bluuebunny/crossref_metadata_2025_split huggingface dataset:
Leishmania HsplOO
Authors: Clos J , Hubei A , Brandau S , Dresel A , Horauf A 
Published: November 2023

Abstract
Leishmaniae have a biphasic life-cycle. In their vectors, the sandflies of the genus Phlebotomus, they inhabit the digestive tract as a flagellated promastigote form. In the mammalian host the promastigotes are phagocytized by macrophages, differentiate into aflagellated amastig-otes,, parasitize the macrophages of the skin (L. major, L. tropica), the mucous membranes (L. mexicana), or the viscera (L. donovani, L. infantum). During the transmission from a fly into a mammalian host the parasites encounter a temperature upshift of c. 10°C. This heat shock induces the synthesis of heat shock proteins, in some species can trigger the differentiation into the amastigote form.
Saccharomyces cerevisiae Hsp26
Authors: Tuite M , Rahman D R J , Bentley N J 
Published: November 2023

Abstract
The HSP26 gene was first isolated from Saccharomyces cerevisiae by the Lindquist laboratory (Petko, Lindquist, 1986) from a genomic library screen using cDNA probes made from heat shock mRNAs. The sequence of the HSP26 gene (GenBank accession number M23871) predicts a 214 amino acid protein (including the initiator Met) with a deduced molecular weight of 27 630 (Bossier et al., 1989.
Drosophila melanogaster small heat shock proteins
Authors: Michaud S , Joanisse D R , Tanguay R M 
Published: November 2023

Abstract
The specific heat shock response in D. melanogaster was first observed as the induction of new puffs on salivary gl,polytene chromosomes following exposure to 37°C (Ashburner, 1970). This response was shown to correlate with the preferential expression of a small number of heat shock proteins, a reduction of synthesis of normal proteins (Tissieres et al., 1974). 35S pulse-labelling experiments in both cultured cells, salivary glands were used by Mirault et al. (1978) to identify a subset of four sHSPs of less than 30 kDa.
Saccharomyces cerevisiae Cne1
Authors: Parlati F , Thomas D Y , Bergeron J 
Published: November 2023

Abstract
The CNE1 sequence (GenBank accession numbers L11012, X66470, U12980) predicts a 502 amino acid protein, Cnelp, with a 19 amino acid N-terminal signal sequence (Parlati et al., 1995). After signal peptide cleavage, the sequence predicts a protein with a molecular mass of 54 685 daltons. There are five consensus N-linked glycosylation sites. In contrast to its mammalian homologues, which encode a C- terminal transmembrane domain, a highly acidic cytosolic tail (Bergeron etal., 1994), Cnelp has a C-terminal transmembrane domain, no cytosolic tail (see Fig. 1).
Schizosaccharomyces pombe Cnx1
Authors: Parlati F , Thomas D Y , Bergeron J 
Published: November 2023

Abstract
Schizosaccharomyces pombe calnexin (Jannatipour, Rokeach, 1995; Parlati etal., 1995b). The nucleotide sequence of cnx1+ (GenBank accession numbers M98799, U13389) predicts an open reading frame encoding a 560 amino acid protein (Cnxlp) with a 22 amino acid N-terminal signal sequence. After signal peptide cleavage, the sequence predicts a 538 amino acid protein with a molecular mass of 61 064 daltons.
Mammalian calnexin
Authors: Pind S , Williams D B 
Published: November 2023

Abstract
p88 (Degen, Williams, 1991), IP90 (Hochstenbach et al., 1992), or B,VII (Cala et al., 1993) in early studies, but the calnexin designation has now been universally adopted. Calnexin was identified as one of four ER proteins that are phosphorylated following incubation of canine pancreatic rough microsomes with [y32P]GTP or [y32P]ATP (Wada et al., 1991). It was purified as a complex with three other proteins: the 35 kDa signal sequence receptor (SSR)a, 25 kDa SSR/3,, an unknown glycoprotein, gp25L.
Escherichia coli glutaredoxin
Authors: Nakamura H , Aslund F , Holmgren A 
Published: November 2023

