bluuebunny/crossref_metadata_2025_split huggingface dataset:
Hepatocyte Growth Factor (HGF) Receptor
Authors: Comoglio P M , Graziani A 
Published: November 2023

Abstract
The HGF receptor was identified as the product of the proto-oncogene c-Met, the pl 90Met protein (Bottaro et al. 1991; Naldini et al. 1991a,b). p190Met is composed of a 50 kDa (a) chain disulphide linked to a 145 kDa (/J) chain in an apcomplex of 190 kDa (GenBank accession number X54559) (Giordano et al. 1989a; Ponzetto et al. 1991). Both the a chain and the p chain are exposed at the cell surface; the pchain contains a 23-amino-acid membrane-spanning segment and an intracellular region containing the tyrosine kinase domain.
Transforming Growth Factor-O (TGFB)
Authors: Gitelman S E , Derynck R 
Published: November 2023

Abstract
The TGF/3 superfamily may be divided into subfamilies according to sequence homology. One group consists of the closely related TGF/31, -2, and -3. cDNAs described previously as chicken TGF/34 and Xenopus TGF/35 are now thought to represent TGF/31 cDNAs. The other subfamilies include the inhibins and activins, Mullerian inhibitory substance, and the decapentaplegic/Vg1/BMP group, which has been referred to as DVR (Lyons et al. 1991). This latter group includes Vg1 from Xenopus laevis, a maternally inherited transcript localized to the vegetal pole of embryos. The bone morphogenetic proteins (BMPs) were originally characterized as osteoinductive factors purified from demineralized bone, and there are now at least eight such related factors (Wozney 1992). BMPs-2 and -4 bear closest homology to the decapentaplegic complex protein, a Drosophila protein mediating dorsal/ventral axis specification. BMPs-5, -6 (also known as vgr-1), -7, and -8 most closely resemble Drosophila protein 60A.
Receptors for Transforming Growth Factor-B (TGFB)
Authors: Knaus P I , Lodish H F 
Published: November 2023

Abstract
The cDNA for the TGF/3 type Ill receptor was first isolated from A10 cells (rat vascular smooth muscle cell line) by expression cloning in COS 7 cells (Wang et al. 1991) (GenBank accession number M 80784) and from rat fetal tissue by a peptide-sequencing-PCR approach (Lopez-Casillias et a/. 1991) (GenBank accession number M 77809). The human and pig cDNAs encoding the type Ill receptor have since been isolated (Moren et al. 1992). The encoded receptor is an 853-amino-acid protein (Fig. 1) with a single hydrophobic transmembrane domain, a 43-amino-acid-long cytoplasmic tail with no obvious signalling motif and a large N-terminal extracellular domain containing at least two sites for glycosaminoglycan addition and six consensus sites for N-linked glycosylation (Wang et al. 1991; Lopez-Casillias et al. 1991).
The Hsp70 family - an overview
Authors: Miao B , Davis J , Craig E A 
Published: November 2023

Abstract
hsp70 genes were first visualized as puffs on polytenechromosomes isolated from salivary glands upon exposureof Drosophila larvae to high temperature orchemicals (Ritossa, 1962). More than a decade later it wasdetermined that the major gene being transcribed andtranslated upon exposure to stress encoded a 70 kDaprotein (reviewed in Ashburner, Bonner, 1979; Craig,1985)). Proteins related to the Drosophila HSP70s havenow been identified in all organisms examined (Fig. 1).
Plant small heat shock proteins (sHSPs)
Authors: Vierling E , Lee GJ 
Published: November 2023

Abstract
Plants synthesize sHSPs belonging to five,, possibly more, nuclear-encoded gene families (Waters et al., 1996). There are over 50 plant sHSP gene sequences available in current databases. The plant sHSPs are categorized according to amino acid sequence similarity, immunological cross-reactivity, intracellular localization. The five best characterized families comprise two classes of cytosolic proteins (class I, II), three families of organelle-localized proteins, which have been shown to be targeted to the endoplasmic reticulum, chloroplast or mitochondrion.
Escherichia coli DsbB
Authors: Bardwell J C A 
Published: November 2023

