genes essential for cell cycle control, is found in most cells in a dormant state in the cytoplasm bound to the inhibitory family I kappaB via an ankyrin repeat domain. Stimulation of cells with a variety of inducers inactivates I kappaB proteins. The active dimeric NF-kappaB complex, often composed of 50- and 65-kilodalton subunits of the Rel family, translocates into the nucleus, where the NF-kappaBp65 subunit stimulates transcription. Here we report that a family of proteins containing ankyrin repeats, the inhibitors of Cdk4 (INK4) is able to bind NF-kappaBp65. The association of p16INK4 with NF-kappaBp65 is considerable in HeLa- or 293 cells, if the NF-kappaB inhibitor I kappaB alpha is degraded in response to TNFalpha stimulation. Overexpression of INK4 molecules suppresses the transactivational ability of NF-kappaB significantly. In contrast to INK4 proteins, the cell cycle inhibitor p27 enhances NF-kappaB transactivation activity. Thus, the effect of INK4 proteins on NF-kappaB function possibly modifies NF-kappaB mediated transcriptional activation of cell cycle associated factors.  (+info)

The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators. (7/741)

The proto-oncoprotein Bcl-3 is a member of the IkappaB family and is present predominantly in the nucleus. To gain insight into specific nuclear functions of Bcl-3 we have isolated proteins that interact with its ankyrin repeat domain. Using the yeast two-hybrid-system we identified four novel binding partners of Bcl-3 in addition to NF-kappaB p50 and p52, previously known to associate with Bcl-3. The novel Bcl-3 interactors Jab1, Pirin, Tip60 and Bard1 are nuclear proteins which also bind to other transcription factors including c-Jun, nuclear factor I (NFI), HIV-1 Tat or the tumor suppressor and PolII holoenzyme component Brca1, respectively. Bcl-3, p50, and either Bard1, Tip60 or Pirin are sequestered into quarternary complexes on NF-kappaB DNA binding sites, whereas Jab1 enhances p50-Bcl-3-DNA complex formation. Furthermore, the histone acetylase Tip60 enhances Bcl-3-p50 activated transcription through an NF-kappaB binding site, indicating that quarternary complexes containing Bcl-3 interactors modulate NF-kappaB driven gene expression. These data implicate Bcl-3 as an adaptor between NF-kappaB p50/p52 and other transcription regulators and suggest that its gene activation function may at least in part be due to recruitment of the Tip60 histone actetylase.  (+info)

Mutation in ankyrin repeats of the mouse Notch2 gene induces early embryonic lethality. (8/741)

Notch family genes encode transmembrane proteins involved in cell-fate determination. Using gene targeting procedures, we disrupted the mouse Notch2 gene by replacing all but one of the ankyrin repeat sequences in the cytoplasmic domain with the E. coli (beta)-galactosidase gene. The mutant Notch2 gene encodes a 380 kDa Notch2-(beta)-gal fusion protein with (beta)-galactosidase activity. Notch2 homozygous mutant mice die prior to embryonic day 11.5, whereas heterozygotes show no apparent abnormalities and are fully viable. Analysis of Notch2 expression patterns, revealed by X-gal staining, demonstrated that the Notch2 gene is expressed in a wide variety of tissues including neuroepithelia, somites, optic vesicles, otic vesicles, and branchial arches, but not heart. Histological studies, including in situ nick end labeling procedures, showed earlier onset and higher incidence of apoptosis in homozygous mutant mice than in heterozygotes or wild type mice. Dying cells were particularly evident in neural tissues, where they were seen as early as embryonic day 9.5 in Notch2-deficient mice. Cells from Notch2 mutant mice attach and grow normally in culture, demonstrating that Notch2 deficiency does not interfere with cell proliferation and that expression of the Notch2-(beta)-gal fusion protein is not toxic per se. In contrast to Notch1-deficient mice, Notch2 mutant mice did not show disorganized somitogenesis, nor did they fail to properly regulate the expression of neurogenic genes such as Hes-5 or Mash1. In situ hybridization studies show no indication of altered Notch1 expression patterns in Notch2 mutant mice. The results indicate that Notch2 plays an essential role in postimplantation development in mice, probably in some aspect of cell specification and/or differentiation, and that the ankyrin repeats are indispensable for its function.  (+info)

*Ankyrin

DARPin (designed ankyrin repeat protein), an engineered antibody mimetic based on the structure of ankyrin repeats PDB: 1N11​; ... Ankyrins at the US National Library of Medicine Medical Subject Headings (MeSH) Proteopedia 1n11 Ankyrin-R. ... These two properties in combination give rise to large repertoire of proteins ankyrin can recognise. Ankyrins are encoded by ... AnkyrinR was first characterized in human erythrocytes, where this ankyrin was referred to as erythrocyte ankyrin or band2.1. ...

*Ankyrin repeat

... s typically fold together to form a single, linear solenoid structure called ankyrin repeat domains. These ... A specialized family of ankyrin proteins known as muscle ankyrin repeat proteins (MARPs) are involved with the repair and ... designed ankyrin repeat protein), an engineered antibody mimetic based on the structure of ankyrin repeats PDB: 1N11​; Michaely ... The ankyrin fold appears to be defined by its structure rather than its function, since there is no specific sequence or ...

*KN motif and ankyrin repeat domains 4

... is a protein that in humans is encoded by the KANK4 gene. GRCh38: Ensembl release 89: ... KN motif and ankyrin repeat domains 4". Retrieved 2017-09-07. ...

*Ankyrin-G binding motif of KCNQ2-3

Interactions with ankyrin-G (ankyrin-3) are crucial to the localisation of voltage-gated sodium channels (VGSCs) at the axon ... This conserved 9-amino acid motif ((V/A)P(I/L)AXXE(S/D)D) is required for ankyrin-G binding and functions to localise sodium ... Pan Z, Kao T, Horvath Z, Lemos J, Sul JY, Cranstoun SD, Bennett V, Scherer SS, Cooper EC (March 2006). "A common ankyrin-G- ... In molecular biology, the ankyrin-G binding motif of KCNQ2-3 is a protein motif found in the potassium channels KCNQ2 and KCNQ3 ...

*ANK2

Ankyrin-B, also known as Ankyrin-2, is a protein which in humans is encoded by the ANK2 gene. Ankyrin-B is ubiquitously ... Ankyrin-B is a member of the ankyrin family of proteins. ankyrin-1 has shown to be essential in normal function of erythrocytes ... and determines ankyrin-B activity. The membrane-binding region of ankyrin-B is composed of 24 consecutive ankyrin repeats, and ... Ankyrin-B is a member of the ankyrin family of proteins, and is a modular protein which is composed of three structural domains ...

*INK4

They contain multiple ankyrin repeats. Ortega, Sagrario; Malumbres, Marcos; Barbacid, Mariano (March 2002). "Cyclin D-dependent ...

*Transient receptor potential channel

Ankyrin (TRPA) Stress (mechanical) receptor. Disputed to be temperature-sensitive; activated by isothiocyanates (pungent ...

*List of OMIM disorder codes

... ankyrin-B-related; 600919; ANK2 Cardiac conduction defect, nonspecific; 612838; SCN1B Cardioencephalomyopathy, fatal infantile ...

*ANKRD1

"Altered expression of cardiac ankyrin repeat protein and its homologue, ankyrin repeat protein with PEST and proline-rich ... "Altered expression of cardiac ankyrin repeat protein and its homologue, ankyrin repeat protein with PEST and proline-rich ... Shen L, Chen C, Wei X, Li X, Luo G, Zhang J, Bin J, Huang X, Cao S, Li G, Liao Y (May 2015). "Overexpression of ankyrin repeat ... Song Y, Xu J, Li Y, Jia C, Ma X, Zhang L, Xie X, Zhang Y, Gao X, Zhang Y, Zhu D (2012). "Cardiac ankyrin repeat protein ...

*ANKRD31

Ankyrin repeat domain 31 is a protein that in humans is encoded by the ANKRD31 gene. GRCh38: Ensembl release 89: ... ENSG00000145700 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". "Entrez Gene: Ankyrin repeat domain ...

