bluuebunny/crossref_metadata_2025_split huggingface dataset:
R-Ras
Authors: Fernandez-Sarabia Maria Jose , Bischoff James R 
Published: November 2023

Abstract
The human R-ras gene was originally isolated by low stringency hybridization with a v-H-ras probe (Lowe etal. 1987). The human R-ras gene contains six exons and the exon-intron organization in R-ras differs from that of H-, K-, and N-ras protooncogenes (Lowe et al. 1987). The human R-ras gene has been localized to chromosome 19 (Lowe et al. 1987). The murine R-ras gene shares 88% nucleotide identity to human R-ras and is localized to chromosome 7 (Lowe etal. 1987).
Rap2a
Authors: Peterson Scott N , Lapetina Eduardo G 
Published: November 2023

Abstract
Rap2a was cloned from a Raji human Burkitt lymphoma cell line cDNA library using the Dras3 gene from Drosophila melanogaster as a probe under low stringency hybridization conditions (Pizon et al. 1988). This clone was named rap2. Upon the cloning of a second rap2 gene (Ohmstede et al. 1990; Farrell et al. 1990), the original clone was renamed rap2a. The DNA sequence and deduced amino acid sequence of human rap2a (Pizon et al. 1988) are shown in Fig. 1. The GenBank accession number is X12383.
Rap2b
Authors: Peterson Scott N , Lapetina Eduardo G 
Published: November 2023

Abstract
Rap2b was cloned by screening a platelet cDNA expression library with the monoclonal antibody M90, which recognizes the highly conserved epitope of H-Ras between amino acids 107-130 (Ohmstede et al. 1990). The DNA sequence and deduced amino acid sequence of human Rap2b (Farrell etal. 1990) are shown in Fig. 1. The GenBank accession number is X52987.
Let-60 Ras
Authors: Sternberg Paul W , Han Min 
Published: November 2023

Abstract
LET-60 was identified by molecular cloning of the C elegans let-60 locus, which was genetically identified by mutations that perturb vulval induction (Beitel etal. 1990; Han etal. 1990) orcause lethality (Rogalski etal. 1982). The DNA sequence is shown in Fig. 1. The GenBank accession number is M5535.
She
Authors: Pelicci Giuliana , Lanfrancone Luisa , Pelicci Pier Giuseppe 
Published: November 2023

Abstract
She was identified by low stringency screening of the human KG1 myeloid leukemia cDNA library using a DNA probe representative of the SH2 domain of the c-fes cytoplasmic tyrosine-kinase (Pelicci etal. 1992). The nucleotide sequence of the She cDNA is shown in Fig. 1. The GenBank accession number is X66321.
Ras-GRF
Authors: Feig Larry A 
Published: November 2023

Abstract
The complete Ras-GRF cDNA was isolated and then sequenced from both the mouse (Cen et al. 1992; Martegani eta/. 1992) and rat (see Fig. 1)(Shou etal. 1992). The former was accomplished by complementation of a mutant yeast strain lacking the Cdc25 gene, and the latter by mixed oligo polymerase chain reation (PCR) after prediction of amino acids that might be conserved among species. In one case, cDNAs were isolated that suggested smaller forms of Ras-GRF might be expressed in brain by alternative splicing (Cen etal. 1992).
MAP kinase activators: Mekl, Mek2
Authors: Leevers Sally , Marshall Chris 
Published: November 2023

Abstract
Sequencing of cDNAs from mouse, rat, rabbit, human and hamster has revealed that there are at least two Mek genes encoding Mekl and Mek2 (Ashworth etal. 1992; Crews et al. 1992; Otsu et al. 1993; Seger et al. 1992; Wu et al. 1993a,b; Zheng and Guan 1993). In addition, there is evidence for an alternatively spliced form of Mekl (Mekl b) that lacks 26 amino acids between domains V and Via (Seger et al. 1992). Mekl and Mek2 have a proline rich domain between kinase subdomains X and XI. In Xenopus laevis cDNA cloning has revealed the existence of a homologue of Mekl, XMEK1 (Kosako et al. 1993), as well as a predicted protein (XMEK2) that lacks the proline rich domain (Yashar etal. 1993).
Ras2p
Authors: Fasano Ottavio 
Published: November 2023