Abstract
dsbB null mutants in E. coli have a severe, general defect in disulfide bond formation within the periplasm. The pleiotropic phenotypes associated with this defect are very similar to those of dsbA mutants (see entry p. 318). dsbB mutants have been isolated based on these phenotypes (Bardwell et al., 1993.
Escherichia coli DsbE
Authors: Missiakis D , Raina S 
Published: November 2023

Abstract
One of the genetic approaches that has led to the identification of genes whose products are involved in thiol-disulfide exchange reactions was based on the rationale that if such activities existed they should be inhibited in vivo by reducing agents such as dithiothreitol (DTT) (Missiakas etal., 1993).
Saccharomyces cerevisiae protein disulfide isomerase (PDI)
Authors: Tuite M F , Dunn A 
Published: November 2023

Abstract
Thioredoxin-related glycoprotein (TRG) (Gunther et al., 1991); glycosylation site binding protein (GSBP) (LaMantia etal., 1991).
Protein disulfide isomerase (PDI; EC 5.3.4.1) is the archetypal member of a family of sequence-related proteins located in the lumen of the endoplasmic reticulum (ER) of eukaryotic cells (Freedman et al., 1994). These proteins contain one or more copies of the -CGHC- motif which is related to the thioredoxin active site sequence -WCGPCK-.
Saccharomyces cerevisiae Mpdlp, Mpd2p
Authors: Tachikawa H , Mizunaga T 
Published: November 2023

Abstract
The MPD1, MPD2 genes were identified as multicopy suppressors of a pdi1 deletion mutant (Tachikawa et al., 1995). Unlike the PDI1 gene (see entry on S. cerevisiae PDI, p. 335), neither MPD1 nor MPD2 is essential for viability. The MPD1 gene encodes a polypeptide of 318 amino acids (GenBank accession number D34633), which is a member of the PDI family. While PDI has two disulfide isomerase active site sequences, mammalian PDI related proteins have two or three of those sites (Freedman et al., 1994).
Saccharomyces cerevisiae cydophilin A /Cpr1/Cyp1
Authors: Haendler B 
Published: November 2023

Abstract
CPH (Haendler etal., 1989); Cpr1 (Heitman et al., 1991); Cyp1 (Koser etal., 1991). CypA was isolated from a S. cerevisiae cell-free lysate using dye-ligand chromatography, isoelectric focusing and gel filtration (Haendler etal., 1989). The cDNA sequence predicts a protein of 162 amino acids (Haendler et al., 1989; Dietmeier and Tropschug, 1990; GenBank accession number X17505). Comparison with the protein sequence of other soluble cyclophilins from yeast or higher eukaryotes shows the existence of a highly conserved central region and of specific N- and C-terminal parts.
Saccharomyces cerevisiae Cpr7
Authors: Chang H -C J , Lindquist S 
Published: November 2023

Abstract
Cpr7 was isolated in a two-hybrid screen for proteins that interact with Rpd3, a yeast homolog of histone deacetylase (Duina etal., 1996a; Taunton etal., 1996). CPR7 was also identified in the yeast genome sequencing project (Zagulski etal., 1995).
The CPR7 gene (GenBank accession number U48868), located on chromosome X, encodes a protein of 393 amino acids with a predicted molecular weight of 45 kDa. The primary amino acid sequence of Cpr7 shares 38% amino acid identity with Cpr6, a Cyp40 homolog (Duina et al., 1996a). A search of the complete genomic sequence of S. cerevisiae indicates that Cpr6 and Cpr7 are the only two cyclophilins in the Cyp40 subfamily.
Saccharomyces cerevisiae CYPD/Cpr5
Authors: Frigerio G 
Published: November 2023