*Polyphosphate kinase

NUC-2 contains several ankyrin repeats. Several members of this family are annotated as XPR1 proteins: the xenotropic and ...

*ANKRD17

Ankyrin repeat domain-containing protein 17 is a protein that in humans is encoded by the ANKRD17 gene. This gene encodes a ... "Entrez Gene: ANKRD17 ankyrin repeat domain 17". Human ANKRD17 genome location and ANKRD17 gene details page in the UCSC Genome ... protein with ankyrin repeats, which are associated with protein-protein interactions. Studies in mice suggest that this protein ...

*ANKRD25

KN motif and ankyrin repeat domain-containing protein 2 is a protein that in humans is encoded by the KANK2 gene. GRCh38: ... "Entrez Gene: ANKRD25 ankyrin repeat domain 25". Human KANK2 genome location and KANK2 gene details page in the UCSC Genome ... Zhu Y, Kakinuma N, Wang Y, Kiyama R (Jan 2008). "Kank proteins: a new family of ankyrin-repeat domain-containing proteins". ... 2007). "SIP, a novel ankyrin repeat containing protein, sequesters steroid receptor coactivators in the cytoplasm". EMBO J. 26 ...

*ANKRD13C

Ankyrin repeat domain-containing protein 13C is a protein that in humans is encoded by the ANKRD13C gene. ANKRD13C is predicted ... "Entrez Gene: ANKRD13C ankyrin repeat domain 13C". Chatr-Aryamontri A, Oughtred R, Boucher L, Rust J, Chang C, Kolas NK, ...

*ANKRD15

KN motif and ankyrin repeat domain-containing protein 1 is a protein that in humans is encoded by the KANK1 gene. This gene ... "Entrez Gene: ANKRD15 ankyrin repeat domain 15". Human KANK1 genome location and KANK1 gene details page in the UCSC Genome ... Zhu Y, Kakinuma N, Wang Y, Kiyama R (Jan 2008). "Kank proteins: a new family of ankyrin-repeat domain-containing proteins". ... "A novel ankyrin repeat-containing gene (Kank) located at 9p24 is a growth suppressor of renal cell carcinoma". J Biol Chem. 277 ...

*KRIT1

"Entrez Gene: KRIT1 KRIT1, ankyrin repeat containing". Pagenstecher A, Stahl S, Sure U, Felbor U (Mar 2009). "A two-hit ... a novel ankyrin repeat-containing protein encoded by a gene mapping to 7q21-22". Oncogene. 15 (9): 1043-9. doi:10.1038/sj.onc. ...

*ANKRD23

This gene is a member of the muscle ankyrin repeat protein (MARP) family and encodes a protein with four tandem ankyrin-like ... 2003), "The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response ... Ankyrin repeat domain-containing protein 23 is a protein that in humans is encoded by the ANKRD23 gene. ... "Entrez Gene: ANKRD23 ankyrin repeat domain 23". Miller, Melanie K; Bang Marie-Louise; Witt Christian C; Labeit Dietmar; ...

*Sigma-1 receptor

Hayashi T, Su TP (Jan 2001). "Regulating ankyrin dynamics: Roles of sigma-1 receptors". Proceedings of the National Academy of ...

*Romano-Ward syndrome

"ANK2 ankyrin 2 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2017-04-06. "KCNE1 potassium voltage- ...

*L1 (protein)

Ankyrin interaction with L1CAM is an example of a protein binding that fails in CRASH patients due to a mutation that causes ... Ankyrin-L1CAM interaction is involved in the growth cone initiation, consequently, a failure in this interaction causes ... The most important binding partners of the cytoplasmic tail of L1 proteins are ankyrins. The interaction is held in high- ... "Tyrosine phosphorylation at a site highly conserved in the L1 family of cell adhesion molecules abolishes ankyrin binding and ...

*NFASC

Tuvia S, Garver TD, Bennett V (1998). "The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin- ... Zhang X, Davis JQ, Carpenter S, Bennett V (1998). "Structural requirements for association of neurofascin with ankyrin". J. ... Jenkins SM, Bennett V (2002). "Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium ... "Ankyrin-based subcellular gradient of neurofascin, an immunoglobulin family protein, directs GABAergic innervation at purkinje ...

*Molecular Partners

They are derived from natural ankyrin repeat proteins. Repeat proteins are among the most common classes of binding proteins in ... Plückthun, A (2015). "Designed ankyrin repeat proteins (DARPins): binding proteins for research, diagnostics, and therapy". ... soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins". Journal of Molecular Biology. ... "High-affinity binders selected from designed ankyrin repeat protein libraries". Nature Biotechnology. 22 (5): 575-582. doi: ...

*TRANK1

Tetratricopeptide repeat and ankyrin repeat containing 1 is a protein that in humans is encoded by the TRANK1 gene. Through a ... Tetratricopeptide repeat and ankyrin repeat containing 1". Mühleisen TW, Leber M, Schulze TG, Strohmaier J, Degenhardt F, ...

*PRR32

Ankyrin repeat domain-1 was overexpressed in both groups. Underexpressed genes in both groups included myosin light chain ...

