bluuebunny/crossref_metadata_2025_split huggingface dataset:
Rho-GDI
Authors: Tanaka Kazuma , Kikuchi Akira , Kaibuchi Kozo , Sasaki kuya , Takai Yoshimi 
Published: November 2023

Abstract
Rho-GDI was first purified from bovine brain and its cDNA was cloned based on the amino acid sequences (Ueda etal. 1990; Fukumoto etal. 1990). The cDNA for human Rho-GDI was also cloned and sequenced (Maeda etal., unpublished results). Recently, a closely related homolog of Rho-GDI, D4 (Lelias etal. 1993) or Ly-GDI (Scherle etal. 1993), has been cloned from human hematopoietic cell lines. D4 and Ly-GDI encode the same protein.
Dbl
Authors: Cerione Richard 
Published: November 2023

Abstract
Proto-Dbl encodes a 115-kDa protein (925 amino acids) that is predicted to be very hydrophilic and contains an amino terminal domain (497 amino acids) that was deleted in the generation of oncogenic Dbl and contains a secondary structure similar to the rod domain of several structural proteins, especially the intermediate filament protein, vimentin (Evaand Aaronson 1985; Ron etal. 1988).
The Chimaerin and Ber familes
Authors: Settleman Jeffrey 
Published: November 2023

Abstract
The following section combines family members n-chimaerins and wice are primarily GTPase-activating porteins(GAPS) for Rac and separate family members,BCr andAbrmwhose chimaterin-related Gap domain acts on both rac and Cdec42 this combination allows convenient co,parisons of the realtionships between different family members and beteween the different families.
Rho 1p
Authors: Madaule Pascal , Johnson Joni , McCaffrey Mary , Boquet Patrice , Myers Alan 
Published: November 2023

Abstract
RHO1 was identified by a low stringency screen of a Saccharomyces cerevisiae genomic library, using as a probe a Rho cDNA from Aplysia californica (Madaule and Axel, 1985; Madaule etal. 1987). RHO1 is an essential gene adjacent to MRP2, which codes for a ribosomal protein of the mitochondrion. The two genes are convergently transcribed, with 281 base pairs separating their termination codons, and their transcripts overlap by at least 111 base pairs (Peterson and Myers, 1993). This gene locus has been mapped physically to chromosome XVI (Myers et al. 1987). The GenBank accession number for RHO1 is M15189.
Rab22
Authors: Olkkonen Vesa M 
Published: November 2023

Abstract
The sequence was first identified in the PCR study of Chavrier et al. (1992). Here, Rab/Rho-related sequences were amplified from adult mouse kidney cDNA using degenerated oligonucleotides corresponding to two of the conserved sequence stretches of Rab/Rho GTPases as primers. The PCR-Rab14 sequence was used for probing an MDCK li cell cDNA library. The sequence of the complete open reading frame (ORF) obtained (Fig. 1) was renamed Rab22 (Olkkonen etal. 1993). The EMBLdatabase/GenBank accession number of the sequence is Z22820.
Rab-GDI
Authors: Sasaki Takuya , Kikuchi Akira , Kaibuchi Kozo , Takai Yoshimi 
Published: November 2023

Abstract
Rab-GDI was purified from bovine brain cytosol and its cDNA was cloned based on the amino acid sequences (Sasaki et al. 1990; Matsui et al. 1990). Human Rab-GDI cDNA was isolated from a human brain cDNA library by use of bovine Rab-GDI cDNA as a probe (Asada et al., unpublished results). Recently, a closely related homolog of Rab- GDI has been cloned from Drosophila ovary (Zahner and Cheney, 1993). Two closely related homologs of Rab-GDI have also been cloned from rat brain (Nishimura et al. 1994).
Sec4p
Authors: Novick Peter 
Published: November 2023

Abstract
Temperature-sensitive, conditionally lethal sec4 mutants were isolated by a density enrichment protocol (Novick et al. 1980). The best characterized sec4 allele is sec4-8. Within 5 min of a shift to the restrictive temperature, sec4-8 cells display a block in the transport of invertase, and accumulate 100-nm secretory vesicles containing fully processed cell surface proteins (Novick et al. 1981; Salminen and Novick 1987).
Betlp/Slyl2p
Authors: Ferro-Novick Susan 
Published: November 2023

