bluuebunny/crossref_metadata_2025_split huggingface dataset:
ω-Grammotoxin SIA (Grammostola spatulata Chilean pink tarantula)
Authors: Lampe R A , Keith R A 
Published: November 2023

Abstract
ω-Grammotoxin SIA (ω-GsTx SIA) is a 36 amino acid, single chain peptide containing three disulfide bonds and an amidated carboxy terminus (Lampe et al. 1993). The average molecular weight of ω-GsTx SIA, determined by electrospray mass spectrometry (ES-MS), is 4109.2 Da in good agreement with the average theoretical molecular mass of 4109.7 Da. (Lampe et al. 1993). Reduction of the peptide results in the anticipated 6 amu shift with a corresponding ES-MS value of 4115.2 Da. Direct confirmation of the cysteine oxidation pattern has not been determined but is presumed to be the alternating Cys 1-4, Cys 2-5, and Cys 3-6 motif characteristic of the Conus snail toxins. The toxin is aqueous soluble, relatively temperature insensitive (extended storage as aqueous solution at 4 °C is routine), not readily susceptible to protease digestion and doesn’t demonstrate a high propensity to stick to either glass or plastic.
Hololena toxin (Hololena curta)
Authors: Bowers C W 
Published: November 2023

Abstract
Hololena toxin was isolated because of its ability to produce a presynaptic block of neuromuscular transmission in Drosophila larvae (Bowers et al. 1987). The nature of the presynaptic block indicated that the toxin was blocking neuronal calcium channels; this hypothesis has been verified directly using intracellular electro-physiology in Drosophila neurons (Leung et al. 1989; Leung and Byerly 1991). Hololena toxin is not active on any of the major voltage-dependent currents in Drosophila muscle, nor is it active at frog neuromuscular junction (Bowers et al. 1987). The isolated activity is only one of several that have now been described from the venom of this funnel web spider (Stapleton et al. 1990; Quistad et al. 1991; Lundy and Frew 1993; Meinwald and Eisner 1995), making the simple designation, hololena toxin, unavoidably anachronistic.
Calciseptine (Dendroaspis polylepis)
Authors: Romey G , Schweitz H , Lazdunski M 
Published: November 2023

Abstract
Calciseptine has been purified from the venom of the black mamba Dendroaspis polylepis polylepis. It is a single polypeptide chain of 7 kDa (60 amino acid residues with eight cysteines forming four disulfide bridges, sequence accession number to the Swiss Prot databank: P22947 TXCA-DENPO). Its primary structure is indicated below.Its sequence and its structural organization have similarities with neurotoxins that block the nicotinic receptors and with snake cyto-cardiotoxins (Rees and Bilwes 1993). Calciseptine has been shown to selectively block L-type calcium channels in a variety of cells but with a clearly tissue-dependent sensitivity. Calciseptine blocks L-type calcium current in aortic smooth muscle cells, ventricular cardiac cells, dorsal root ganglion nervous cells, and insulinoma cells.
Calcidudine (Dendroaspis angusticeps)
Authors: Romey G , Schweitz H , Lazdunski M 
Published: November 2023

Abstract
Calcicludine has been purified from the venom of the green mamba Dendroaspis angusticeps. It is a polypeptide of 7 kDa (60 amino acid residues with six cysteines forming three disulfide bridges, sequence accession number to PIR databank: A36989). Calcicludine is structurally homologous to Kunitz-type protease inhibitors. Homologies are 40 per cent with dendrotoxins, 29 per cent with the basic pancreatic trypsin inhibitor, and 39 per cent with the protease inhibitor domain of the amyloid b protein (APPi). Its primary structure is shown below.
Snake toxins against muscarinic acetylcholine receptors
Authors: Karlsson E , Jolkkonen M , Adem A 
Published: November 2023

Abstract
Muscarinic acetylcholine receptors participate in many physiological functions, such as reduction of heart rate, contraction of smooth muscles, glandular secretion, transmitter release and cognitive functions like learning and memory. There are five subtypes of receptors (m1-m5) and one organ or even a cell can express several subtypes. One exception is heart muscle which has only m2. Muscarinic receptors belong to a group of G-protein coupled receptors that consist of a single peptide chain which forms four extracellular, seven transmembrane and four intracellular domains (reviews: Hulme et al. 1990; Caulfield 1993: Wess 1993).
Introduction
Authors: Montecucco C 
Published: November 2023