*ASB1

Ankyrin repeat and SOCS box protein 1 is a protein that is in humans, encoded by the ASB1 gene. The protein encoded by this ... They contain ankyrin repeat sequence and SOCS box domain. The SOCS box serves to couple suppressor of cytokine signalling (SOCS ... 2001). "Cloning and characterization of the genes encoding the ankyrin repeat and SOCS box-containing proteins Asb-1, Asb-2, ... ASB1 ankyrin repeat and SOCS box-containing 1". Human ASB1 genome location and ASB1 gene details page in the UCSC Genome ...
We have recently found that the erythroid ankyrin gene, Ank1, expresses isoforms in mouse skeletal muscle, several of which share COOH-terminal sequence with previously known Ank1 isoforms but have a novel, highly hydrophobic 72-amino acid segment at their NH2 termini. Here, through the use of domain-specific peptide antibodies, we report the presence of the small ankyrins in rat and rabbit skeletal muscle and demonstrate their selective association with the sarcoplasmic reticulum. In frozen sections of rat skeletal muscle, antibodies to the spectrin-binding domain (anti-p65) react only with a 210-kD Ank1 and label the sarcolemma and nuclei, while antibodies to the COOH terminus of the small ankyrin (anti-p6) react with peptides of 20 to 26 kD on immunoblots and decorate the myoplasm in a reticular pattern. Mice homozygous for the normoblastosis mutation (gene symbol nb) are deficient in the 210-kD ankyrin but contain normal levels of the small ankyrins in the myoplasm. In nb/nb skeletal
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Bromine atom in PDB 3f59: Crystal Structure Of ZU5-Ank, the Spectrin Binding Region of Human Erythroid Ankyrin
Erythrocyte ankyrin contains an 89-kDa domain (residues 2-827) comprised almost entirely of 22 tandem repeats of 33 amino acids which are responsible for the high affinity interaction of ankyrin with the anion exchanger (Davis, L., and Bennett, V. (1990) J. Biol. Chem. 265, 10589-10596). The question of whether the repeats are equivalent with respect to binding to the anion exchanger was addressed using defined regions of erythrocyte and brain ankyrins expressed in bacteria. The conclusion is that the repeats are not interchangeable and that the 44 residues from 722 to 765 are essential for high affinity binding between erythrocyte ankyrin and the anion exchanger. Residues 348-765 were active whereas a polypeptide of the same size (residues 305-721) but missing the 44 residues was not active. The difference between the active and inactive polypeptides was not caused by the degree of folding based on circular dichroism spectra. The 44 residues from 722 to 765 were not sufficient for binding since ...
Erythrocyte ankyrin contains an 89-kDa domain (residues 2-827) comprised almost entirely of 22 tandem repeats of 33 amino acids which are responsible for the high affinity interaction of ankyrin with the anion exchanger (Davis, L., and Bennett, V. (1990) J. Biol. Chem. 265, 10589-10596). The question of whether the repeats are equivalent with respect to binding to the anion exchanger was addressed using defined regions of erythrocyte and brain ankyrins expressed in bacteria. The conclusion is that the repeats are not interchangeable and that the 44 residues from 722 to 765 are essential for high affinity binding between erythrocyte ankyrin and the anion exchanger. Residues 348-765 were active whereas a polypeptide of the same size (residues 305-721) but missing the 44 residues was not active. The difference between the active and inactive polypeptides was not caused by the degree of folding based on circular dichroism spectra. The 44 residues from 722 to 765 were not sufficient for binding since ...
Ankyrins are a family of proteins that are believed to link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key…
N terminal band 3 binding domain with 24 tandem subunits of 33 amino-acids (the SW16/Ank repeat), important for lipid-binding activity of the beta-spectrin ankyrin-binding domain and its substantial role in maintaining the spectrin-based skeleton distribution ...
In addition to the variable phenotype observed, another notable characteristic of the affected individuals is that the clinical presentation of LQTS4 may be proportional to age.27 We suspect this could be due to age-related decreased expression of molecular chaperones,44 which normally act to buffer the cardiomyocyte from stress associated with genetic mutations.45 For example, with a high level of molecular chaperone coexpression, the catalytic activity of enzymes harboring mutations is preserved to a significantly greater extent.46 Therefore, it is reasonable to speculate that the relatively small difference in protein expression and partial mislocalization of AnkB p.S646F with concomitant effects on NCX observed in the in vitro system (Figure 6) during a relatively short duration (days), would likely be exacerbated with age in the context of the living organism, consistent with what is observed in our patient population. Furthermore, heterogeneity in these cellular systems that buffer against ...
Recruitment of ankyrin G by NF186 is critical for PNS node assembly. (A) DRG neurons expressing NF186-GFP or NF186ΔABD-GFP were cultured with Schwann cells under myelinating conditions, fixed, and stained for GFP, P0, and ankyrin G (left) or sodium channels (NaCh; right). Robust levels of NF186ΔABD at nodes were associated with reduced coexpression of ankyrin G and sodium channels, as evident by comparison of nontransfected nodes (asterisks) to transfected nodes (arrowheads). Bars, 10 μm. (B) Schematic diagram and sequence of NF constructs used for rescue experiments. The modified sequence within the NF mucin-like domain is shown with substituted codons marked in red. (C) Western blot of NF186 knockdown and rescue. DRG neurons were infected with pLL3.7 vector alone (sh Con) or encoding shRNA to endogenous NF186. shRNA-treated neurons were either not nucleofected (sh NF) or were nucleofected with the codon-modified NF186-GFP (+NF) or NF186ΔABD-GFP constructs (+NFΔABD). Lysates were blotted ...
The site in ank1.5 able to interact with obscurin is located in a sequence highly conserved among ankyrins. (A) A schematic representation of the structure of t
A distinct subtype of dopaminergic interneuron displays inverted structural plasticity at the axon initial segment.: The axon initial segment (AIS) is a special
KEYWORD: 3D-structure Activator Alternative splicing ANK repeat Apoptosis DNA-binding Nuclear protein Phosphorylation Polymorphism Repeat Transcription regulation Ubl conjugation ...
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Beh lt sich der Arbeitgeber durch arbeitsvertragliche Klauseln vor, eine Dienstwagenberechtigung zu widerrufen, braucht die Widerrufsklausel keine Ank ndigungsfrist zu enthalten
Das Ziel ist durch das Verständnis molekularer Krankheitsmechanismen neue Therapiestrategien gegen die Herzinsuffizienz zu entwickeln.
A recent investigative report by Steve Silberman from Wired about the highly resistant Acinetobacter baumannii, encountered by clinicians treating wounded
Mice with normoblastosis, nb/nb, have a severe hemolytic anemia. The extreme fragility and shortened lifespan of the mutant erythrocytes result from a defective membrane skeleton. Previous studies in our laboratory indicated a 50% deficiency of spectrin and an absence of normal ankyrin in erythrocyte membranes of nb/nb mice. We now report genetic mapping data that localize both the nb and erythroid ankyrin (Ank-1) loci to the centromeric end of mouse chromosome 8. Using immunological and biochemical methods, we have further characterized the nature of the ankyrin defect in mutant erythrocytes. We do not detect normal sized (210 kDa) erythroid ankyrin by immunoblot analysis in nb/nb reticulocytes. However, nb/nb reticulocytes do contain a 150-kDa ankyrin immunoreactive protein. The 150-kDa protein is present with normal-sized ankyrin in nb/+ reticulocytes but is not found in +/+ reticulocytes. Our genetic and biochemical data indicate that the nb mutation results from a defect in the
Using shRNA mediated knockdown in primary erythroblasts prior to terminal erythroid differentiation we have demonstrated the ability to deplete ankyrin-R expression by up to 95% generating an effective novel near null reticulocyte phenotype. As would be predicted, the reduction of ankyrin expression predominantly impacts the surface expression of membrane proteins assigned to the band 3 tetramer based erythrocyte multiprotein complex. The greatest impact of ankyrin deficiency is not on band 3 itself, however, but on the stability of the Rhesus protein sub complex (RhAG, Rh in particular), whether mediated by shRNA or by natural ankyrin genetic mutations. Importantly, reduced surface expression of the core Rh subcomplex components Rh and RhAG precedes the loss of the more extensively studied ankyrin binding protein band 3. We also demonstrate that absence of ankyrin during erythropoiesis abrogates the ability of band 3 to form the larger of two band 3-containing macrocomplexes (likely the band 3 ...
Spectrin and ankyrin are two essential proteins acting like bricks and...Ron Dubreuil associate professor of biological sciences at the Univer...Spectrin was first discovered in red blood cells where it forms a pro...Dubreuil and his UIC co-workers have spent a decade looking at differe... In our study we showed spectrin doesnt have to bind to ankyrin to d...,Ghost,protein,leaves,fresh,tracks,in,the,cell,biological,biology news articles,biology news today,latest biology news,current biology news,biology newsletters
The axon initial segment (AIS) is a specialized domain essential for neuronal function, the formation of which begins with localization of an ankyrin‐G (AnkG) scaffold. However, the mechanism directing and maintaining AnkG localization is largely unknown. In this study, we demonstrate that in vivo knockdown of microtubule cross‐linking factor 1 (MTCL1) in cerebellar Purkinje cells causes loss of axonal polarity coupled with AnkG mislocalization. MTCL1 lacking MT‐stabilizing activity failed to restore these defects, and stable MT bundles spanning the AIS were disorganized in knockdown cells. Interestingly, during early postnatal development, colocalization of MTCL1 with these stable MT bundles was observed prominently in the axon hillock and proximal axon. These results indicate that MTCL1‐mediated formation of stable MT bundles is crucial for maintenance of AnkG localization. We also demonstrate that Mtcl1 gene disruption results in abnormal motor coordination with Purkinje cell ...
To date little attention has focused on the relation between AF and prolongation of the QT interval. Maintenance of AF is dependent on vagal stimulation in multiple model systems, and this dependence is thought to reflect the role of dispersion of refractoriness in the sustained propagation of electrical rotors within the atria.2 Atrial repolarisation has not been extensively studied in the context of long QT syndrome, but in at least one form of the disorder abnormalities of atrial electrophysiology have been documented. In long QT syndrome type 4 (LQT4), caused by mutations in the β-ankyrin gene, affected family members exhibit not only typical ventricular repolarisation abnormalities, but also sinoatrial dysfunction and AF. Recently, Chen and colleagues identified an unusual mutation in the LQT1 potassium channel gene, KCNQ1, that resulted in very early onset AF and long QT syndrome.5 These findings, coupled with the variable sensitivity of the surface ECG in inherited repolarisation ...