Abstract
DNA sequence analysis of the BET1 gene predicts a protein (142 amino acids) that is serine-rich at its amino-terminus. The BET1 sequence also predicts the presence of a 131-bp intron that contains a non-conserved 5*-splice site (GTATGA). BET1 shares certain structural features with BOS1. Both genes contain introns and encode small proteins that have a hydrophobic stretch of amino acids at or near their COOH-termini (Dascher eta/. 1991; Shim etal. 1991; Newman etal. 1992).
Slylp
Authors: Schmitt Hans Dieter , Dascher Christiane , Gallwitz Dieter 
Published: November 2023

Abstract
The dominant SLY1-20 mutant allele of S. cerevisiae was isolated from a genomic library made with DNA from a SLY1-20 mutant strain (Dascher et al. 1991). The genomic yeast DNA had been partially digested with Taql and inserted into the C/a/ site of the centromer vector YCp50. Galactose-dependent GAL10-YPT1 cells containing the SLY1-20 allele on a plasmid can grow on glucose-contain- ing media. As the original SLY1-20 mutant, the cloned allele enables the cell to survive the deletion of the YPT1 gene.
Ypt5 (Schizosaccharomyces pombe)
Authors: Armstrong John 
Published: November 2023

Abstract
The ypt5 gene was isolated by hybridizing a S. pombe genomic library with mixed oligonucleotides encoding the conserved sequence DTAGQE (Fawell et al. 1992, Armstrong etal. 1993). The sequence, which includes seven introns, is shown in Fig. 1(A). The positions of the introns were confirmed by isolation and sequencing of cDNA. The EMBL accession number Z22220.
Interleukin-la, Interleukin-ip, and Interleukin-1 Receptor Antagonist (IL-la, IL-1 p, and IL-lra)
Authors: Dower S K , Sims J E 
Published: November 2023

Abstract
Catabolin, endogenous pyrogen (EP), osteoclast activating factor (OAF), lymphocyte activating factor (LAF), epidermal cell derived thymocyte activating factor (ETAF), serum amyloid A inducer or hepatocyte stimulating factor (HSF), leucocyte endogenous mediator (LEM), fibroblast activating factor (FAF), B cell activating factor (BAF), proteolysis inducing factor (PIF), haemopoietin-1 (H-1).
Interleukin-2 (IL-2)
Authors: Greene M A Goldsmith ,W C 
Published: November 2023

Abstract
IL-2 is a 15.5 kDa glycoprotein secreted primarily by activated T lymphocytes. The mature human IL-2 protein contains 133 amino acid residues, while the homologous proteins in other species contain 133 to 149 amino acids. The IL-2 primary translation product undergoes several post-translational processing steps that include removal of an Nterminal signal peptide, glycosylation at Thr 3, and disulphide linkage of Cys 58 and Cys 105. Glycosylation appears to be dispensable for IL-2 function, but formation of the disulphide bond is critical for bioactivity of the resultant molecule (Robb et al. 1983). IL-2 appears to be a very stable protein, exhibiting resistance to both heat and acidic pH. An X-ray crystallographic study of human IL-2 demonstrated that it is a largely helical molecule, with a-helices representing approximately 67 per cent of the entire protein (Brandhuber et al. 1987). A proposed structure derived from these studies contains six distinct helical domains involving 89 amino acids (Fig. l(a)). However, an alternative three-dimensional structure was subsequently described which appeared to accommodate the carbon backbone data provided by the above analysis and simultaneously to incorporate the results of mutational studies defining the site of ligand-receptor binding (Bazan 1992).
Interleukin 8 and Related Chemokine a Family Members
Authors: Taub D D , Oppenheim J J 
Published: November 2023

Abstract
The chemokine a family members from mouse and man exhibit a great deal of homology in their amino acid sequences (Fig. 1) (Oppenheim et al. 1991; Schall 1991). The cDNAs code for a precursor protein which contains a leader sequence. This presumably enables the chemokines to be secreted and enzymatically cleaved to yield a mature form. The mature form of all chemokine a proteins contains four cysteine residues which form two disulphide bridges. The first two cysteines in this subfamily are separated by only one amino acid. Members of this family are typically secreted as non-glycosylated dimers and tetramers containing between 66 and 80 amino acids in their mature monomeric protein form (Oppenheim et al. 1991; Schall 1991; Matsushima et al. 1992).
Interferon-Gamma (IFNy)
Authors: Gray P W 
Published: November 2023