Abstract
The RAS2 gene was identified by screening a yeast DNA genomic library under low stringency with a vertebrate RAS probe (DeFeo-Jones et al. 1983; Powers et al. 1984). GenBank accession numbers are K01971 and X00528 for the coding region and X52411 for the promoter region.
Bud5p
Authors: Chant John , Pringle John R 
Published: November 2023

Abstract
BUD5 has been isolated in two ways. First, it was identified as a gene that overlaps the MAT locus and is required for producing ordered budding patterns. It was then cloned from a genomic library based on this map position (Chant et al. 1991). Second, BUD5 was also isolated from a high-copy-number plasmid library as a clone that could provide partial CDC25 function when overexpressed (Powers et al.
The Rho subfamily of small GTPases
Authors: Hall Alan 
Published: November 2023

Abstract
Rho (Ras homology) was first picked up back in 1987 from an Aplysia cDNA library as a cloning artefact! Despite this inauspicious start, it turned out to be the founder member of a new and very interesting subgroup of the Ras GTPase superfamily that so far includes nine mammalian (RhoA,B and C; Rac1 and 2; CDC42Hs and G25K; RhoG and TC10) and five Saccharomyces cerevisiae (Rho 1,2,3,4 and CDC42Sc) proteins. Members of the Rho subfamily each have around 30% amino acid identity to Ras and have a carboxy-terminal ‘CAAX’ box used as a signal for posttranslational modification. Consequently, it has generally been assumed that Rho-like proteins probably act like Ras at the plasma membrane to regulate signal transduction pathways.
Cdc42p
Authors: Johnson Douglas I , Pringle John R 
Published: November 2023

Abstract
CDC42 was first isolated in S. cerevisiae by complementation of the cdc42-1ts mutation (Adams et al. 1990) using a genomic DNA library (Johnson and Pringle 1990; GenBank accession number X51906). The 5. pombe CDC42 homolog was isolated by complementation of the S. cerevisiae cdc42-1ts mutation using a S. pombe cDNA library (Miller and Johnson 1994; GenBank accession number L25677) and by screening a 5. pombe cDNA library using mixed oligonucleotides corresponding to conserved regions of Ras-like GTPases (Fawell et al. 1992; GenBank accession number M83650).
Rab6
Authors: Goud Bruno 
Published: November 2023

Abstract
Rab6 was originally identified by screening a human pheochromocytoma cDNA library with a probe derived from the human rab3A cDNA (Zahraoui et al., 1989). The DNA sequence of human Rab6 is shown in Fig. 1. The Genbank/EMBL accession number is JO4941.
Rab7
Authors: Bucci Cecilia , Chiariello Mario , Bruni Carmelo Bruno 
Published: November 2023

Abstract
Rab7 was first identified by screening a cDNA library from BRL-3A cells (buffalo rat liver) and initially called BRL-ras (Bucci et al. 1988). Later, a cDNA library from MDCK (Madin-Darby canine kidney) cells was screened with degenerated oligonucleotides made in the conserved domains and the canine clone was isolated (Chavrier et al. 1990). The protein was then renamed Rab7 due to its high homology to the members of the Rab protein family. In Fig. 1(A), the rat coding cDNA and amino acid sequence is shown. Northern blot analysis has demonstrated that two messenger RNAs were present (Bucci etal. 1988): one major species of 2.5 kb and a minor one of 1.5 kb (Fig. 1 (B)).
Rab8
Authors: Huber Lukas A 
Published: November 2023

Abstract
Rab8 was originally identified by screening a cDNA library (Zahraoui et al. 1989; Chavrier et al. 1990) with degenerated oligonucleotides corresponding to the amino acid sequence WDTAGQE (these seven residues are strictly conserved in Ypt1, Sec4 and all of the proteins of this subfamily identified so far). The DNA sequence of canine Rab8 is shown in Fig. 1. The EMBL accession number is X56385.
Sec22p
Authors: Ferro-Novick Susan 
Published: November 2023