MWDPRAARVPPRDLAVLLCNKSNAFFSLGKWNEAFVAAKECLQWDPTYVKGYYRAGYSLLRLHQPYEAAR 1 - 70 MFFEGLRLVQRSQDQAPVADFLVGVFTTMSSDSIVLQSFLPCFDHIFTTGFPTEVWQSVIEKLAKKGLWH 71 - 140 SFLLLSAKKDRLPRNIHVPELSLKSLFEKYVFIGLYEKMEQVPKLVQWLISIGASVETIGPYPLHALMRL 141 - 210 CIQARENHLFRWLMDHKPEWKGRINQKDGDGCTVLHVVAAHSPGYLVKRQTEDVQMLLRFGADPTLLDRQ 211 - 280 SRSVVDVLKRNKNFKAIEKINSHLEKLATCSKDLSGFSNGDGPTSENDIFRKVLEQLVKYMNSGNRLLHK 281 - 350 NFLKQEVVQRFLRLLSTLQEIPPDLVCDINQDCATTVFKFLLEKQRWPEVLLLLTRKVSGEPPLGDCLIK 351 - 420 DCNFSDLDICTIIPHLSTWDQRKKQLLGCLIDSGALPDGLQESQERPVVTCLKHEDFELAFLLLTKGADP 421 - 490 RAISLTEGDTPLHAALHIFLEIKADIGFSFLSHLLDLFWSNPTEFDYLNPNVQDSNGNTLMHILFQKGML 491 - 560 KRVKKLLDLLVKFDINFNLKNKEGKDARHRIKKNDSLLLAWNKALMENRRRSRQDSAAHLGKLSKSTAPG 561 - 630 HTSQLKSQGSFKSVPCGATARTLPEGSAVPDSWETLPGTQVTRKEPGALRPCSLRDCLMQDITVLIQQVE 631 - 700 VDPSFPEDCLQSSEPLEAGAGKEGKKDDKPTLGAGAPDCSEVGEGHAQVGLGALQLVPDDNRGKEGNDDQ 701 - 770 DDWSTQEIEACLQDFDNMTWEIECTSEMLKKLSSKVMTKVIKKKIILAIQQLGNGEWTQGLQKRLKHLKG 771 - 840 ...
Zongming Pan, Tingching Kao, Zsolt Horvath, Julia Lemos, Jai-Yoon Sul, Stephen D Cranstoun, Vann Bennett, Steven S Scherer, Edward C Cooper. J. Neurosci., 2006 Mar 8 , 26, 2599-613. KCNQ (KV7) potassium channels underlie subthreshold M-currents that stabilize the neuronal resting potential and prevent repetitive firing of action potentials. Here, antibodies against four different KCNQ2 and KCNQ3 polypeptide epitopes show these subunits concentrated at the axonal initial segment (AIS) and node of Ranvier. AIS concentration of KCNQ2 and KCNQ3, like that of voltage-gated sodium (NaV) channels, is abolished in ankyrin-G knock-out mice. A short motif, common to KCNQ2 and KCNQ3, mediates both in vivo ankyrin-G interaction and retention of the subunits at the AIS. This KCNQ2/KCNQ3 motif is nearly identical to the sequence on NaV alpha subunits that serves these functions. All identified NaV and KCNQ genes of worms, insects, and molluscs lack the ankyrin-G binding motif. In contrast, vertebrate ...
Article{pmid23619335, Author=Lamboy, J. A. and Kim, H. and Dembinski, H. and Ha, T. and Komives, E. A. , Title={{S}ingle-molecule {F}{R}{E}{T} reveals the native-state dynamics of the {I}κ{B}α ankyrin repeat domain}, Journal=J. Mol. Biol., Year=2013, Volume=425, Number=14, Pages=2578--2590, Month=Jul ...
Alexis S Hill, Atsuo Nishino, Koichi Nakajo, Giuxin Zhang, Jaime R Fineman, Michael E Selzer, Yasushi Okamura, Edward C Cooper. PLoS Genet., 2008 Dec , 4, e1000317. In many mammalian neurons, dense clusters of ion channels at the axonal initial segment and nodes of Ranvier underlie action potential generation and rapid conduction. Axonal clustering of mammalian voltage-gated sodium and KCNQ (Kv7) potassium channels is based on linkage to the actin-spectrin cytoskeleton, which is mediated by the adaptor protein ankyrin-G. We identified key steps in the evolution of this axonal channel clustering. The anchor motif for sodium channel clustering evolved early in the chordate lineage before the divergence of the wormlike cephalochordate, amphioxus. Axons of the lamprey, a very primitive vertebrate, exhibited some invertebrate features (lack of myelin, use of giant diameter to hasten conduction), but possessed narrow initial segments bearing sodium channel clusters like in more recently evolved ...
View mouse Shank2 Chr7:144001928-144424494 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
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MTHSPATSEDEERHSASECPEGGSESDSSPDGPGRGPRGTRGQGSGAPGSLASVRGLQGRSMSVPDDAHF 1 - 70 SMMVFRIGIPDLHQTKCLRFNPDATIWTAKQQVLCALSESLQDVLNYGLFQPATSGRDANFLEEERLLRE 71 - 140 YPQSFEKGVPYLEFRYKTRVYKQTNLDEKQLAKLHTKTGLKKFLEYVQLGTSDKVARLLDKGLDPNYHDS 141 - 210 DSGETPLTLAAQTEGSVEVIRTLCLGGAHIDFRARDGMTALHKAACARHCLALTALLDLGGSPNYKDRRG 211 - 280 LTPLFHTAMVGGDPRCCELLLFNRAQLGIADENGWQEIHQACQRGHSQHLEHLLFYGAEPGAQNASGNTA 281 - 350 LHICALYNKETCARILLYRGADKDVKNNNGQTPFQVAVIAGNFELGELIRNHREQDVVPFQESPKYAARR 351 - 420 RGPPGTGLTVPPALLRANSDTSMALPDWMVFSAPGAASSGAPGPTSGSQGQSQPSAPTTKLSSGTLRSAS 421 - 490 SPRGARARSPSRGRHPEDAKRQPRGRPSSSGTPREGPAGGTGGSGGPGGSLGSRGRRRKLYSAVPGRSFM 491 - 560 AVKSYQAQAEGEISLSKGEKIKVLSIGEGGFWEGQVKGRVGWFPSDCLEEVANRSQESKQESRSDKAKRL 561 - 630 FRHYTVGSYDSFDAPSLMDGIGPGSDYIIKEKTVLLQKKDSEGFGFVLRGAKAQTPIEEFTPTPAFPALQ 631 - 700 YLESVDEGGVAWRAGLRMGDFLIEVNGQNVVKVGHRQVVNMIRQGGNTLMVKVVMVTRHPDMDEAVHKKA 701 - 770 PQQAKRLPPPTISLRSKSMTSELEEMEYEQQPAPVPSMEKKRTVYQMALNKLDEILAAAQQTISASESPG 771 - 840 ...
Video created by Peking University for the course Advanced Neurobiology I. Lets learn more about the basic unit of the nervous system: the neuron. 2000+ courses from schools like Stanford and Yale - no application required. Build career skills ...
Shop Ankyrin ELISA Kit, Recombinant Protein and Ankyrin Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
LIAR antibody (ankyrin repeat domain 54) for ELISA, ICC/IF, IHC-P, WB. Anti-LIAR pAb (GTX85269) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
Complete information for FANK1 gene (Protein Coding), Fibronectin Type III And Ankyrin Repeat Domains 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for ANKRD9 gene (Protein Coding), Ankyrin Repeat Domain 9, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
To examine this further, we subtracted the membrane potential in the soma from the membrane potential simultaneously recorded in the axon. Shown here is a plot of membrane potential difference between the axon initial segment and the soma in a layer 5 pyramidal cell during injection of noise into the soma. Note that
SHANK3 antibody (SH3/ankyrin domain gene 3) for ICC/IF, IHC-Fr, WB. Anti-SHANK3 pAb (GTX133133) is tested in Mouse, Rat samples. 100% Ab-Assurance.
POTED - POTED (untagged)-Human POTE ankyrin domain family, member D (POTED) available for purchase from OriGene - Your Gene Company.
This antibody pair set comes with matched antibody pair to detect and quantify protein level of human ANKRA2. (H00057763-AP11) - Products - Abnova
Opens the Highlight Feature Bar and highlights feature annotations from the FEATURES table of the record. The Highlight Feature Bar can be used to navigate to and highlight other features and provides links to display the highlighted region separately. Links in the FEATURES table will also highlight the corresponding region of the sequence. More... ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
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Looking for online definition of ankyrin repeat domain 3 in the Medical Dictionary? ankyrin repeat domain 3 explanation free. What is ankyrin repeat domain 3? Meaning of ankyrin repeat domain 3 medical term. What does ankyrin repeat domain 3 mean?
TY - JOUR. T1 - Structure and stability of the ankyrin domain of the Drosophila Notch receptor. AU - Zweifel, Mark E.. AU - Leahy, Daniel J.. AU - Hughson, Frederick M.. AU - Barrick, Doug. PY - 2003/11. Y1 - 2003/11. N2 - The Notch receptor contains a conserved ankyrin repeat domain that is required for Notch-mediated signal transduction. The ankyrin domain of Drosophila Notch contains six ankyrin sequence repeats previously identified as closely matching the ankyrin repeat consensus sequence, and a putative seventh C-terminal sequence repeat that exhibits lower similarity to the consensus sequence. To better understand the role of the Notch ankyrin domain in Notch-mediated signaling and to examine how structure is distributed among the seven ankyrin sequence repeats, we have determined the crystal structure of this domain to 2.0 Å resolution. The seventh, C-terminal, ankyrin sequence repeat adopts a regular ankyrin fold, but the first, N-terminal ankyrin repeat, which contains a 15-residue ...
Ankyrin-B is a member of the ankyrin family of proteins. ankyrin-1 has shown to be essential in normal function of erythrocytes;[10] however, ankyrin-B and ankyrin-3 play essential roles in the localization and membrane stabilization of ion transporters and ion channels in cardiomyocytes.[9][11] Functional insights into ankyrin-B function have come from studies employing ankyrin-B chimeric proteins. One study showed that the death/C-terminal domain of ankyrin-B determines both the subcellular localization as well as activity in restoring normal inositol trisphosphate receptor and ryanodine receptor localization and cardiomyocyte contractility.[8] Further studies have shown that the beta-hairpin loops within the ankyrin repeat domain of ankyrin-B are required for the interaction with the inositol trisphosphate receptor, and a reduction of ankyrin-B in neonatal cardiomyocytes reduces the half-life of the inositol trisphosphate receptor by 3-fold and destabilizes its proper localization; all of ...
Spinal muscular atrophies (SMA, also known as hereditary motor neuropathies) and hereditary motor and sensory neuropathies (HMSN) are clinically and genetically heterogeneous disorders of the peripheral nervous system. Here we report that mutations in the TRPV4 gene cause congenital distal SMA, scapuloperoneal SMA, HMSN 2C. We identified three missense substitutions (R269H, R315W and R316C) affecting the intracellular N-terminal ankyrin domain of the TRPV4 ion channel in five families. Expression of mutant TRPV4 constructs in cells from the HeLa line revealed diminished surface localization of mutant proteins. In addition, TRPV4-regulated Ca(2+) influx was substantially reduced even after stimulation with 4alphaPDD, a TRPV4 channel-specific agonist, and with hypo-osmotic solution. In summary, we describe a new hereditary channelopathy caused by mutations in TRPV4 and present evidence that the resulting substitutions in the N-terminal ankyrin domain affect channel maturation, leading to reduced ...
Dendritic spines are postsynaptic structures in neurons often having a mushroom-like shape. Physiological significance and cytoskeletal mechanisms that maintain this shape are poorly understood. The spectrin-based membrane skeleton maintains the biconcave shape of erythrocytes, but whether spectrins also determine the shape of nonerythroid cells is less clear. We show that βIII spectrin in hippocampal and cortical neurons from rodent embryos of both sexes is distributed throughout the somatodendritic compartment but is particularly enriched in the neck and base of dendritic spines and largely absent from spine heads. Electron microscopy revealed that βIII spectrin forms a detergent-resistant cytoskeletal network at these sites. Knockdown of βIII spectrin results in a significant decrease in the density of dendritic spines. Surprisingly, the density of presynaptic terminals is not affected by βIII spectrin knockdown. However, instead of making normal spiny synapses, the presynaptic structures ...