Abstract
The human IFNycDNA (GenBank accession number X13274) encodes a 143-amino-acid mature protein with a 23 residue signal sequence (Gray et al. 1982). The activity of IFNy is species specific due to the low level of homology between different species sequences. Mouse IFNy only contains 40 per cent identical residues (Gray and Goedde/ 1983). The mouse cDNA (GenBank K00083) encodes a 133 residue mature protein with a 22 amino acid signal sequence (Gray and Goedde/ 1983).
Receptor for Granulocyte Colony-Stimulating Factor (G-CSF)
Authors: Nagata S 
Published: November 2023

Abstract
The nucleotide sequences of mouse and human G-CSF receptor cDNAs (GenBank accession numbers M58288 and M59820) predict a protein of 837 (mouse) or 836 (human) amino acids each containing a 25- or 23-amino-acid leader sequence (Fukunaga et al. 1990a, 1990b; Larsen et al. 1990). Human and mouse G-CSF receptors have marked homology (62.5 per cent) at the amino acid sequence level, and the two G-CSF receptors cross-react in their G-CSF binding and signal transducing activities. The G-CSF receptor has a significant overall similarity with the gpl30 (the interleukin 6 receptor signal transducer) and leukaemia inhibitory factor receptor (Fig. 1) (Nagata and Fukunaga 1991, 1993).
Insulin-like Growth Factors (IGFs)
Authors: LeRoith D , Roberts C T 
Published: November 2023

Abstract
The nucleotide sequences encoding IGF-1 and IGF-II have been characterized for most major vertebrate species. The mammalian IGF-1 genes are large, spanning over 90 kb of chromosomal DNA [GenBank accession numbers X57025 (cDNA) and X03419 (gene)]. The human IGF.
Vascular Endothelial Growth Factor (VEGF)
Authors: Ferrara N , Park J E 
Published: November 2023

Abstract
VEGF purified from conditioned media of normal and neoplastic cells is a glycoprotein of -45000 kDa (Ferrara and Henzel 1989). It is inactivated by reducing agents but it is heat- and acid-stable. By alternative splicing of RNA, VEGF may exist in four different homodimeric isoforms (Leung et al. 1989; Houck et al. 1991; Tisher et al. 1991). Following signal sequence cleavage, human VEGF monomers are expected to have 121, 165, 189, and 206 amino acids, respectively (VEGF121, VEGF165, VEGF189, VEGF206). Rodent or bovine VEGF monomers are shorter by one amino acid.
Endothelin and Its Receptors
Authors: Luscher T F 
Published: November 2023

Abstract
Endothelins are products of three distinct genes [GenBank accession numbers (AC): Y00749 (Endothelin-1), M65199 and X55177 (Endothelin-2), and X52001 (Endothelin-3)]. 2.2 kb human preproendothelin messenger RNA is encoded on chromosome 6 in five exons which are distributed over nearly 7 kb of the genome. The 5’ flanking region contains several response elements which confer inducibility of transcription by phorbol esters (e.g. fos/jun complex inducibility), nuclear factor-1 (responsible for transforming growth factor beta-induced expression) and hexanucleotide sequence elements, which may be involved in induction byacute physical stress.
The small heat shock proteins — an overview
Authors: Buchner J , Gaestel M , Vierling E 
Published: November 2023