Abstract
DNA sequence analysis has revealed that SEC22 is structurally similar to BET1 and BOS1 (see chapter ‘Bet1’) and encodes a 25-kDa protein. Sec22 protein is hydrophilic with a hydrophobic carboxy-terminal stretch of amino acids that are potentially membrane spanning (Dascher et al. 1991; Newman etal. 1992).
Ypt2
Authors: Mundt Maren , Gallwitz Dieter 
Published: November 2023

Abstract
The ypt2 gene was isolated from total genomic 5. pombe DNA using a protein-coding fragment of the S. cerevisiae YPT1 gene (Gallwitz et al. 1983) as hybridization probe (Haubruck et al. 1990). The protein-coding region of the gene is not interrupted by introns. The ypt2 gene has been mapped on the right arm of chromosome I, approximately 2.5 cM apart from ura2 (Miyake et al. 1991). The DNA sequence of ypt2 (Haubruck et al. 1990) is shown in Fig. 1. The GenBank accession number is X52469.
The ARF subfamily
Authors: Kahn Richard A 
Published: November 2023

Abstract
Unlike most of the members of the Ras superfamily, Arf was identified first as an activity and then as a distinct protein and only later as a family of structurally related proteins. As a result, many of the activities assigned to Arf can still only be ascribed to the subfamily (rather than one specific gene product) as the Arf prepared from mammalian sources is a mixture of several gene products. Earlier suggestions that distinct Arf proteins reside in membrane versus cytosol fractions have proven misleading. Rather, one of the more interesting features of Arf action in cells is the dynamic aspect of its reversible association with membranes (see below).
Arf6
Authors: Kahn Richard A 
Published: November 2023

Abstract
A chicken-processed pseudogene, termed CPS1 (accession number P26990; Alsip and Konkel 1986), was originally cloned by serendipity and thought to be a novel Ras protein, as no other small GTP-binding proteins were known at that time. With the cloning of a human homologue (accession number P26438; Tsuchiya, etal. 1991), it became clear that this gene is expressed in humansand, by extension, probably in chickens as well, and it was renamed ARF6 at that time as the ARF family was by then well-established. The human ARF6 was cloned from a differentiated HL-60 lambda cDNA library by cross-species hybridization with the bovine ARF2 probe (Tsuchiya, eta/. 1991). Two different message sizes, 1.8 and 4.2 kb, were detected in a panel of tissues and mammalian species (Tsuchiya, etal. 1991).
Sarlp
Authors: Barlowe Charles , Schekman Randy , Nakano Aki 
Published: November 2023

Abstract
The SAR1 gene (EMBL accession number X51667) contains an intervening sequence that after splicing predicts an open reading frame of 190 amino acids. SAR1 cDNA sequencing confirms the excision of a 139 bp intron. Sari protein contains the four consensus motifs characteristic of GTPases (Bourne et al. 1991), although there are other notable features contained within the protein sequence. Sari p does not contain a C-terminal cysteine or an N-terminal glycine as potential residues for lipid modification, a feature observed in a number of other small GTPases.
Escherichia coli Hsc66
Authors: Kawula T H 
Published: November 2023

Abstract
The hscA gene sequence (£. coli K-12 accession number U01827, E. coli B U05338) encoding Hsc66 revealed that this protein is composed of 615 amino acids totalling 65 913 Da with an isoelectric point of 4.93. Hsc66 classification as an HSP70 protein is based on the fact that the amino acid sequence of this protein is 42% identical, 62% similar to the classic E. coli HSP70 protein DnaK (Kawula, Lelivelt, 1994; Seaton, Vickery, 1994), ,contains perfect matches to two amino acid sequences conserved among all of the known HSP70 proteins.
The HSP110/SSE stress proteins — an overview
Authors: Easton D P , Subjeck J R 
Published: November 2023