Actin Dynamics: Roles in Cell and Tissue Morphogenesis in Development. Our laboratory studies the role of actin dynamics in regulating assembly and function of the diverse cytoskeletal structures that contribute to cell and tissue morphogenesis during embryonic development. Current research focuses on tropomodulins (Tmods), a conserved family of actin pointed end-capping proteins that block association and dissociation at slow-growing (pointed) ends of actin filaments. Tmods also bind tropomyosins (TMs), which cooperate with Tmods to tightly cap actin pointed ends, regulating actin filament lengths and stability in the spectrin-based membrane skeleton of non-muscle cells and in the contractile myofibrils of skeletal and cardiac muscle. Differences among Tmod family members in expression patterns, TM isoform binding, and actin monomer and polymer regulation suggest unique functions for each of the four vertebrate Tmods. Recent studies of mouse knockouts further implicate key requirements for ...
In this simulation action potential initiation, action potential properties and the role of axon initial segment Na+ channels are investigated in a realistic model of a layer 5 pyramidal neuron axon initial segment. The main Na+ channel properties were constrained by experimental data and the axon initial segment was reconstructed. Model parameters were constrained by direct recordings at the axon initial segment ...
Kidney ankyrin repeat-containing proteins (KANK1/2/3/4) belong to a family of scaffold proteins, playing critical roles in cytoskeleton organization, cell polarity and migration. Mutations in KANK proteins are implicated in cancers and genetic diseases, such as nephrotic syndrome. KANK proteins can bind various target proteins through different protein regions, including a highly conserved ankyrin repeat domain (ANKRD). However, the molecular basis for target recognition by the ANKRD remains elusive. In this study, we solved a high-resolution crystal structure of the ANKRD of KANK1 in complex with a short sequence of the motor protein kinesin family member 21A (KIF21A), revealing that the highly specific target-binding mode of the ANKRD involves combinatorial use of two interfaces ...
PIKE-A (PIKE-activating gene differs from PIKE-S with the addition of a 40-kDa C-terminal extension containing Arf-GAP and two ankyrin-repeat domains. and peripheral bloodstream leukocytes (4-6). Weve proven that PIKE-A is certainly coamplified with CDK4 on chromosome 12 in a number of human malignancies including sarcoma RG7112 neuroblastoma and glioblastoma (32). PIKE-A is certainly readily discovered in 12q-amplified cell lines including RMS13 rhabdomyosarcoma and OSA osteosarcoma however not in regular muscles (6). PIKE-A provides the GTPase PH ArfGAP and two Ankyrin repeats domains within PIKE-L but does not have the N-terminal proline-rich area which binds proteins 4.1N PLC-γ1 and PI3-kinase. PIKE-A particularly binds to energetic Akt and up-regulates its activity within a GTP-dependent way mediating human cancers cell invasion (32). Akt/PKB is an essential regulator of divergent cellular procedures including apoptosis proliferation fat burning capacity and differentiation. Constitutive ...
Using single-molecule atomic force microscopy, we find that a protein consisting of six identical ankyrin repeat units flanked by N- and C-terminal modules (N6C) unfolds in a stepwise, unit-by-unit fashion under a mechanical force. Stretching a N6C molecule results in a sawtooth pattern fingerprint, with as many as six peaks separated by ~10 nm and an average unfolding force of 50 ± 20 pN. Our results demonstrate that a stretching force can unfold multiple repeat units individually in a single protein molecule, despite extensive hydrophobic interactions between adjacent units ...
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Ion channels and transporters control the movement of charged ions across cell membranes. In the heart, the coordinate activities of these proteins regulate the...
Ion channels and transporters control the movement of charged ions across cell membranes. In the heart, the coordinate activities of these proteins regulate the...
J:44447 Baumeister A, Arber S, Caroni P, Accumulation of muscle ankyrin repeat protein transcript reveals local activation of primary myotube endcompartments during muscle morphogenesis. J Cell Biol. 1997 Dec 1;139(5):1231-42 ...
Allergan will make Molecular Partners a combined up-front payment of $62.5 million as part of two new agreements centered on the discovery, development, and commercialization of DARPin® (Designed Ankyrin Repeat Protein) therapeutics for treating serious ophthalmic disorders.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
As the constriction of the throat gently massaged her down into the pit below, she held her breath, tears in her eyes mixing with the saliva around her. She wondered if she would suffocate in the throat, contorted into an awkward pose, but as she was dragged deeper and deeper into the stocky body of her predator, eventually her head and shoulders poked out into the space below. It was not like her bra at all. There was no light, and the air was acrid with the stench of chlorine. She did not know how far the drop would be until she fell, but she could already hear the gurgling of the stomach as juices flooded in to greet her. Aside from that, only her mistressess breathing and heartbeat could be heard. It was much, much louder than she imagined, as if the Goblin machinists body itself was loud machinery that she had been fed to as fuel. When she thought no other sound could be heard from the outside, the Goblin stretched and burped loudly, giggling and covering her smirking lips with the flat ...
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Buy our Human Neurofascin peptide. Ab102740 is a blocking peptide for ab90979 and has been validated in BL. Abcam provides free protocols, tips and expert…
No. We know its confusing for people who grew up with Amahl and the Night Visitors, but its gender neutral pretty much to the extent that "Hope" is in English. Contrary to popular belief, Amal El-Mohtar is a woman. Mr. El-Mohtar is her father. He is not an editor of Goblin Fruit. Please stop addressing submissions to him ...
Choose and determine which version of Goblin Kaiser chords and tabs by At The Throne Of Judgment you can play. Last updated on 08.29.2014
Heres a look at just a few of the possible wrecks that can happen and some steps to protect against disease, weather and other goblins.
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Eine symptomlose Besiedlung des unteren Genitaltraktes bedarf keiner Therapie. Tiefe Keimzahlen (,104/ml= vereinzelt/mässig nachweisbar) sind eher mit Kolonisation assoziert, Keimzahl ,104/ml (= mässig/reichlich nachweisbar) und klinischen Beschwerden sind als mögliche Infekte zu behandeln. Im Zweifelsfall sollte eine Infektion mit Mycoplasmen allerdings immer behandelt werden. Bei einer behandlungsbedürftigen genitalen Mykoplasmeninfektion ist auch der symptomlose Partner zu untersuchen und ggf. zu therapieren, um Reinfekte zu vermeiden. Dies gilt besonders für rezidivierende Mykoplasmen u. Ureaplasmen - Infektionen ...
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Der Konsum von Kokain führt zu einer Überaktivität des Nervensystems. Das wiederum kann nicht nur zu einem Mangel an Neurotransmittern führen, sondern kann dem ganzen Körper schaden. Ein Mangel an Neurotransmittern führt zu Schlaflosigkeit, vermindertem Antrieb, Depressionen und einem allgemeinen Gefühl eines schweren Katers.. After C enthält die richtige Zusammenstellung von Nahrungsergänzungsmitteln und Vitaminen, um zu helfen, daß die negativen Effekte auf einem Minimum gehalten werden. Am Morgen nach dem Sündigen, je eine dieser 3 Kapseln mit ausreichend Wasser schlucken.. ...
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Scrub typhus is an understudied, potentially fatal infection that threatens one billion persons in the Asia-Pacific region. How the causative obligate intracellular bacterium, Orientia tsutsugamushi facilitates its intracellular survival and pathogenesis is poorly understood. Many intracellular bacterial pathogens utilize the Type 1 (T1SS) or Type 4 secretion system (T4SS) to translocate ankyrin repeat-containing proteins (Anks) that traffic to distinct subcellular locations and modulate host cell processes. The O. tsutsugamushi genome encodes one of the largest known bacterial Ank repertoires plus T1SS and T4SS components. Whether these potential virulence factors are expressed during infection, how the Anks are potentially secreted, and to where they localize in the host cell are not known. We determined that O. tsutsugamushi transcriptionally expresses 20 unique ank genes as well as genes for both T1SS and T4SS during infection of mammalian host cells. Examination of the Anks C-termini revealed that
Isoforms of Spectrin and Ankyrin Reflect the Functional Topography of the Mouse Kidney. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Hereditary Spherocytosis : A true, personal story from the experience, I Have Hereditary Spherocytosis. Im 22 living with hs i was diagnosed with it when i was younger i had a blood transfusion when i was younger and had my spleen and gallbladder removed when i was 7. I was great after that till abou...
Since the alarming report by King and Schumacher [1] in 1952, it has been evident that some asplenic persons are at increased risk for life-threatening and fatal bacterial infections. Because all of the patients described in the 1952 report were children, it was briefly thought that this risk might be higher in children only. However, subsequent reports [2-6] have provided convincing evidence that splenectomy carries a substantial risk for sepsis in adults as well; adults should be instructed in prevention. I have been unable to find a quantitative estimate of the risk for fatal fulminant sepsis in persons who have had a splenectomy for hereditary spherocytosis. Although an extensive review by Singer [4] found a 2.2% mortality from sepsis after splenectomy for hereditary spherocytosis, such a review cannot estimate fatalities per year at risk. As a result of my long-term interest in this disorder [7, 8], I have access to numerous persons who have had splenectomies for hereditary spherocytosis, ...
Home , Papers , Spinal transient receptor potential ankyrin 1 channel induces mechanical hypersensitivity, increases cutaneous blood flow, and mediates the pronociceptive action of dynorphin A. ...
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Recommended Articles:. Horresh I, Poliak S, Grant S, et al.. 2008. Multiple Molecular Interactions Determine the Clustering of Caspr2 and Kv1 Channels in Myelinated Axons. JOURNAL OF NEUROSCIENCE 28(52): 14213-14222 Goldberg EM, Clark BD, Zagha E, et al.. 2008. K+ channels at the axon initial segment dampen near-threshold excitability of neocortical fast-spiking GABAergic interneurons. NEURON 58 (3): 387-400 Kole MHP, Letzkus JJ, Stuart GJ. 2007. Axon initial segment Kv1 channels control axonal action potential waveform and synaptic efficacy. NEURON 55( 4): 633-647 Gu C, Zhou W, Puthenveedu MA, et al. 2006. The microtubule plus-end tracking protein EB1 is required for Kv1 voltage-gated K+ channel axonal targeting. NEURON 52(5 ): 803-816 Kleopa KA, Elman LB, Lang B, et al. 2006. Neuromyotonia and limbic encephalitis sera target mature Shaker-type K+ channels: subunit specificity correlates with clinical manifestations. BRAIN 129(Part 6):1570-1584 Hasband MN, Park EW, Zhen DK, et al. 2002. ...