Abstract
The synapse is a privileged site of communication of messages within the animal body. Synapses show different anatomical specializations depending on the type of cells involved: the main difference is between nerve-nerve and nerve-muscle synapses. The majority of synapses of vertebrates are present within the central nervous system. They are well protected from the rest of the body by anatomical barriers and are not easily reachable by toxins. Animal movement and behaviour strictly depends on the correct and timely function of central synapses and peripheral. The latter type of synapses are rapidly and easily accessible to a variety of molecules that enter body fluids. On this basis, it is not surprising that hundreds of protein toxins have been elaborated by many different animal species to block the transmission of nerve impulses to muscles. This result can be obtained by acting on the nerve terminal, i.e. presynaptically, or on the muscle cells, i.e. post-synaptically. This section focuses on those toxins blocking synaptic functions by binding to the presynaptic membrane. Several toxins acting on channels of the presynaptic membrane have been considered in previous parts.
Actin-binding protein-120 (ABP-120)
Authors: Cox Dianne , Condeelis John 
Published: November 2023

Abstract
Actin-binding protein-120 (ABP-120) is an actin-binding protein from Dictyostelium discoideum which cross-links actin filaments into networks containing orthogonal filaments in vitro.1 These networks closely resemble those found in ABP-120-rich pseudopods in situ (Fig. 1). The activity of ABP-120 in forming these networks is essential for the formation of normal pseudopods which, in turn, are necessary for normal cell migration, chemotaxis, and phagocytosis. The archetypical actin-binding site, shared by a large number of actin cross-linking proteins, was first identified in ABP-120. Other structural features of ABP-120 indicate that it is a member of the non-muscle filamin family of actin-binding proteins.
Actin Deploymerizing Factor (Adf)/Cofilin
Authors: Bamburg James R , Drubin David G 
Published: November 2023

Abstract
ADF/cofilins are essential proteins that increase the turnover rates of actin filaments. Within cells, they are concentrated in regions containing dynamic actin pools, such as ruffling membrane, and they are essential for cytokinesis. In higher vertebrates ADF and cofilin are products of different genes, but they have about a 70 per cent sequence identity within the same species. Since ADF and cofilin are often found in the same cell, they may be considered isoforms. Proteins of similar mass (15–19 kDa) and activity appear to exist in all eukaryoties.
Angiogenin
Authors: Hu Guo-fu , Vallee Bert L 
Published: November 2023

Abstract
Angiogenin, a potent inducer of neovascularization, is the first tumour-derived angiogenic factor to have been isolated based solely on its ability to induce the formation of new blood vessels. It is a member of the pancreatic ribonuclease superfamily and its characteristic ribonucleolytic activity is necessary for its angiogenic activity. ft induces most of the individual events in the process of angiogenesis, including binding to endothelial cells through its cell surface receptors; stimulating second messengers; mediating cell adhesion; promoting endothelial cell invasion; stimulating cell proliferation; and organizing endothelial cells to form a tubular structure. Angiogenin antagonists have been demonstrated to inhibit significantly the establishment of human cell tumours in athymic mice.
Nestin
Authors: Josephson Richard , McKay Ronald D G 
Published: November 2023

Abstract
Nestin is an approximately 220–240 kDa intermediate filament protein transiently expressed by mammalian neural precursor cells and myoblasts. Nestin is the first member of a new class of intermediate filaments, which appears to have evolved from an ancestral gene shared with the neurofilaments. Outside of the coiled-coil ‘core’ domain, nestin has little homology to other intermediate filaments; it has a large, acidic C-terminal tail with a novel repeated motif and virtually no N-terminal head domain. Its assembly into filaments requires a partner such as vimentin.
Neurofilament triplet proteins
Authors: Herrmann Harald , Aebi Ueli 
Published: November 2023

Abstract
The neurofilament triplet proteins (i.e. the low, middle, and high molecular weight neurofilament proteins NF-L, NF-M, and NF-H) are the most abundant cytoskeletal components found in neurones and their precursor cells. In vivo they assemble into obligate heteropolymeric filaments that, different from the other intermediate filaments (IF), run in parallel bundles for long distances. The intron-exon pattern of their genes deviates completely from that of the other four classes of IF proteins. However, all three NF proteins follow the general structural principles of IF protein architecture. At the cellular level, neurofilaments appear to be important for the establishment of the neuronal cytoskeleton, and particularly in specifying the axonal calibre.
Nuclear lamins
Authors: Moir Robert D , Spann Timothy P , Goldman Robert D 
Published: November 2023