Abstract
11 kDa-late embryogenesis abundant protein, 14 kDa- Myobacterium tuberculosis antigen, 18 kDa-M. leprae antigen, 25 kDa-growth-related protein, 25 kDa-inhibitor of actin polymerization, aB-crystallin, a-crystallin B-chain, AV25 protein, C14B9.1 protein, estrogen-regulated ‘24K’ protein, estrogen receptor-related protein, Hsp16, Hsp16.3, Hsp16.9, Hsp17, Hsp17.1, Hsp17.3, Hsp17.4, Hsp17.5, Hsp17.6, Hsp17.7, Hsp17.8, Hsp17.9, Hsp18, Hsp18.1, Hsp18.2, Hsp18.5, Hsp18.6, Hsp20, Hsp21, Hsp22, Hsp22.3, Hsp22.5, Hsp22.7, Hsp23, Hsp23.5, Hsp23.9, Hsp25, Hsp26, Hsp26.6, Hsp27, Hsp30, Hsp42, IbpA, IpbB, low molecular weight/mass Hsp, IAP-25, p25, p27, pPf203.
Small heat shock protein Hsp25 from mouse, rat
Authors: Gaestel M , Buchner J 
Published: November 2023

Abstract
Rodent/murine low molecular weight heat shock protein (Arrigo, Landry, 1994); mouse Hsp27/28 (Zantema etal., 1992); rat Hsp27/28 (Uoshima etal., 1993); 25 kDa growth-related protein p25 (Benndorf et al., 1988; Oesterreich etal., 1990).
Escherichia coli thioredoxin
Authors: Nakamura H , Bjornstedt M , Holmgren A 
Published: November 2023

Abstract
Escherichia coli B thioredoxin was originally purified to homogeniety from a neutralized pH 5.0 supernatant by heat treatment to 85°C, followed by chromatography on DEAE-cellulose, Sephadex G-50 (Holmgren, Reichard, 1967). A source of E. coli thioredoxin is the K12 strain, SK 3981 (Lunn, et al., 1984), which contains a derivative of the plasmid pBR325 (pBHK8) into which- a 3 kb Pvu II fragment of E. coli DNA containing the thioredoxin gene was inserted.
Synechococcus TxIA
Authors: Grossman A , Collier J 
Published: November 2023

Abstract
The nucleotide sequence of the txlA gene was determined (Collier, Grossman, 1995) from a genomic clone isolated from the cyanobacterium Synechococcus sp. strain PCC7942 (GenBank accession number U05044). The sequence predicts a protein of 191 amino acids, with an isolelectric point of 4.2. While the N-terminal 37 amino acids, the C-terminal 44 amino acids show no homology to sequences in the GenBank database, the central sequence of 110 amino acids is similar to a number of protein disulfide oxidoreductases, including thioredoxins (Buchanan, 1991), protein disulfide isomerases (Bardwell, Beckwith, 1993).
BS2: Trypanosoma brucei protein disulfide isomerase homologue
Authors: Bangs J D 
Published: November 2023

Abstract
African trypanosomes of the T. brucei species (Order Kinetoplastida) are parasitic protozoa that are the causative agents of African trypanosomiasis (African sleeping sickness) in humans, Nagana in cattle (Vickerman et al., 1993). Analyses of 18S rRNA sequence homologies indicate that these organisms comprise one of the most ancient of all eukaryotic lineages, being as distant phylogenetically from yeast as they are from humans (Sogin et al., 1989).
Saccharomyces cerevisiae Scc3/Cpr4
Authors: Contreras R , Demolder J 
Published: November 2023

Abstract
The genomic sequence of the SCC3 gene (Accession numbers: EMBL: X59720; PIR: S26658; HSSP: PO5092; PROSITE: PS00170) was originally identified during the sequencing of chromosome III in the overlap of the insert of phages PM5307 and PM6589 (Franco etal., 1991). SCC3 corresponds to the third cyclophilin gene from 5. cerevisiae. It is present as a single copy in the genome. Analysis of the 5’ non-coding region of SCC3 shows a TATA box at -135, a putative CAAA (at -78) and a CAPyACA (at -64) promotor motif. No upstream activating sequences are detected, which is reflected in Northern analysis which indicates that SCC3 renders an abundant 1.2 kb transcript during exponential growth. The 3’ non-coding region of SCC3 shows a potential sequence (i 111 lATA) at +1054 for polyadenylation.
Three-dimensional structure of FKBPs
Authors: Liang J , Clardy J 
Published: November 2023

Abstract
The mammalian cytosolic FKBP12 protein was discovered through its ability to bind the immunosuppressive agents FK506 (tacrolimus) and rapamycin (sirolimus) (Harding et al., 1989; Siekierka et al., 1989). The FKBP family, for FK506 binding proteins, is growing rapidly, and the best characterized members are the mammalian proteins FKBP12, FKBP13 (Jin et al., 1991), FKBP25 (Galat et al., 1992), and FKBP59 (Tai et al., 1992).
Escherichia coli FkpA
Authors: Raina S , Missiakas D 
Published: November 2023