Abstract
The genomic CYPD sequence is part of cosmid 9740 from chromosome IV (GenBank accession number U28374; Johnston et al., unpublished entry). The open reading frame of a previously isolated cDNA (EMBL accession number X73142; Frigerio and Pelham, 1993), predicts a protein of 225 amino acids with a 22 residue N-terminal hydrophobic signal sequence and the C-terminal ER retrieval signal HDEL (Pelham, 1990). The 162 amino acid cyclophilin core domain defined with regard to cytoplasmic cyclophilins has up to 62% amino acid identity with other 5. cerevisiae cyclophilins. Sequence similarity is highest with a second cyclophilin found in the secretory pathway followed by the mitochondrial and the cytoplasmic form.
Vertebrate cydophilin B
Authors: Price E R , McKeon F 
Published: November 2023

Abstract
Cyclophilin B was identified by low stringency hybridization screens of cDNA libraries using the cyclophilin A sequence as a probe (Bergsma et al., 1991; Hasel et al., 1991; Price et al., 1991). Cyclophilin B was also identified as a protein in human breast milk (Spik et al., 1991) and in the media of COS cells transfected with a chicken cDNA library (Caroni etal., 1991).
Neurospora crassa FKBPs
Authors: Tropschug M 
Published: November 2023

Abstract
FK506-binding proteins; rapamycin-binding proteins; peptidyl-prolyl cis-trans isomerases (PPIase, EC no. 5.2.1.8.); rotamases, immunophilins (Schreiber, 1992).
Neurospora crassa is sensitive against the immunosuppressants FK506 and rapamycin, which originally were isolated as antifungal agents. This led to the search for receptor proteins for these immunsuppressants. In 1990, the abundant human (Standaert et al., 1990) and N. crassa cytosolic FKBPs (Tropschug et al., 1990) were cloned (see separate entry on N. crassa Cyps, p. 382). FKBPs are found in every prokaryotic and eukaryotic cell and in all subcellular localizations, like cytosol, endoplasmic reticulum (ER) or nucleus (reviewed by Schreiber, 1992; Kunz and Hall, 1993; Schmid, 1993; Fischer, 1994; Galat and Metcalfe, 1995).
Drosophila FKBP39
Authors: Theopold U , Hultmark D 
Published: November 2023

Abstract
Drosophila FKBP39 is the first member of the FK506-binding proteins found in this species. FKBP39 shows the highest similarity to a subfamily of these proteins that comprises one yeast and another insect protein. These FKBPs are characterized by a highly charged N-terminal domain followed by a C-terminal domain that binds the immunosuppressive drug FK506.
The cDNA isolated from a library of immune-induced adult flies (GenBank accession number Z46894) shows an open reading frame which codes for a protein with a bipartite domain structure (Theopold et al., 1995): the N-terminus contains two stretches of amino acids with acidic residues, separated by highly basic stretches (Fig. 1). Part of the second basic stretch comprises two overlapping, possible nuclear localization signals. The C-terminal domain shows high similarity to proteins that bind the-immunosuppressive drug FK506 (Gething and Sambrook, 1992; Kay, 1996; see overview, p. 359).
Mammalian Pin1
Authors: Lu K P , Hunter T 
Published: November 2023

Abstract
Pinl, a human protein interacting with the mitotic NIMA kinase isolated from Aspergillus nidulans, contains a catalytic domain characteristic of the highly conserved third family of peptidyl-prolyl cis-trans isomerases that are distinct from either the cyclophilins or the FK506-binding proteins. Pinl is a widely expressed 18 kDa protein localized in nuclear speckles which also contain spliceosomes. Pin 1 is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast, and to the Drosophila dodo protein. The biological function of this protein includes an essential role in regulation of mitotic progression, via direct interaction with a subset of mitosis-specific phosphoproteins, including NIMA and CDC25.
Pinl was originally isolated as a protein that interacts with the Aspergillus NIMA protein kinase and suppresses its mitosis-promoting activity in a yeast two-hybrid screen (Lu etal., 1996).
Mammalian MSF
Authors: Sakaguchi K Mihara,M 
Published: November 2023

Abstract
MSF (mitochondrial import stimulation factor) was isolated as a N-ethyl maleimide (NEM)-sensitive cytosolic factor required for in vitro protein import into mitochondria. MSF catalyses unfolding of precursor proteins, keeps them in an import-competent conformation, targets the unfolded proteins to mitochondria, and eventually mediates ATP-dependent mitochodrial protein import.
Mammalian Hip
Authors: Hohfeld J 
Published: November 2023