Abstract
Purification, characterization of E. coli glutaredoxin Grx1 (see below) showed an acidic 10 kDa small protein exhibiting hydrogen donor activity with E. coli ribonucleotide reductase in the presence of 4 mM GSH, a general GSH-disulfide oxidoreductase activity with hydroxyethyl disulfide (Holmgren, 1976, 1979a, b). Grx1.
Escherichia coli DsbD
Authors: Missiakis D , Raina S 
Published: November 2023

Abstract
DsbA, DsbC periplasmic proteins of Escherichia coli (see entries pp. 318, 324) are two key players involved in disulfide bond formation. DsbA has been shown to act as an oxidase (Wunderlich, Glockshuber, 1993; Zapun et al., 1993), DsbC exhibits the dual properties of an oxidase, an isomerase (Zapun et al., 1995). These findings suggested that a reductase activity could also be required in the bacterial periplasm to facilitate disulfide bond rearrangement, some specific processes requiring reduced cysteines. Isolation of extragenic suppressors of dsbA null mutants led to the identification of such a putative activity encoded by a gene designated as dsbD (Missiakas etal., 1995).
Rhodobacter capsulatus HeIX
Authors: Kranz R G 
Published: November 2023

Abstract
The he/X gene of the photosynthetic bacterium Rhodobacter capsulatus (Beckman, Kranz, 1993; GenBank accession number M96013) encodes a protein of 176 amino acids with a traditional signal sequence that is related to the class of disulfide oxidoreductases called thioredoxins. Proteins of this class contain a conserved active site (FWAXWCXPCR). The functions of members of the disulfide oxidoreductase family of proteins in bacteria have recently been reviewed (Loferer, Hennecke, 1994).
Bradyrhizobium japonicum TIpA
Authors: Loferer H 
Published: November 2023

Abstract
A random Tn5 mutagenesis of Bradyrhizobium japonicum strain 110 was performed, the mutant bank screened for respiration-deficient strains using the electron donor TMPD (A/,A/,/V’,A/’-tetramethyl-p-phenylenediamine). Three independent Tn5 insertions, which resulted in defective TMPD oxidation, were located in the tlpA gene (Loferer etal., 1993).
Mammalian glutaredoxin
Authors: Nakamura H , Aslund F , Holmgren A 
Published: November 2023

Abstract
Mammalian glutaredoxin was first purified to homogeneity from calf thymus (Luthman et al., 1979; Luthman, Holmgren, 1982), which later enabled determination of the primary structure (Klintrot et al., 1984) demonstrating an active site with the sequence Cys-Pro-Tyr-Cys, identical to that of Escherichia coli glutaredoxin. Calf thymus Grx showed a general GSH-disulfide oxidoreductase activity with hydroxyethyldisulfide in a coupled system with NADPH.
Mammalian CaBP1
Authors: Fuellekrug J , Soling H -D 
Published: November 2023

Abstract
The nucleotide sequences of cDNAs encoding rat liver CaBPl (EMBL X79328; Fullekrug et al., 1994), the homologous P5 protein (95 % identity) from CHO cells (EMBL X62678; Chaudhuri et al., 1992) reveal two internal repeats of a thioredoxin-like domain including the putative catalytic site CGHC (75% internal homology, 65% homology to Escherichia coli thioredoxin).
Peptidyl-prolyl isomerases — an overview of the cydophilin, FKBP, parvulin families
Authors: Dolinski K , Heitman J 
Published: November 2023

Abstract
Because the peptide bond has partial double bond character, like all appropriately substituted double bonds it can exist in two isomers: cis, trans. For every amino acid except proline, there is a profound steric clash between adjacent side chains for the cis isomer but not for the trans isomer. In the case of proline, because the side chain is a secondary amide bound back to the main chain, this steric conflict is roughly equal for the two isomers.
Mip
Authors: Fischer G , Rahfeld J -U 
Published: November 2023