Abstract
In Escherichia coli, misfolded proteins accumulating in the cell envelope, that is the periplasm or the outer membrane, induce a stress response that is controlled at the transcriptional level by the Er/ polymerase (Mecsas et al., 1993; Raina etal., 1995; Missiakas etal., 1996a). Unfolding of proteins is quite pronounced in strains lacking major periplasmic catalysts such as the Dsb proteins, which are involved in the formation of disulfide bonds of exported proteins (Bardwell, 1994; see entries on the Dsb proteins, pp. 318–328).
Plant FKBP73
Authors: Blecher O , Breiman A 
Published: November 2023

Abstract
FKBP73 of wheat is a PPIase (peptidyl-prolyl cis-trans isomerase) member of the FKBP (FK506-binding protein) family, being most homologous to mammalian FKBP52. Uniquely, the deduced amino acid sequence contains three FKBP12-like domains, a calmodulin-binding site and a putative TPR (tetratricopeptide) motif. The wheat FKBP73 is abundant in highly dividing tissues and an additional isoform of 71 kDa is associated with mature cells.
The amino acid sequence deduced from the nucleotide sequence of a cDNA clone isolated from a wheat root tip cDNA library (EMBL accession number X86903) reveals an open reading frame of 559 amino acids with calculated molecular mass of 62 kDa and with electrophoresis mobility of 73 kDa on SDS-PAGE (Blecher et al., 1996). The N- terminal amino acid sequence does not reveal similarity to mitochondrial or chloroplast targeting sequences.
Mammalian FKBP12
Authors: Siekierka J J 
Published: November 2023

Abstract
The amino acid sequence deduced from a single cDNA clone isolated from a phytohaemagglutinin (PHA)-stimulated human T-cell library (GenBank accession number M34539; Maki etal., 1990) reveals a protein of 108 amino acids and a molecular weight of 11 951 Da in agreement with the molecular mass estimated by SDS-PAGE (Siekierka et al., 1989b). No significant homology was observed at that time with other sequences in the GenBank and EMBL databases. Hydropathy analysis did not reveal any significant hydrophobic stretches indicative of a signal peptide or transmembrane region and is consistent with the cytoplasmic localization of FKBP12. A physical map of the human FKBP12 gene has been obtained and the gene has been mapped to chromosome 20 (DiLeila and Craig, 1991).
Mammalian FKBP51
Authors: Smith D F 
Published: November 2023

Abstract
FKBP51 was originally noted as a component of native chicken progesterone receptor complexes (Smith et al., 1990), but cDNAs for mouse FKBP51 were independently isolated in two laboratories. The gene for FKBP51 was one of several identified in the WEHI-7TG murine thymoma cell line whose expression was increased during glucocorticoid-induced apoptosis (Baughman et al., 1991) . A cDNA for FKBP51 was subsequently sequenced and shown to be a novel FKBP (Baughman etal., 1995). In a separate study (Yeh et al., 1995), a cDNA for FKBP51 was cloned based on the accumulation of the mRNA during the clonal expansion phase of 3T3-L1 cell growth. A cDNA sequence for human FKBP51 has also recently been obtained (Nair etal., 1997).
Escherichia coli parvulin
Authors: Fischer G , Rahfeld J -U 
Published: November 2023

Abstract
Parvulin (latin: parvulus, very small) is the first member of a new family of PPIases, sharing no sequence homology in their amino acid sequence to the cyclophilins or FKBPs. The enzyme was purified from Escherichia coli cells by monitoring the enzymatic activity with the protease-coupled PPIase assay. The mature enzyme consists only of 92 amino acid residues. To our knowledge parvulin represents the smallest known enzyme being enzymatically active as a monomer.
The amino acid sequence of parvulin was determined by Edman degradation (Rahfeld et al., 1994a). The corresponding gene was identified by translation from the amino acid sequence using the TFASTA (Rahfeld et al., 1994a) or TBLASTN (Rudd et al., 1995) program. It was localized in the E. coli genome between 84.5 and 86.5 minutes, a previously unidentified open reading frame between the E. coli ilvC and rep genes in the ECOUW85U sequence (Daniels et al., 1992). This gene encodes a protein consisting of 93 amino acid residues (PIR accession number S45525).
Vertebrate p60
Authors: Johnson J L 
Published: November 2023