Abstract
The nuclear lamins are intermediate filament proteins that are found exclusively in the cell nucleus of most multicellular animals and probably plants. The lamins assemble to form the nuclear lamina at the nuclear periphery. There also appear to be lamin assemblies within the nucleus. The lamins have been implicated as the major structural determinants of nuclear size and shape. The lamina, and therefore most likely the lamins, forms an interface between the nuclear envelope and chromatin, influencing both chromatin organization and DNA replication. The expression of different Jamin isotypes during development seems to parallel changes in nuclear structure and processes.
Peripherin
Authors: Parysek Linda 
Published: November 2023

Abstract
Peripherin is a neurone-specific 57 kDa intermediate filament subunit protein that is expressed mainly in the peripheral nervous system. Peripherin is initially expressed during the post-mitotic differentiation of neurones and during neuronal growth after axon injury,4,5 implicating a biological role for peripherin in the attainment or maintenance of the differentiated neuronal phenotype.
Vimentin
Authors: Chou Ying-Hao , Goldman Robert D 
Published: November 2023

Abstract
The expression of vimentin is developmentally regulated. Analyses of the vimentin gene structure indicate the presence of both positively and negatively regulated elements. In adult tissues, vimentin is mainly expressed in cells of mesenchymal origin. During early embryogenesis, it is expressed in parietal endoderm during midgestation, in neural crest cells, and in stem cells of the neuroepithelium. In most of these cases, vimentin expression precedes and overlaps transiently with the expression of tissue-specific IF proteins— that is, glial fibrillary acidic protein (GFAP) in astroglial cells, neurofilament proteins in neurones, and desmin and nestin in skeletal muscle cells. Many cultured cell lines express vimentin irrespective of their developmental origin.
FtsZ
Authors: Erickson Harold P , Stricker Jesse 
Published: November 2023

Abstract
FtsZ is a universal cytoskeletal protein in prokaryotes. FtsZ assembles into a ring that encircles the bacterium at the site of septation and contracts as the septum is formed. It is found in eubacteria, archaebacteria, and chloroplasts. FtsZ assembles into protofilaments and protofilament sheets in vitro, with a lattice similar to that of the microtubule wall. Sequence alignment, three-dimensional structure, and polymer similarity show that FtsZ is a bacterial homologue of tubulin.
Introduction
Authors: Vale Ronald D 
Published: November 2023

Abstract
Lamin-associated polypeptides are relatively minor nuclear envelope components, and are estimated to be present at less that a few per cent of the abundance of lamins. lmmunoprecipitation has been used to isolate LAP1 and LAP2 from rat liver nuclear envelopes and LBR from avian erythrocyte nuclear envelopes after the proteins are solubilized in buffers containing non-ionic detergent.
Kinesin, chromo
Authors: Vernos Isabelle 
Published: November 2023

Abstract
Chromokinesin defines a new class of kinesin-like proteins (KLP) in the Kin N family that are characteristically associated to chromosome arms during mitosis. This new class comprises chicken chromokinesin and Xenopus Xklp. Other KLPs are related to them either at the sequence level or at the functional level. Xenopus Xklp1 participates in the positioning of chromosomes on to the metaphase plate probably by contributing to the ‘polar ejection forces’ that push chromosomes away from the poles. In addition, it is essential to maintain spindle bipolarity, probably by mediating the interaction of spindle microtubules with chromosomes.
Kinesin, internal motor domain
Authors: Walczak Claire E 
Published: November 2023

Abstract
The internal motor kinesins (Kin I family for kinesin internal) have an N-terminal globular domain, a centrally located catalytic domain, and a C-terminal α-helical tail. All Kin I family members to date are homodimers. Each subunit of the homodimer is approximately 85 kDa, and no accessory polypeptides have been identified. They have been implicated to function in both vesicle transport and in mitosis with a specific role in regulating microtubule dynamics.
Kinesin, monomeric
Authors: Hirokawa Nobutaka 
Published: November 2023

Abstract
KIF1 (k.inesin superfamily protein 1) forms a subfamily of kinesin superfamily proteins that function as monomeric proteins associated with microtubule-based motor activity. 1 KIF1 A and KIF1B have been suggested to be involved in the intracellular transport of membranous organelles such as synaptic vesicle precursors and mitochondria, respectively.
Muscle myosin, scallop
Authors: Szent-Györgyi Andrew G 
Published: November 2023