Abstract
The group of the Mip (macrophage infectivity potentiator) proteins should be thought of as a subfamily of the FK506-binding proteins (FKBPs). Proteins that are combined in this group share a C-terminal region homologous to FKBP12, and an N-terminal extension of about 100 amino acid residues. Almost exclusively, the members are of prokaryotic origin, deriving from pathogenic facultative or obligate intracellular bacteria. The peptidyl-prolyl cis-trans isomerase (PPIase) activity is inhibited by FK506. The Mip protein of Legionella pneumophila is the archetype of the subfamily.
Mammalian FKBP25
Authors: Galat A 
Published: November 2023

Abstract
The prokaryotic homologs of mammalian FKBP25 are named macrophage infectivity potentiator (Mip) (Engleberg et al., 1989; Bangsborg etal., 1991; see entry p. 399).
FKBP25 was isolated to homogeneity from bovine brain and other organs using two different procedures (Galat et al., 1992). Brain tissues were extracted with (1) phosphate or (2) Tris buffer, each containing 0.3-0.5 M NaCI and 0.5% Triton X-100. After dialysis the solubilized proteins were passed through a DEAE-cellulose (in Tris buffer, method 1) or were trapped on a CM-cellulose column (in phosphate buffer, method 2). The first fractions from DEAE (1) or the proteins eluted with high salt from CM (2) were fractionated on a chromatofocusing (PBE118) gel or were resolved on a preparative flat-bed isoelectrofocusing (ampholites from 11 to 7) gel. Final purification of FKBP25 was carried out on MonoS (Pharmacia).
Escherichia coli SecB
Authors: Randall L L 
Published: November 2023

Abstract
Escherichia coli SecB was originally identified in genetic studies as a factor that facilitated the export of a number of proteins destined for either the periplasmic space or the outer membrane (Kumamoto and Beckwith, 1983).
Genes with sequence similarity to secB have been identified in Buchnera aphidicola (GenBank accession number M90644) and Haemophilus influenzae (GenBank accession number L42023). Both bacteria are members of the gamma subdivision of Proteobacteria, which also includes E. coli. The deduced sequence of the protein encoded by the Buchnera gene is 47% identical (Lai and Baumann, 1992) to that of the E. coli SecB protein (Kumamoto and Nault, 1989) and the deduced sequence of the protein from Haemophilus is 56% identical to the E. coli protein (Fleischmann etal., 1995).
Escherichia coli FtsH
Authors: Akiyama Y , Ogura T , Ito K 
Published: November 2023

Abstract
FtsH is a membrane-bound ATPase found in the cytoplasmic membrane of prokaryotic cells. The cytoplasmic domain of FtsH contains an ATPase segment that is homologous to the corresponding domains of ‘AAA family’ members as well as a segment with a zinc protease signature. FtsH has proteolytic activity towards a selected set of unstable proteins. It has been postulated that FtsH has chaperone-like activities by which it assists in proper assembly of some membrane proteins.
Escherichia coli PapD
Authors: Lombardo M -J , Thanassi D G , Hultgren S J 
Published: November 2023

Abstract
PapD is the prototype member of the immunoglobulin- like superfamily of periplasmic chaperones (Hultgren et al., 1993). Most members of the family have been identified only by sequence or genetic analysis. The PapD superfamily can be divided into two subclasses according to conserved structural differences. These two subclasses assemble organelles with distinctly different architectures (Hung etal., 1996). PapD is the best characterized chaperone, but studies have been performed with other members of the family [FimC, type I pili of E. coli (Jones et al., 1993); FaeE, K88 pili of E. coli (Mol et al., 1994); and FanE, K99 pili of E. coli (Bakker etal., 1991)].
Subtilisin
Authors: Shinde U , Inouye M 
Published: November 2023