Abstract
The proteins so far identified as members of the HSP110/SSE family (Lee-Yoon et al., 1995) are: yeast stress seventy proteins Sse1, Sse2 (D13908, D13909, Mukai et al., 1993; Shirayama et al., 1993), C30c11.4, Caenorhabditis elegans hypothetical protein (GenBank accession number Q05036, Wilson etal., 1994); sea urchin egg receptor for sperm (L04969, D67016, Foltz et al., 1993; but see Just et al., 1997), human B lymphocyte HSP70-like protein, Hsp70RY (L127123, Fatallah et al.,
Human Hdj2
Authors: Chellaiah A , Davis A , Mohanakumar T 
Published: November 2023

Abstract
An hdj2 cDNA clone was originally isolated from a A-gt11 human umbilical vein endothelial cDNA library (HUVE) using a monoclonal antibody, SK2H10, which reacts specifically to human endothelial cells, monocytes (Schook et al., 1987; Wood et al., 1988). The cDNA clone consists of 1275 nucleotides (GenBank accession number L08063) with an open reading frame (ORF) of 1191 nucleotides (Chellaiah etal., 1993). BLAST comparison of nucleic sequences showed that Hdj2 is 99% homologous to another human cDNA, isolated from a human fibrosarcoma HT-1080 cDNA library, that encodes a homologue (HSDJ) of the DnaJ protein (Oh et al., 1993). Considering the utilization by the yeast Saccharomyces cerevisiae of multiple DnaJ-like proteins (see earlier entries in this section), it is not surprising to find three DnaJ homologues in humans (Cheetham et al., 1992; Chellaiah etal., 1993; Oh etal., 1993).
SPARC
Authors: Celio Marco R 
Published: November 2023

Abstract
SPARC, BM-40, and osteonectin are synonyms for identical proteins initially identified from different sources, such as bone (Termine et al. 1981), endothelial cells (Sage et al. 1984; Mason et al. 1986), platelets (Stenner et al. 1986), and basement membranes (Dziadek et al. 1986). Comparison of cDNA sequences have shown that all these proteins are identical molecules or interspecies homologs and that they are the product of a single gene. The acronym SPARC (secreted protein acidic and rich in cysteine) is perhaps the most appropriate name for this protein, because both other names refer to only part of its widespread extracellular tissue localization.
Bacterial calcium-binding proteins
Authors: Celio Marco R 
Published: November 2023

Abstract
The importance of Ca2+ in bacterial physiology is at last being confirmed (for references see Lynn and Rosen 1987; Norris et al. 1991a; Onek and Smith 1992). Almost 20 years after Ca2+ was first implicated in bacterial chemotaxis, manipulations of putative Ca2+channels and intracellular Ca2+ levels in Escherichia coli have been clearly shown to affect chemotaxis (Tisa et al. 1993). Examples of bacterial differentiation that reveal a connection with Ca2+ now include sporulation, fruiting body formation, gliding and heterocyst formation. Ca2+ is also implicated in the cell cycle, with intracellular Ca2+ apparently increasing during cell division in E. coli. Such division entails formation of non-bilayer structures which may depend on Ca2+(Rietveld et al. 1993). Clarification of the role of Ca2+in the heat shock response awaits discovery of a role for Ca2+ in phosphorylation of DnaK in vivo (see below). The role of Ca2+ in bacterial disease now extends from the expression of virulence-related genes in strains of Yersinia pestis and dental plaque formation in Streptococcus mutans to nodulation in the “parasitic” relationship between Rhizobium spp. and plants.
Calreticulin
Authors: Celio Marco R 
Published: November 2023

Abstract
Calreticulin is a ubiquitous and highly conserved Ca2+-bindinglstorage protein associated with endo(sarco)plasmic reticulum membranes. Calreticulin is a multifunctional protein implicated to play a role in a variety of cellular functions ranging from Ca2+homeostasis to the control of gene expression. Rabbit calreticulin has a calculated molecular weight of 46, 567 (for recent reviews on the structure, function, amino acid sequence and localization of calreticulin see Michalak et al. 1992; Sontheimer et al. 1993; Burns et al. 1994; Nash et al. 1994 and references within). The protein migrates on 5D5 gels with an apparent molecular mass of 60 kDa (at pH 8.0) or of 55 kDa (at pH 7.0). The molecular weight of calreticulin estimated by sedimentation equilibrium is 55,000. The isoelectric point of the human protein is 4.65-4.67 and the protein stains blue with “Stains-All”. Calreticulin contains potential glycosylation sites; however, only bovine and rat liver proteins are shown to be glycosylated. In CHO cells calreticulin undergoes a heat shock-induced glycosylation (Jethmalani et al. 1994). Bovine calreticulin has one disulfide bridge (Cys120-Cys146: Matsuoka eta/. 1994).
Crystallins
Authors: Celio Marco R 
Published: November 2023