Abstract
Scallop myosin is a Ca2+-regulated contractile muscle protein that initiates contraction by the direct binding of Ca2+. Its regulatory subunits are the essential and regulatory light chains (ELC and RLC) present in one to one stoichiometry with the myosin heavy chain. The RLC inhibits contractile functions in the absence of Ca2+; the ELC contains a unique triggering Ca2+-binding site.
Muscle myosin, smooth
Authors: Trybus Kathleen M 
Published: November 2023

Abstract
Cytoplasmic myosin II has also been referred to as non-muscle myosin, non-sarcomeric myosin, cellular myosin, or just myosin IL The term conventional myosin has sometimes been used to distinguish this enzyme from the unconventional types of cellular myosins, like the myosin Is.
Arp2/3 complex
Authors: Mullins R Dyche , Pollard Thomas D 
Published: November 2023

Abstract
Actin-related proteins Arp2 and Arp3 are major cellular proteins in Acanthamoeba castel/ani, present at micromolar levels and concentrated in the actin-rich cortex. Arp2 and Arp3 are closely related to actin, with 40–50 per cent and 30–40 per cent sequence identity respectively but they appear to be incapable of forming actin-like filaments. Both are components of a multiprotein particle, the Arp2/3 complex, initially purified from Acanthamoeba castellani by affinity chromatography on profilin.
Myosin II, cytoplasmic
Authors: Warrick Hans M , Spudich James A 
Published: November 2023

Abstract
The term cytoplasmic myosin 11 is used to describe a family of eukaryotic force-generating enzymes that hydrolyse ATP to ADP and P; and use the derived chemical energy to produce force when attached to actin filaments. The biological roles of these myosins include generating contractile forces in the furrow during cytokinesis and in maintaining cortical tension. They have also been implicated in developmental processes where cellular shape changes, internal reorganizations, and directed cell migrations appear to drive morphogenesis.
Kathryn G. Miller
Authors: Cheney Richard E 
Published: November 2023

Abstract
Class VI myosins are unconventional myosins that share sequence similarity to other myosins in the motor domain. One myosin in this class, Drosophila 95F myosin, has been demonstrated to participate in ATP-dependent, actin-based movement in vivo. This and other evidence suggest that class VI myosins do have enzymatic properties characteristic of myosins and that one function of this class of myosin is in intracellular transport.
Myomesin and M-protein
Authors: Perriard Jean-Claude , Fürst Dieter 
Published: November 2023

Abstract
Myomesin and M-protein are structural proteins with a molecular weight in the range of 163𩀓182 000 which typically localize in the centre of the M-band region of sarcomeres of skeletal and heart myofibrils. Although derived from different genes, both share the same domain organization and are members of the immunoglobulin superfamily of muscle proteins. It was proposed that these protein are involved in the maintenance of the regular lattice of the sarcomeric thick filaments. The spatial organization might be brought about by specific interactions of M-protein and myomesin with myosin thick filaments and titin.
Paramyosin
Authors: Cohen Carolyn 
Published: November 2023

Abstract
Genetic experiments in C elegans indicate that paramyosin is probably essential for the functional organization of invertebrate thick filaments. There is a rough correlation between thick filament length and paramyosin content. Since tension development in a muscle is proportional to thick filament length, muscles with large amounts of paramyosin develop large tensions. These same muscles are specialized for catch contraction, and it has been suggested that paramyosin may have a role in this mechanism.
Titin
Authors: Wang Kuan 
Published: November 2023

Abstract
The name connectin was originally used in 1977 to designate a SOS-insoluble protein mixture from exhaustively extracted striated muscle. Subsequent isolation of titin from the ‘connectin’ fraction in 1981 led to the synonymous usage of titin and connectin in recent literature. An unrelated 70 kDa actin- and laminin-binding protein from fibrosarcoma cells is also called connectin.
Adaptor proteins (AP-1-AP-3)
Authors: Robinson Margaret S 
Published: November 2023

Abstract
The ADP-ribosylation factors (Arf) are a family of 21 kDa GTP binding proteins which have been implicated as regulators of a wide variety of vesicular transport steps, as structural components of non-clathrin (COP!) coated vesicles and as direct activators of phospholipase D (PLD1). Activation of Arfs, coincident with the binding of GTP, causes a translocation of the otherwise soluble protein to membranes and is proposed to result in the nucleation of coat protein assembly and vesicular budding. Apparently conflicting data currently lead to uncertainty regarding the role of (Arf sensitive) PLO in vesicular transport, the role of Arf proteins in transport in general, and the view of Arf as a structural component of vesicle or membrane coated structures.
ADP-ribosylation factors (Arfs)
Authors: Kahn Richard A 
Published: November 2023