Abstract
The complete amino acid sequence of subtilisin E was deduced from the nucleotide sequences from chromosomal DNA isolated from B. subtilis 168 (Genbank accession number K01988; Ikemura et al., 1987) and is homologous with the sequences of subtilisin BPN’ (B. amyloliquefaciens; Stahl and Ferrari, 1984; accession number X00165) and Carlsberg (B. licheniformis and B. pumilis; Jacobs et al., 1983; accession number X03341). The protease is produced in the sporulation phase of Bacilli, and the late expression of the gene is mainly controlled at the level of transcription (Wong et al., 1986). The protein sequences of pre-pro-subtilisins are made up of 381 amino acid residues, 29 of which correspond to the signal peptide and 77 to the IMC (Inouye, 1991). The mature active proteins are made up of 275 amino acid residues and are devoid of the signal peptide as well as their IMCs. The molecular weights of the mature proteins vary between 28 and 30 kDa (Wong et al., 1986; Shinde and Inouye,1994).
Mammalian Hsc70, Hsp70 proteins
Authors: Hightower L E , Leung S -M 
Published: November 2023

Abstract
Hsc70 is also known as dathrin-uncoating ATPase (Ungewickell, 1985), Hsc73 (Welch, 1992), Prp73 (Terlecky et al., 1992, see entry p. 58). Hsp70 is also named Hsp72 (Welch, 1992), may generally be designated a stress- 70 protein (Gething, Sambrook, 1992).
Drosophila melanogaster Droelp
Authors: Mehta A D , Lee J Y , Palter K B 
Published: November 2023

Abstract
Droelp was isolated from embryos using Drosophila Hsc4p-affinity chromatography (A.D. Mehta, K.B. Palter, unpublished data; Hsc4p is an Hsc70 homolog, see entry p. 42). The Hsc4p-Droe1p complex is resistant to dissociation by 2M KCI but dissociates in the presence of Mg2+/ATP, as is true for bacterial GrpE (Zylicz etal., 1987). Similar results were obtained using Drosophila Hsc3p-affinity chromatography (Hsc3p is the ER HSP70 protein, see entry p. 45).
Escherichia coli GroES
Authors: Taher A , Landry SJ 
Published: November 2023

Abstract
The groE locus maps at 94 minutes on the E. coli chromosome, encodes two polypeptides, GroES, GroEL, in that order (Genbank accession number X07850) (Hemmingsen et al., 1988). The 97 residue GroES polypeptide has a predicted Mr of 10 368 daltons, a pl of 4.92. There exists approximately 35% sequence identity between the GroES, bovine cpn10 amino acid sequences.
Saccharomyces cerevisiae Hsp60
Authors: Langer T , Neupert W 
Published: November 2023

Abstract
The HSP60 gene of Saccharomyces cerevisiae was identified in the conditional mutant mif4 that lacked enzymatic activity of imported ornithine transcarbamylase (Cheng et al., 1989). Concurrently, the yeast HSP60 gene was isolated by screening a A-gt11 genomic library with a polyclonal antiserum raised against purified Tetra- hymena thermophila Hsp60 (Reading et al., 1989) or monoclonal antibodies directed against a protein fraction enriched in mitochondrial ribosomal proteins, respectively (Johnson et al., 1989).
Plastid Cpn60
Authors: Ellis RJ 
Published: November 2023

Abstract
Rubisco large subunit binding protein (Ellis, 1981; Lennox, Ellis, 1986; Musgrove, Ellis, 1986: Musgrove etal., 1987) ;rubisco subunit binding protein (Ellis, van der Vies, 1988); chloroplast chaperonin 60 (Gutteridge, Gatenby, 1995); chi cpn60.
CCT ε
Authors: Kubota H , Willison K 
Published: November 2023

Abstract
Mouse Ccte cDNA (GenBank accession number Z31555) was isolated by hybridization using a human PCR probe produced with a mixed primer for a motif (TNDGATI) conserved between CCTa, the archaebacterial chaperonin TF55 (Kubota etal., 1994).
The HSP100 family — an overview
Authors: Schirmer E C , Lindquist S 
Published: November 2023