Medical Dictionary Definitions A - Z List - «D»Medical Dictionary Definitions A - Z List - «D»

Deficiency, ankyrin Deficiency, ankyrin: Known also as hereditary spherocytosis (HS), this is a genetic disorder of the red ... due to deficiency of ankyrin, a protein in the membrane of the red cell. ... ...
more infohttp://drugline.org/medic/letter/D/page/7

Ankyrin - WikipediaAnkyrin - Wikipedia

DARPin (designed ankyrin repeat protein), an engineered antibody mimetic based on the structure of ankyrin repeats PDB: 1N11​; ... Ankyrins at the US National Library of Medicine Medical Subject Headings (MeSH) Proteopedia 1n11 Ankyrin-R. ... These two properties in combination give rise to large repertoire of proteins ankyrin can recognise. Ankyrins are encoded by ... AnkyrinR was first characterized in human erythrocytes, where this ankyrin was referred to as erythrocyte ankyrin or band2.1. ...
more infohttps://en.wikipedia.org/wiki/Ankyrin

Ankyrin repeat - WikipediaAnkyrin repeat - Wikipedia

Ankyrin repeats typically fold together to form a single, linear solenoid structure called ankyrin repeat domains. These ... A specialized family of ankyrin proteins known as muscle ankyrin repeat proteins (MARPs) are involved with the repair and ... designed ankyrin repeat protein), an engineered antibody mimetic based on the structure of ankyrin repeats PDB: 1N11​; Michaely ... The ankyrin fold appears to be defined by its structure rather than its function, since there is no specific sequence or ...
more infohttps://en.wikipedia.org/wiki/Ankyrin_repeat