Abstract
AP180 is an abundant neurone-specific clathrin-associated phosphoprotein, which supports in vitro the assembly of clathrin triskelia into a homogeneous population of cage-like structures. This function appears to be regulated by inositol polyphosphates. Proteins related to AP180 are also expressed in non-neuronal cells.
Amphiphysin
Authors: McMahon Harvey T , Wigge Patrick 
Published: November 2023

Abstract
AP180 is extracted from coated vesicles with 0.5 M Tris along with other major coat proteins. AP180 can be purified by a combination of chromatographic techniques which include gel filtration, ion exchange chromatography on MQ resin and hydroxyapatite adsorption chromatography. Alternatively, AP180 has been expressed successfully in bacteria as either a GST or polyhistidinetagged fusion protein. Both are readily purified from bacterial lysates by affinity chromatography.
Coatomer
Authors: Lowe Martin , Pepperkok Rainer , Kreis Thomas E 
Published: November 2023

Abstract
lmmunofluorescence labelling of coatomer in tissue culture cells gives a perinuclear Golgi pattern with numerous smaller punctate structures scattered throughout the cell (Fig. 1(a)). The perinuclear labelling appears to form an envelope around the periphery of the Golgi complex, a localization consistent with the original immunoelectron microscopy studies showing coatomer predominantly on buds and vesicles on the rims of the Golgi complex.
Copii
Authors: Barlowe C 
Published: November 2023

Abstract
Genes encoding COPII proteins were first identified inS. cerevisiae through a genetic screen for secretion defective cells and later found to be required for transport vesicle budding from the ER. Subsequent biochemical approaches allowed for the isolation of three protein fractions, Sec23p/Sec24p complex, Sec13p/Sec31p, and Sar1p, that reproduce vesicle budding from ER membranes in vitro. The proteins that drive vesicle budding assemble into a uniform coat structure on ER-derived vesicles (Fig. 1). /n vitro synthesized COPl!-coated vesicles are competent to fuse with the Golgi and their composition is distinct from the donor membrane fraction in that they are enriched for cargo protein over resident ER protein.
Eps15
Authors: Sorkin Alexander 
Published: November 2023

Abstract
Eps15 is a prototype of the growing family of proteins containing EH domains.5 EH domains are found in yeast, worm, fly, frog, and mammalian proteins. The closest known homologue of Eps15 in mammalian cells is Eps15R, an Eps15-related protein4 (Fig. 1).
Giantin
Authors: Linstedt Adam D , Hauri Hans-Peter 
Published: November 2023

Abstract
Giantin is expressed and specifically localized to the Golgi complex in all avian and mammalian cells examined to date.1,5 Figure 1 shows a typical giantin staining pattern in a mammalian tissue culture cell. Following gradient fractionation, giantin is primarily recovered with markers of the cis/medial Golgi subcompartments.
p115
Authors: Sapperstein Stephanie K , Waters M Gerard 
Published: November 2023

Abstract
The mammalian intra-Golgi transport factor p 115 and the Saccharomyces cerevisiae ER to Golgi transport factor Uso 1 p are members of a novel family of proteins required for intracellular protein transport. These proteins possess a distinctive globular head/coiled-coil tail structure, reminiscent of myosin II, with three regions of high homology in the primary sequence. The available biochemical and genetic data suggest that p 115 is required for efficient docking of intracellular transport vesicles at the target compartment. The precise mechanism by which p 115 carries out this function remains to be determined.
Synaptojanin
Authors: Camilli Pietro De , Nemoto Yasuo 
Published: November 2023

Abstract
Synaptojanin (now referred to as synaptojanin 1) was initially identified as a major Grb2-binding protein in the total homogenate1,5 and synaptic fractions1 from rat brain and initially desdribed as p1451,2 or p150.
Coronin
Authors: Hostos Eugenio L de 
Published: November 2023

Abstract
p57 (mammals), Cm1p (Saccharomyces), coronin-like protein (Caenorhabditis, other organisms).
Coronin is an actin-associated protein isolated from Dictyoste/ium discoideum which belongs to the WD-repeat family of proteins, a group of proteins which includes the β subunits of the trimeric G proteins. lmmunolocalization using monoclonal antibodies and, more recently, direct localization using GFP-tagged coronin have shown that coronin is found in a variety of dynamic F-actin rich structures derived from the cell cortex (Fig. 1).