Abstract
CIpA, CIpB, CIpC, etc., component A of protease Ti. CIpP (Ti) is not a member of this family, but functions in a complex with CIpA or CIpX (Hwang et al., 1987; Katayama-Fujimura etal., 1987; Gottesman etal., 1993). HsIU — a subunit of a distinct two component protease, HsIVU (Chang etal., 1993).
Escherichia coli CIpY
Authors: Gottesman S , Wu W -F , Missiakas D 
Published: November 2023

Abstract
The E. coli clpY gene is the second gene of a heat shock operon; the first gene is dpQ (also called hsIU), which resembles a /3-type proteasome subunit (Chuang et al., 1993). The operon is at 88.9 minutes on the E. coli genetic map. Both genes show increased expression in vivo after heat shock, are transcribed in vitro by a32 (Chuang etal., 1993).
Saccharomyces cerevisiae Hsp78
Authors: Schmitt M , Langer T 
Published: November 2023

Abstract
The HSP78 gene was isolated from a A-gt11 expression library (accession numbers: GenBank L16533; PIR S39001; SwissProt P33416). Monoclonal antibodies were raised against yeast mitochondrial ribosomal proteins, used for screening the library (Leonhardt etal., 1993).
Diphtheria toxin (Corynebacterium diphtheriae)
Authors: Murphy J R 
Published: November 2023

Abstract
Diphtheria toxin is the primary virulence factor of toxigenic C. diphtheriae the etiologic agent of clinical diphtheria (Pappenheimer 1977). The structural gene for diphtheria toxin, tox, is carried by a closely related family of corynebacteriophages of which the β-phage has been the best studied (Buck et al. 1985; Bishai and Murphy 1988). The regulation of tox gene expression is controlled by the C. diphtheriae determined iron-activated repressor DtxR (Tao et al. 1994). Diphtheria toxin is produced in maximal yield only during the decline phase of the bacterial growth cycle when iron becomes the growth rate limiting substrate. The toxin is synthesized in precursor form and is co-translationally secreted into the growth medium (Smith et al. 1980). As shown in Fig. 1, diphtheria toxin is a three domain protein and is composed of the catalytic (C), transmembrane (T), and receptor binding (R) domains. The R domain has been shown to specially bind to a heparin binding epidermal growth factor-like precursor on the surface of sensitive eukaryotic cells (Naglich et al. 1992).
Cytotoxic necrotizing factors (Escherichia coli)
Authors: Donelli G , Fiorentini C 
Published: November 2023

Abstract
Certain Escherichia coli strains belonging to the normal microflora present in the gastrointestinal tract, have been often associated with gastroenteritis, urogenital infections, septicemia, and bacteremia in both humans and animals. Among these pathogenic £. coli, a number of strains have been described as producing new putative virulence factors named cytotoxic necrotizing factors type 1 and 2 (CNF1 and CNF2). The first type of CNF was described as a cell-associated product of. coli strains isolated from children with diarrhea causing necrosis of rabbit skin and multinucleation in cultured cells (Caprioli et al. 1983). Subsequently, a second type of CNF was detected in extracts of £. coli strains isolated from calves with enteritis (De Rycke et al. 1987). Purified CNF1 (Caprioli et al. 1984) and CNF2 (Oswald and De Rycke 1990) are immunologically related and similar in molecular weights (113.7 and 110 kDa, respectively).
ActA (Listeria monocytogenes)
Authors: Kocks C , Cossart P 
Published: November 2023

Abstract
ActA is a major surface protein of the Gram positive human bacterial pathogen L. monocytogenes. It is encoded by gene actA (Genebank accession number M82881 and EMBL Data library accession number X59723) whose sequence predicts a 639-amino-acid protein with an amino-terminal signal peptide and a C-terminal membrane anchor (Domann et al. 1992; Vazquez-Boland et al. 1992). The N-terminus is processed at the predicted site and the mature 610-amino-acid protein is expressed on the bacterial surface and anchored into the bacterial membrane via its hydrophobic C-terminal region (Domann et al. 1992; Kocks et al. 1992). ActA (predicted isoelectric point: 4.74) is rich in glutamic acid (12 per cent) and proline (9.2 per cent). The N-terminal domain of ActA is highly charged. Its central region contains a succession of proline/glutamic rich stretches. The C-terminal part is more hydrophobic. As shown by immunogold labelling, the two first parts of the protein protrude from the cell wall and are thus able to interact with cytoskeleton components. ActA displays a polar distribution on the bacterial body. It is highly expressed at one pole of the bacterium and its distribution gradually decreases towards the other (Kocks et al. 1993).
Tetanus neurotoxin (Clostridium tetani)
Authors: Pellizzari R , Rossetto O 
Published: November 2023