Ankyrin-2 (Q8C8R3) | InterPro | EMBL-EBIAnkyrin-2 (Q8C8R3) | InterPro | EMBL-EBI

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
more infohttps://www.ebi.ac.uk/interpro/protein/Q8C8R3

Ankyrin repeat (IPR002110) | InterPro | EMBL-EBIAnkyrin repeat (IPR002110) | InterPro | EMBL-EBI

Ankyrin repeat (IPR002110). Short name: Ankyrin_rpt Description. The ankyrin repeat is one of the most common protein-protein ... The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or ... Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse ... Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?. Proteins 17 ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR002110

ANK3 ankyrin 3 [Homo sapiens (human)] - Gene - NCBIANK3 ankyrin 3 [Homo sapiens (human)] - Gene - NCBI

Death_ank3; Death domain of Ankyrin-3. cd00204. Location:62 → 187. ANK; ankyrin repeats; ankyrin repeats mediate protein- ... Death_ank3; Death domain of Ankyrin-3. cd00204. Location:51 → 176. ANK; ankyrin repeats; ankyrin repeats mediate protein- ... Death_ank3; Death domain of Ankyrin-3. cd00204. Location:68 → 193. ANK; ankyrin repeats; ankyrin repeats mediate protein- ... Death_ank3; Death domain of Ankyrin-3. cd00204. Location:68 → 193. ANK; ankyrin repeats; ankyrin repeats mediate protein- ...
more infohttps://www.ncbi.nlm.nih.gov/gene/288

Ankyrin-3 isoform X26 - Sus scrofa (Pig)Ankyrin-3 isoform X26 - Sus scrofa (Pig)

Ankyrin-3 isoform X26Imported. ,p>Information which has been imported from another database using automatic procedures.,/p> ,p ... IPR040745 Ankyrin_UPA. IPR011029 DEATH-like_dom_sf. IPR000488 Death_domain. IPR000906 ZU5_dom. ... IPR040745 Ankyrin_UPA. IPR011029 DEATH-like_dom_sf. IPR000488 Death_domain. IPR000906 ZU5_dom. ... tr,A0A480SDG8,A0A480SDG8_PIG Ankyrin-3 isoform X26 OS=Sus scrofa OX=9823 PE=4 SV=1 ...
more infohttps://www.uniprot.org/uniprot/A0A480SDG8

Ank2 - Ankyrin - Rattus norvegicus (Rat) - Ank2 gene & proteinAnk2 - Ankyrin - Rattus norvegicus (Rat) - Ank2 gene & protein

IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR036770. Ankyrin_rpt-contain_sf. ... IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR036770. Ankyrin_rpt-contain_sf. ... AnkyrinImported. ,p>Information which has been imported from another database using automatic procedures.,/p> ,p>,a href="/ ... tr,P97582,P97582_RAT Ankyrin (Fragment) OS=Rattus norvegicus GN=Ank2 PE=2 SV=1 ...
more infohttp://www.uniprot.org/uniprot/P97582

Ankyrin Repeat - Medical Dictionary online-medical-dictionary.orgAnkyrin Repeat - Medical Dictionary online-medical-dictionary.org

Ankyrin Repeat. Protein Motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating ... Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions. ... sequence of 33-Amino Acids was discovered in Ankyrin where it is involved in interaction with the anion exchanger (Anion ...
more infohttp://www.online-medical-dictionary.org/definitions-a/ankyrin-repeat.html

WikiGenes - ANK2 - ankyrin 2, neuronalWikiGenes - ANK2 - ankyrin 2, neuronal

Diversity in membrane binding sites of ankyrins. Brain ankyrin, erythrocyte ankyrin, and processed erythrocyte ankyrin ... Diversity in membrane binding sites of ankyrins. Brain ankyrin, erythrocyte ankyrin, and processed erythrocyte ankyrin ... Moreover, analysis of rat 190-kDa ankyrin G/ankyrin B chimeras shows that all three domains of 190-kDa ankyrin-G are required ... Ankyrins G and B also exhibit differences; mutations affecting spectrin binding had no effect on ankyrin-B function but did ...
more infohttps://www.wikigenes.org/e/gene/e/287.html

Analyses of Physcomitrella patens Ankyrin Repeat Proteins by Computational ApproachAnalyses of Physcomitrella patens Ankyrin Repeat Proteins by Computational Approach

... Niaz Mahmood1 and Nahid Tamanna2 ... Ankyrin (ANK) repeat containing proteins are evolutionary conserved and have functions in crucial cellular processes like cell ...
more infohttps://www.hindawi.com/journals/mbi/2016/9156735/abs/

Ankyrin repeat domain 29 ELISA Kits | Biocompare.comAnkyrin repeat domain 29 ELISA Kits | Biocompare.com

Compare Ankyrin repeat domain 29 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, ... Ankyrin repeat domain 29 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established antibody-based tool ... Your search returned 13 Ankyrin repeat domain 29 ELISA ELISA Kit across 1 supplier. ...
more infohttps://www.biocompare.com/pfu/110627/soids/2-321282/ELISA_Kit/ELISA_Ankyrin_repeat_domain_29

Ankyrin repeat domain 12 ELISA Kits | Biocompare.comAnkyrin repeat domain 12 ELISA Kits | Biocompare.com

Compare Ankyrin repeat domain 12 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, ... Ankyrin repeat domain 12 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established antibody-based tool ... Your search returned 20 Ankyrin repeat domain 12 ELISA ELISA Kit across 5 suppliers. ...
more infohttps://www.biocompare.com/pfu/110627/soids/2-27276/Assay_Kit/ELISA_Ankyrin_repeat_domain_12

Protocols Anti-Ankyrin brain antibody [N105/13] (ab131419) | AbcamProtocols Anti-Ankyrin brain antibody [N105/13] (ab131419) | Abcam

There are no specific protocols for Anti-Ankyrin brain antibody [N105/13] (ab131419). Please download our general protocols ...
more infohttps://www.abcam.com/ankyrin-brain-antibody-n10513-ab131419-protocols.html

Ankyrin repeat | definition of ankyrin repeat by Medical dictionaryAnkyrin repeat | definition of ankyrin repeat by Medical dictionary

... ankyrin repeat explanation free. What is ankyrin repeat? Meaning of ankyrin repeat medical term. What does ankyrin repeat mean? ... Looking for online definition of ankyrin repeat in the Medical Dictionary? ... ankyrin repeat. Also found in: Wikipedia. ankyrin repeat. A short repetitive sequence of amino acids consisting of a beta ... Ankyrin repeats were first identified in ankyrin, which tethers different proteins (e.g., nuclear and cytoplasmic proteins), ...
more infohttp://medical-dictionary.thefreedictionary.com/Ankyrin+repeat

Ankyrin CRISPR Plasmids | SCBT - Santa Cruz BiotechnologyAnkyrin CRISPR Plasmids | SCBT - Santa Cruz Biotechnology

offers a broad range of Ankyrin CRISPR/Cas9 Knockout plasmids and Ankyrin Double Nickase Plasmids. ... Ankyrin gene silencers are available as Ankyrin CRISPR/Cas9 Knockout plasmids and Ankyrin Double Nickase Plasmids. Ankyrin ... Ankyrin Antibodies for analysis of cellular responses to Ankyrin CRISPR Products * For further details describing the CRISPR ... Ankyrin G CRISPR Activation Plasmid (h2) sc-400421-ACT-2. h. Gene Activation. Puro, Blast, Hygro. ...
more infohttps://www.scbt.com/browse/Ankyrin-CRISPR-Plasmids/_/N-c0kfid

Ankrd13c (ankyrin repeat domain 13c) - Rat Genome DatabaseAnkrd13c (ankyrin repeat domain 13c) - Rat Genome Database