Abstract
The nucleotide sequence of the hip cDNA of rat predicts a 368 amino acid protein of 41.3 kDa (GenBank accession number X82021). The protein migrates with reduced mobility in SDS-PAGE resulting in an apparent mass of c. 50 kDa. Hip forms a homo-oligomer of c. 160 kDa probably containing four subunits. Rat Hip is 90.5% identical to p48 of the human Hsp90-progesterone receptor complex (accession number U28918) and 36 % identical to a so-called heat shock-related protein of Plasmodium berghei (accession numbers L04508 and L21710), revealing conservation of the Hip protein during eukaryotic evolution.
Quality control in the endoplasmic reticulum
Authors: Simons J F , Helenius A 
Published: November 2023

Abstract
The reasons for quality control are at least threefold. First, it makes sense to keep newly synthesized proteins in the ER until folding is completed because the ER contains a rich variety of chaperones and folding enzymes at high concentrations. The ER also has an ionic and redox milieu optimized for folding and disulfide formation. In the extracellular space, or other final compartments of residence, no folding machinery is available.
The HSP90 family — an overview
Authors: Scheibel T , Buchner J 
Published: November 2023

Abstract
Hsp90, Hsp80, Hsp81, Hsp82, Hsc82, Hsp83, Hsp85, HsplOO, Grp94, endoplasmin, Gp96, HtpG, c62.5, Erp99, Hsp108
Arabidopsis capsulatum, g-S21764; Arabidopsis thaliana, S-P27323; Candida albicans, g-X81025; Canis familiaris, (e) g-U01153; Cricetulus griseus, g-L33676; Catharanthus roseus, (e) g-L14594; Drosophila melanogaster, S-P02828; Escherichia coli, S-P10413; Gallus gallus, (a) s-P11501; G. gallus, (b) S-Q04619; G. gallus, (e) S-P08110; Histoplasma capsulatum, g-M55629; Homo sapiens, (a) S-P07900; H. sapiens, (b) S-P08238; H. sapiens, (e) S-P24625; Hordeum vulgare, (e) e-S31862; Leishmania.
Escherichia coli GroEL, structure, function
Authors: Weissman J S , Fenton W A , Braig K , Adams P D , Horwich A 
Published: November 2023

Abstract
Chaperonin 60, cpn60 (Hemmingsen et al., 1988; Goloubinoff etal., 1989b); GroES as chaperonin 10, cpn10 (Goloubinoff etal., 1989a). GroEL was originally identified through mutations of Escherichia coli that led to defective A phage biogenesis (Georgopoulos et al., 1973; Sternberg, 1973).
The structure of Escherichia coli GroES
Authors: Hunt J F , Deisenhofer J 
Published: November 2023

Abstract
The crystal structure of GroES shows that the 10 kDa monomer forms a topologically irregular four-stranded 0- barrel (Hunt et al., 1996; Mande et al., 1996). This structure is homologous to that of a /3-barrel domain found in the enzymes alcohol dehydrogenase, quinone oxi-doreductase (Murzin, 1996).
Cytosolic chaperonins — an overview
Authors: Kubota H , Willison K 
Published: November 2023

Abstract
In the cytosol of both prokaryotic, eukaryotic cells, many proteins that are newly synthesized or recovering from denatured states require folding assistance from a variety of molecular chaperones (Gething, Sambrook, 1992; Hartl, 1996). Early studies on chaperones identified a family of c. 60 kDa chaperonins (now called CPN60s) that includes GroEL of Escherichia coli, Hsp60 of mitochondria, the rubisco subunit binding protein of chloroplasts (Ellis, van der Vies, 1991).
CCTη,
Authors: Kubota H , Willison K 
Published: November 2023