Abstract
In bovine !3-crystallin, six or more chains are primary products, whereas some ten others arise by post-translational modifications. cDNAs have been sequenced for cow i3A2 and i3A4 (van Rens et al. 1991; EMBL accession no. M60329 and M60328), bovine i3B1 (Quax-Jeuken et al. 1984; M11850), bovine i3B2 (Hogg et al. 1987; M22466), human i3B3 (Aarts et al. 1989; X15144), human i3B2 (Aarts eta/. 1989; X15144, X15146), human i3A3/A1 (Hogg eta/. 1986; M14301), human i3B2 (Aarts et al. 1987; M18440, L10035), mouse i3A3/A1 (Peterson and Piatigorsky 1986; M21472), mouse i3B2 (Chambers and Russell, 1991; M60559), rat i3B1 (den Dunnen et al. 1986; M13526), rat i3B3 (den Dunnen et al. 1985; X05899), rat i3A3/A1 (Aarts et al. 1989; X15143), chicken i3A3/A1 (Peterson and Piatigorsky 1986; McDermott et al. 1992; M84460), chick i3B1 (Hejtmancik et al. 1986; M 11619), and for frog i3A1 (Luchin et al. 1987; X06421).
Introduction
Authors: Dufourcq J , Castano S 
Published: November 2023

Abstract
The first primordial function of the plasma membrane is to maintain all materials, from macromolecules to small solutes, selectively in the cell, i.e. the membrane is equipped in order to very selectively and efficiently regulate permeability. Consequently, it is not surprising that many bacterial toxins act on the plasma membrane and have evolved to change efficiently the first critical property required for living. Indeed, any unbalanced entry, or efflux of ions or small molecules should be opposed by selective pumps and channels in order to recover, as soon as possible, the physiological conditions by active transport. But if the nonselective fluxes induced by toxins overcome the capabilities of the cells to recover their equilibrium quickly, due either to an important transitory change, ‘a burst’, or to a permanent leakage through a ‘hole’, cells will generally die. This often results from the entry of ions inducing metabolic disorders, like Ca2+ entry, causing entry of water which swells the cell in order to compensate the osmotic pressure due to the presence of concentrated polyelectrolytes inside the cell. Conversely, the escape of vital compounds, again ions and small metabolites, can be lethal. Then all the following toxins have the same effect, they only differ in the way they perform it, in their efficiency in inducing the deleterious imbalance of permeability, and in the detailed structure and mechanism causing an open structure through which lethal leakage will occur.
Cholesterol binding toxins (Streptococcus, Bacillus, Clostridium, Listeria)
Authors: Alouf J 
Published: November 2023

Abstract
The 19 toxins identified to date are produced by gram-positive aerobic or anaerobic, sporulating or non-sporulating bacteria from the genera Streptococcus, Bacillus, Clostridium, and listeria (Smyth and Duncan 1978, Alouf and Geoffroy 1991) listed below in Table 1.Except for PLY, which is intracytoplasmic, the other toxins are secreted in culture medium during bacterial growth. Among the toxin-producing bacteria, only Listeria are intracellular pathogens which grow and release their toxins in host phagocytes or possibly in other cells.
Escherichia coli hemolysin
Authors: Ludwig A , Goebel W 
Published: November 2023