Abstract
Tetanus neurotoxin (TeNT) is the cause of the spastic paralysis of tetanus (van Heyningen 1968; Montecucco and Schiavo 1995). It is produced as a single polypeptide chain of 150 kDa (1315 amino acid residues, sequence accession number to the Swiss Prot data bank: P04958ITETX_CLOTE). As shown in Fig. 1, it consists of three 50 kDa domains. Selective proteolysis generates within the bacterial culture the active di-chain toxin with a single interchain disulfide bond, whose reduction leads to total loss of neurotoxicity (Schiavo et al. 1990). The dichain toxin is the commercially available form. The heavy chain (H, 100 kda) is composed of two domains. He is responsible for the neurospecific binding to a yet unknown presynaptic nerve terminal protein receptor. HN is involved in the membrane translocation of the L chain in the cytosol (L, 50 kDa). In the course of the pathogenesis of tetanus, TeNT is internalized at the presynaptic terminal of the neuromuscular junction and migrates retroaxonally, inside the motorneuron, to the spinal cord (Schwab et al. 1979). It is then released in the inter¬synaptic space between the motorneuron and the inhibitory interneuron (Renshaw cell), it penetrates this latter cell via intracellular acidic compartments (Williamson and Neale 1994) and blocks their neuro-exocytosis.
Introduction
Authors: Benson J A 
Published: November 2023

Abstract
For defence and offense in the natural world, evolution and human design have placed a high premium on rapid knock-down. Sedentary or slow animals which defend themselves from or prey upon faster animals, plants that produce chemical defences against herbivores, and farmers who wish to reduce to a minimum crop damage due to infestation with pest insects and other species, all utilize toxic substances that act on the nervous system (Benson 1992). The sodium channel is a primary site of action for these compounds because of its central role in action potential conduction and because it is apparently highly conserved in function, although less so in molecular structure, throughout the animal kingdom (Trimmer and Agnew 1989). For example, tetrodotoxin (TTX), a non-peptidergic component of puffer fish venom, is famous for the potent, rapid, and highly specific action in blocking axonal action potentials that has made it a favourite research tool among electrophysiologists. DDT, a compound of wholly chemical inspiration which was for forty years an inexpensive, safe, broad spectrum insecticide has its insecticidal effect by slowing sodium channel inactivation (Narahashi and Haas 1967). Taken off the market in recent years due to its persistence and consequent deleterious accumulation at the top of the food chain, DDT has been replaced in large part by the pyrethroids, which also have their site of action on the sodium channel.
α-Scorpion toxins
Authors: Martin-Eauclaire M -F , Bougis P E 
Published: November 2023

Abstract
α-Toxins can be considered as the cause of the scorpion venom toxicity for mammals and particularly human beings, in the ‘Old World’ (Miranda et al. 1970). For example, 90 per cent of the toxicity for the mouse in the venom of Androctonus australis from North Africa is due to only 2 per cent of the weight of the crude venom. The toxic fractions are α-toxins (named AaH I, AaH II, AaH Ill according to their chromatographic behaviour) (Martin and Rochat 1986). These toxins are constituted by a single polypeptide chain of 60 to 70 amino acid residues reticulated by four disulfide bridges (Miranda et al. 1970). Their three dimensional structure is well documented: the AaH II structure has been determined at high resolution by X-ray crystallography (Fontecilla-Camps et al. 1988) and AaH Ill by 1H-nuclear magnetic resonance (NMR) (Mikou et al. 1992).