Homo sapiens (human) : ANKRD13C (ankyrin repeat domain 13C) HGNC Alliance Rattus norvegicus (Norway rat) : Ankrd13c (ankyrin ... Pan paniscus (bonobo/pygmy chimpanzee) : ANKRD13C (ankyrin repeat domain 13C) Canis lupus familiaris (dog) : ANKRD13C (ankyrin ... Sus scrofa (pig) : ANKRD13C (ankyrin repeat domain 13C) Chlorocebus sabaeus (green monkey) : ANKRD13C (ankyrin repeat domain ... Ankrd13c (ankyrin repeat domain 13C). Transitive Ortholog Pipeline. Transitive Ortholog Pipeline. Sus scrofa (pig):. ANKRD13C ( ...
more infohttps://rgd.mcw.edu/rgdweb/report/gene/main.html?id=1617912

RCSB PDB - Gene View 









 - RFXANK - regulatory factor X associated ankyrin containing proteinRCSB PDB - Gene View - RFXANK - regulatory factor X associated ankyrin containing protein

The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
more infohttp://www.rcsb.org/pdb/gene/RFXANK?chromosome=chr19&range=19312458&v=hg19

SOWAHD sosondowah ankyrin repeat domain family member D [Homo sapiens (human)] - Gene - NCBISOWAHD sosondowah ankyrin repeat domain family member D [Homo sapiens (human)] - Gene - NCBI

ankyrin repeat domain-containing protein SOWAHD. Names. ankyrin repeat domain 58. ankyrin repeat domain-containing protein 58. ... SOWAHD sosondowah ankyrin repeat domain family member D [Homo sapiens] SOWAHD sosondowah ankyrin repeat domain family member D ... ANK; ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ... sosondowah ankyrin repeat domain family member Dprovided by HGNC. Primary source. HGNC:HGNC:32960 See related. Ensembl: ...
more infohttps://www.ncbi.nlm.nih.gov/gene/347454

High-Resolution Crystallographic Analysis of AcrB Using Designed Ankyrin Repeat Proteins (DARPins) | SpringerLinkHigh-Resolution Crystallographic Analysis of AcrB Using Designed Ankyrin Repeat Proteins (DARPins) | SpringerLink

Tam H.K., Malviya V.N., Pos K.M. (2018) High-Resolution Crystallographic Analysis of AcrB Using Designed Ankyrin Repeat ... High-Resolution Crystallographic Analysis of AcrB Using Designed Ankyrin Repeat Proteins (DARPins). ... High-affinity binders selected from designed ankyrin repeat protein libraries. Nat Biotechnol 22:575-582CrossRefPubMedGoogle ... soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J Mol Biol 332:489-503CrossRef ...
more infohttps://link.springer.com/protocol/10.1007%2F978-1-4939-7454-2_1

Ankyrin-1 antibody | acris-antibodies.comAnkyrin-1 antibody | acris-antibodies.com

Ankyrins are a family of proteins that are believed to link the integral membrane proteins to the underlying spectrin-actin ... Background of Ankyrin-1 antibody. Ankyrins are a family of proteins that are believed to link the integral membrane proteins to ... Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats ... Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and ...
more infohttps://www.acris-antibodies.com/target/ankyrin-1-antibody.htm

Sequence Similarity 









- 1SW6: S. CEREVISIAE SWI6 ANKYRIN-REPEAT FRAGMENT Sequence Similarity Report PageSequence Similarity - 1SW6: S. CEREVISIAE SWI6 ANKYRIN-REPEAT FRAGMENT Sequence Similarity Report Page

X-ray structural analysis of the yeast cell cycle regulator Swi6 reveals variations of the ankyrin fold and has implications ...
more infohttps://www.rcsb.org/pdb/explore/sequenceCluster.do?structureId=1SW6

Ankyrin | Article about ankyrin by The Free DictionaryAnkyrin | Article about ankyrin by The Free Dictionary

Find out information about ankyrin. A protein found in the cell membrane of erythrocytes that attaches the membrane to the ... ankyrin. Also found in: Medical, Wikipedia. ankyrin. [aŋ′kī·rən] (cell and molecular biology) A protein found in the cell ... Ankyrin , Article about ankyrin by The Free Dictionary https://encyclopedia2.thefreedictionary.com/ankyrin ... However, as they align with ankyrin repeat domains, common in TRPA and TRPV as well as many other types of proteins (Sedgwick ...
more infohttp://encyclopedia2.thefreedictionary.com/Ankyrin

JCI -
Ankyrin-B dysfunction predisposes to arrhythmogenic cardiomyopathy and is amenable to therapyJCI - Ankyrin-B dysfunction predisposes to arrhythmogenic cardiomyopathy and is amenable to therapy

Our findings introduce what we believe to be a new pathway for ACM, a role of ankyrin-B in cardiac structure and signaling, a ... Following identification of deceased ACM probands possessing ANK2 rare variants and evidence of ankyrin-B loss of function on ... Ankyrin-B dysfunction predisposes to arrhythmogenic cardiomyopathy and is amenable to therapy. ... Ankyrin-B dysfunction predisposes to arrhythmogenic cardiomyopathy and is amenable to therapy. ...
more infohttps://jci.org/articles/view/125538/pdf

Fragment-based screening identifies molecules targeting the substrate-binding ankyrin repeat domains of tankyrase | Scientific...Fragment-based screening identifies molecules targeting the substrate-binding ankyrin repeat domains of tankyrase | Scientific...

... uses its ankyrin repeat clusters (ARCs) to bind a wide range of proteins and thereby controls diverse cellular functions. A ... Tankyrase-1 Ankyrin Repeats Form an Adaptable Binding Platform for Targets of ADP-Ribose Modification. Structure 24, 1679-1692 ... Pollock, K., Liu, M., Zaleska, M. et al. Fragment-based screening identifies molecules targeting the substrate-binding ankyrin ... The PARP enzyme and scaffolding protein tankyrase (TNKS, TNKS2) uses its ankyrin repeat clusters (ARCs) to bind a wide range of ...
more infohttps://www.nature.com/articles/s41598-019-55240-5?error=cookies_not_supported&code=98a664ae-42ad-4f6e-b364-9adecec25a5f
  • Ankyrin 3 is an immunologically distinct gene product from ankyrins 1 and 2, and was originally found at the axonal initial segment and nodes of Ranvier of neurons in the central and peripheral nervous systems. (nih.gov)
  • Ankyrin gene silencers are available as Ankyrin CRISPR/Cas9 Knockout plasmids and Ankyrin Double Nickase Plasmids. (scbt.com)
  • Ankyrin CRISPR/dCas9 Activation Plasmids and CRISPR Lenti Activation Systems for gene activation are also available. (scbt.com)
  • The AFLP2 fragment showed a significant level of similarity with the porcine ankyrin repeat domain 16 (ANKRD16) gene (GenBank accession no. (thefreedictionary.com)
  • Source:RefSeq mRNA;Acc :NM_ENSSSCG00000005 607 RALGPS 1 Ral GEF with PH domain and SH3 binding motif 1 [Source:HGNC Symbol;Acc:ENSSSCG00000005 679 ASB6 Sus scrofa ankyrin repeat and SOCS box containing 6 (ASB6), mRNA. (thefreedictionary.com)
  • Immunoblot against crude membranes from adult rat brain (RBM) and wild-type (WT) and Ankyrin-R knockout (KO) mouse brains probed with N388A/60 (left) and K58/35 (right) TC supe. (acris-antibodies.com)
  • Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. (acris-antibodies.com)
  • The ankyrin fold appears to be defined by its structure rather than its function, since there is no specific sequence or structure that is universally recognised by it. (wikipedia.org)
  • The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [ PMID: 8875926 , PMID: 9353127 , PMID: 9461436 , PMID: 9865693 ]. (ebi.ac.uk)
  • Ankyrin repeats typically fold together to form a single, linear solenoid structure called ankyrin repeat domains. (wikipedia.org)
  • Most studies have found that ankyrin repeats fold in a two-state folding mechanism, suggesting a high degree of folding cooperativity despite the local inter-residue contacts and the evident need for successful folding with varying numbers of repeats. (wikipedia.org)
  • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. (ebi.ac.uk)