Abstract
E. coli hemolysin (Hly A) is the most extensively studied member of the family of RTX toxins, which represents a group of structurally and functionally related cytolysins and cytotoxins produced by a variety of gram-negative bacteria. In addition to E. coli hemolysin, the RTX toxins include hemolysins from Proteus vulgaris and Morganella morganii, hemolysins, and cytotoxins from Actinobacillus pleuropneumoniae and Actinobacillus suis, leukotoxins from Pasteurella haemolytica and Actinobacillus actino-mycetemcomitans, and the bifunctional adenylate cyclase-hemolysin (adenylate cyclase toxin) from Bordetella pertussis (Coote 1992). All RTX toxins are Ca2+-dependent, pore-forming protein toxins. The most pronounced structural feature of these toxins is the presence of a characteristic repetitive domain, which is composed of a toxin-specific number of highly conserved glycine-and aspartate-rich repeat motifs of nine amino acids (XLXGGXGN/DD). The designation RTX (Repeats in ToXins) was deduced from this common structure.
Adducin
Authors: Matsua Yoichiro , Bennett Vann 
Published: November 2023

Abstract
Adducin is a membrane-skeletal protein localized at spectrin-actin junctions that was first purified from human erythrocytes based on calmodulin-binding activity. Adducin also is a substrate for protein kinases A and C.3–5 Adducin caps the fast-growing end of actin filaments and promotes association of spectrin with actin. Adducin capping activity may target spectrin to the ends of actin filaments and help stabilize the short actin filaments that comprise the spectrin-actin network of erythrocytes.
Introduction
Authors: Kreis Thomas E 
Published: November 2023

Abstract
Intracellular membrane traffic between different subcellular compartments is mediated predominantly by vesicular carriers. These transport processes involve rounds of sorting of cargo into specific domains of an organelle where vesicles bud, directed movement of the transport intermediates to their corresponding acceptor compartments, and subsequent delivery of cargo by fusion of the vesicular and acceptor compartment membranes. Many of the factors building up the protein machinery regulating these processes have been identified and characterized at the molecular level. These proteins include (i) membrane-bound coat proteins which, together with additional factors, regulate cargo sorting and vesicle budding; (ii) structural or scaffold proteins required for establishing and maintaining shape and identity of organelles; and (iii) proteins linking organelles and transport intermediates to cytoskeletal filaments.
AP180
Authors: Ungewickell Ernst 
Published: November 2023

Abstract
AP180 binds to clathrin protomers (triskelions) and promotes their assembly into regular coat structures. This activity can be quantitated in a sedimentation assay by either pelleting or fractionation in 5-30 per cent sucrose gradients. Assembled clathrin is also readily detected by electron microscopy of negatively stained specimens.
MAP1B/MAP5
Authors: Gordon-Weeks Philip , Matus Andrew 
Published: November 2023

Abstract
This protein was originally described under a variety of names of which two, MAP1 B and MAPS, are currently in use. MAP18/MAPS binds to microtubules during successive cycles of repolymerization in vitro (although more weakly than MAP2 and tau protein) and when transfected into cell lines, and immunoaffinity purified MAP18/MAPS promotes the polymerization of tubulin in vitro.
MAP2
Authors: Bustos Rodrigo , Moraga, Daniel , Murphy Doug 
Published: November 2023

Abstract
MAP2 is a monomeric protein that occurs as three primary isoforms, MAP2a, MAP2b, and MAP2c, with approximate molecular weights of 200, 200, and 42 kDa, respectively. The apparent molecular weights of all three isoforms on SDS-PAGE gels are considerably higher. These three isoforms are derived from a single gene by alternative splicing2,3 and are subject to strong developmental regulation in their expression.
MARK protein kinases
Authors: Drewes Gerald , Ebneth, Andreas , Mandelkow Eva-Maria 
Published: November 2023

Abstract
EMK, a mouse putative kinase gene (the encoded protein has not been characterized),4 is probably the murine homologue of MARK2. p78, the human homologue of rat MARK3, was discovered as a marker which localizes to the lateral membrane of human pancreas cells, but is lost upon carcinogenesis.5 In cultures of polarized epithelial (MDCK) cells, a canine homologue of MARK2, termed mPAR, was shown to localize at the lateral membrane, and overexpression of C-terminal fragments resulted in the loss of polarity and cell death.