Abstract
Mouse Cctq cDNA (GenBank accession number Z31399) was isolated by random selection from a testis cDNA library (Kubota et al., 1994). The mouse CCT protein is 544 amino acids in length, it shares approximately 30% identity with the other subunits of CCT, 40% with the archaebacterial chaperonin TF55 (Kubota et al., 1994). The CCT17 protein also shows weak similarity to the eubacterial chaperonin GroEL, intraorganellar chaperonins Hsp60, rubisco subunit-binding protein (Kim et al., 1994; Kubota et al., 1994, 1995a).
CCTб
Authors: Kubota H , Willison K 
Published: November 2023

Abstract
The yeast homologue of CCT0 is also called Cct8p (Kubota etal., 1995a). Mouse Ccte cDNA (GenBank accession number Z37164) 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., 1995b).
Cofactors in the facilitated folding of a-, β-tubulin
Authors: Cowan N J 
Published: November 2023

Abstract
Cofactor A, Rbl2 (S. cerevisiae) (Archer et al., 1995); cofactor D, Cin1 (5. cerevisiae, S. pombe) (Stearns et al., 1990); cofactor E = Pac2 (S. cerevisiae, 5. pombe) (GenBank accession number U16814). The tubulin cofactors were originally discovered as two crude fractions obtained by ion exchange chromatography that were together required (in addition to ATP, GTP, CCT, native tubulin heterodimers, the latter included so as to provide the opportunity for stabilization by exchange of newly folded tubulin polypeptides) for the productive folding of a-, j8-tubulin (Gao et al., 1993).
Synechococcus sp. PCC 7942 CIpC
Authors: Clarke A K 
Published: November 2023

Abstract
The Synechococcus sp. PCC 7942 CIpC (Clarke, Eriksson, 1996) is an 87 kDa polypeptide (840 amino acids) containing the two conserved ATP-binding domains characteristic of all larger Clp proteins (i.e. CIpA, B, C; see overview of HSP100/Clp proteins, p. 231). The length of the intervening region between the ATP-binding domains (i.e. 100-110 amino acids) is also representative of proteins within the CIpC subfamily, as are the two highly conserved repeat motifs located within the N-terminal region (Squires, Squires, 1992).
Chloroplast-localized Clp proteins
Authors: Vierling E 
Published: November 2023

Abstract
Complete derived amino acid sequences of higher plantClpC proteins are available from (Moore andKeegstra, 1993; GenBank accession number L09546) and(Gottesman 1990; P31541,P31542),, a sequence missing less than 70 codons atthe amino terminus available from Brassica napus(X75328). Overall the ClpC amino acid fromare also reported as ESTs for Arabidopsis thaliana (Squires,Squires, 1992;
Guidebook to the Calcium-binding Proteins
Authors: Celio Marco R 
Published: November 2023

Abstract
This is the latest book in the Sambrook and Tooze Guidebook Series, and it comprehensively details all that is currently known about the calcium-binding proteins. Calcium-binding proteins form a large family and have many functions within the cell, including decoding cellular signals. This is an active and expanding area of research, with new and important discoveries continually being made. Biochemists will find this book particularly useful, as will biologists in many fields in which the calcium-binding proteins are involved, such as neuroscience.
Introduction to EF-hand calcium-binding proteins
Authors: Celio Marco R 
Published: November 2023

Abstract
Calbindin D-28k is an intracellular soluble Ca2•-binding protein which, together with calretinin, constitutes the six EF-hand-domain branch of the troponin C superfamily of Ca2•-binding proteins. Ca/bind in D-28k shows a tissue-specific expression pattern, in some of the tissues its expression is regulated by vitamin D.
Leukocidins and gamma lysins (Staphylococcus sp.)
Authors: Ferraras M , Menestrina G 
Published: November 2023

Abstract
Staphylococcus aureus strains produce two kinds of bi¬ component toxins designated as leukocidins and γ-lysins (Freer and Arbuthnott 1983; Noda and Kato 1991).The Panton-Valentine (PV) leukocidins are two single polypeptide chains of 32 and 34.5 kD, called LukS and LukF respectively (S and F stand for slow and fast eluting during preparation). As single components they are inactive but act synergistically to induce damage of selected white cells: monocytes, macrophages, and polymorphonucleated cells (neutrophils), but not lymphocytes.
Depressant insect selective neurotoxins from scorpion venoms
Authors: Zlotkin E 
Published: November 2023