Abstract
IEFSSP3521 (Honore etal., 1992).
p60 was first observed to be up-regulated twofold in SV40-transformed human fibroblasts and also up-regulated by stress (Honore et al., 1992). Using peptides generated from purified protein, p60 was further identified as the 60 kDa protein that copurifies with immunoprecipitated avian Hsp90 (Smith etal., 1993).
Vertebrate Hsp47
Authors: Nagata K 
Published: November 2023

Abstract
Colligin (Kurkinen etal., 1984) and J6 protein (Wang and Gudas, 1990) in mice, and gp46 in rats (Cates etal., 1987) and in humans (Clarke and Sanwal, 1992).
Hsp47 was originally identified as a gelatin-binding protein from chick embryo fibroblasts (Nagata and Yamada, 1986). Therefore, Hsp47 can be easily purified by a single step of affinity chromatography on gelatin- Sepharose or collagen-Sepharose following cell lysis with 1% Nonidet P-40 (Kurkinen et al., 1984; Nagata and Yamada, 1986).
Carboxypeptidase Y and its propeptide
Authors: Winther J R 
Published: November 2023

Abstract
Carboxypeptidase Y (CPY) is a resident of the yeast vacuole (equivalent to the lysosome in mammals). It is synthesized as a zymogen (procarboxypeptidase Y; proCPY) which contains a 91 amino acid N-terminal propeptide. The propeptide is essential for folding of the protein in vivo. In vitro, CPY is unable to refold in the absence of high concentrations of salt, while proCPY refolds efficiently. Under high salt conditions CPY refolds with a low efficiency, and the isolated propeptide is able to stimulate folding of the enzyme through low-affinity interactions.
Ribosome-associated chaperones and protein synthesis: molecular machines catalysing protein targeting, folding and assembly
Authors: McColl D , Hartl F U 
Published: November 2023

Abstract
The process of polypeptide translation, intracellular targeting and folding is a highly complex biochemical reaction. During translation, several events occur while the polypeptide is present as a ribosome-bound nascent chain that determine its ultimate fate in the cell. First, misfolding and aggregation of nascent chains are prevented. Secondly, the correct cellular location of the emerging nascent chain is determined based on the presence of targeting sequences such as an N-terminal signal sequence. Targeting to the correct cellular location may require translocation across intracellular membranes such as those of the endoplasmic reticulum (ER) and mitochondria. In order for this to occur, nascent polypeptides must be maintained in an unfolded state. Finally, polypeptides must be folded to their correct native state or be assembled into homo- or hetero-oligomeric complexes.
The periplasmic unfolded protein response in Escherichia coli
Authors: Raina S , Missiakas D 
Published: November 2023

Abstract
Misfolding of proteins in Escherichia coli triggers two stress responses. Accumulation of misfolded proteins in the cytoplasm induces the ‘classical’ heat shock regulon controlled by the σ32 polymerase. In contrast, misfolding of proteins in the extracytoplasm induces the newly described EσE dependent regulon. Such an intercompartmental organization implies the presence of signal-transducing molecules located in the periplasm and in the inner membrane. EσE, by itself, is the master regulator of the heat shock response since it ensures, at high temperatures, the transcription of the rpoH gene encoding σ32.
Mammalian Grp94
Authors: Melnick J , Argon Y 
Published: November 2023

Abstract
Endoplasmin (Koch etal., 1986), ERp99 (Mazzarella, Green, 1987), hsp 108 (Sargan etal., 1986), gp96 (Li, Srivastava, 1993). Grp94 was isolated by several independent approaches. Biochemically, it was identified as the major concanavalin A-binding protein in rough microsomes (Koch et al.,
1986), as a component of the chicken progesterone receptor (Sargan et al., 1986),, as the major protein responding to either glucose starvation (Lee et al., 1983) or to differentiation signals (Mazzarella, Green, 1987) .