Abstract
The depressant insect-toxins, upon injection, induce a slow, progressively developing flaccid paralysis of blowfly larvae, which reveal a prolonged-extended shape of their body in contrast to the shortened-contracted body shape induced by the excitatory toxins (see above entry; Fig. 1; Zlotkin 1983).Depressant toxins were isolated from the venom of the following Buthinae scorpions: Buthotus judaicus (Bj IT2; Lester et al. 1982), Leiurus quinqauestriatus quinquestriatus, (Lqq 2; Zlotkin et al. 1985), leiurus quinquestriatus hebraeus (Lqh IT2; Zlotkin et al. 1991).
µ-Agatoxins (Agelenopsis aperta)
Authors: Adams M E , Norris T M 
Published: November 2023

Abstract
µ-Agatoxins are a group of homologous polypeptide toxins from venom of the American funnel web spider, Agelenopsis aperta (Adams et al. 1989b; Skinner et al. 1989). Six toxins, μ-Aga-I to VI (Fig. 1), which range in size from 36-38 amino acids, have been isolated and sequenced. The amino acid sequences of μ-agatoxins are highly conserved and the spacing of cysteine residues, which form four internal disulfide bonds, is identical among all of the toxins. The μ-agatoxins cause convulsive paralysis when injected into insects
Margatoxin, noxiustoxin, and kaliotoxin (Centruroides margaritatus, Centruroides noxius, Androctonus mauretanicus)
Authors: Slaughter R 
Published: November 2023

Abstract
Margatoxin (MgTX) and noxiustoxin (NxTX) are 39 amino acid peptides which share with charybdotoxin (ChTX) significant sequence homology and such structural motifs as three disulfide bridges, a mid-chain {a-helix), and a C terminal antiparallel β-sheet. MgTX and NxTX comprise the best-studied members of a second class of scorpion venom derived potassium channel blockers based on structure and channel selectivity. One other scorpion toxin that has been included in this class because of sequence homology with MgTX and NxTX is Centruroides limpidus limpidus toxin I (Martin et al. 1994). This peptide also blocks voltage-gated potassium channels but has not been extensively studied.
Dendrotoxins (Dendroaspis species)
Authors: Harvey A L 
Published: November 2023

Abstract
Dendrotoxins block certain voltage-dependent K+ channels in neurones (Harvey and Anderson 1991). They are isolated from venom of three species of African mamba snakes: the Eastern green mamba (Dendroaspis angusticeps), the Western green mamba (D. viridis), and the black mamba (D. polylepis) (Strydom 1973a; Harvey and Karlsson 1980). The dendrotoxins are small basic proteins of 57–60 residues in a single polypeptide chain crosslinked by three disulfide bonds (Fig. 1). Six natural variants have been sequenced: two isoforms of α-dendrotoxin and δ-dendrotoxin from D. angusticeps, toxin I and toxin K from D. polylepis, and Dv-14 from viridis (Strydom 1973b; Joubert and Taljaard 1980;Mehraban et al. 1986). Two related toxins, γ- and y-dendrotoxin, from D. angusticeps have been partially sequenced (Benishin et al. 1988).
ω-Conotoxins (Conus spp.)
Authors: Olivera B M , Imperial J S , Yoshikami D 
Published: November 2023

Abstract
The ω-conotoxins are a major family of paralytic neurotoxins produced in the venoms of various species of marine gastropods belonging to the genus Conus. At this time, the most widely known of these peptides is ω-conotoxin Gv1A (wGv1A), which has 27 amino acids and three disulfide linkages; in many scientific publications, the term ω-conotoxin (and sometimes the even more general ‘conotoxin’) is used to refer to ω-conotoxin Gv1A. (For example, the widely used ‘conotoxin-sensitive Ca channel’ usually means the channel is sensitive to wGv1A.) Several other ω-conotoxins have the same pharmacological specificity as ω-conotoxin Gv1A in mammalian systems, notably ω-conotoxins Mv11A and Sv1A.