bluuebunny/crossref_metadata_2025_split huggingface dataset:
Saccharomyces cerevisiae Ssh1p
Authors: Craig E A 
Published: November 2023

Abstract
The Ssh1 protein is encoded by an open reading frame on chromosome 12 (GenBank YSCL8039, accession number U19103) predicted to encode a 657 amino acid protein. The predicted sequence includes an N-terminal sequence with similarity to mitochondrial presequences. Sshlp is imported into the mitochondrial matrix, is cleaved in the process. Sshlp shares most identity (53%) with Ssdp. It is 46, 43% identical to Ssalp, Kar2p of the cytosol, ER lumen, respectively (Schilke et al., 1996).
Mammalian HSP100
Authors: Glover J R 
Published: November 2023

Abstract
To date only a single representative of the HSP100 family has been cloned from a mammalian source. The gene (SKD3) was cloned as a suppressor of a potassium transport defect in yeast, suggesting a potential function for HSP100 proteins in solute transport. In addition to the gene from mouse, the human genome sequencing project has thus far contributed a number of partial cDNA sequences corresponding to HSPIOOs of at least two subfamilies. The prevalence of HSPIOOs in prokaryotes, in multiple subcellular compartments of eukaryotes suggests that many more mammalian HSPIOOs will be identified.
Saccharomyces cerevisiae Ssi1p
Authors: Baxter A K , Craig E A 
Published: November 2023

Abstract
SSI1 was sequenced as part of the yeast genome sequencing project,, identified by its homology of its deduced gene product to known HSP70 proteins (Rasmussen, 1994; Craven etal., 1996; Baxter etal., 1996).
The SSI1 gene (GenBank accession number Z28073) has an open reading frame of 2643 nucleotides, potentially encoding a protein of 881 amino acids with a predicted size of 99.6 kDa.
Calnexin, calreticulin proteins — an overview
Authors: Williams D B 
Published: November 2023

Abstract
cDNA sequences have been determined for calnexin, calreticulin from a variety of species including diverse mammals (see calreticulin, calnexin entries, pp. 299, 304), invertebrates (e.g. GenBank accession numbers L08641 for Schistosoma mansoni calnexin, Hawn et al., 1993; X59589 for Caenorhabditis elegans calreticulin. Smith, 1992; M20565 for Onchocerca volvulus calreticulin, Rokeach et al., 1994),, plants (e.g. Arabidopsis thaliana calnexin Z18242, Huang et al., 1993; N. tabacum calreticulin X85382, Denecke et al., 1995.
Escherichia coli DsbA
Authors: Bardwell J C A 
Published: November 2023

Abstract
The structure of oxidized Escherichia coli DsbA has been determined by X-ray crystallography, originally at a resolution of 2.0 A (Martin et al., 1993), more recently to 1.7 Å (Guddat et al., 1977). The structure consists of two domains, a thioredoxin domain, a helical domain (Fig. 1a). Although the classical thioredoxin fold incorporates a four-stranded β sheet flanked by three helices (Martin, 1995), the thioredoxin domain of DsbA (comprising residues 1-61, 140-189) has an additional N-terminal str,that extends the central β sheet to five strands.
Structure of DsbA
Authors: Guddat L W , Martin J L 
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; Belin, Boquet, 1993; Dailey, Berg, 1993; Alksne et al., 1995), by The dsbB gene is located at 26.5 minutes on the E. coli chromosome (Bardwell etal., 1993; Missiakas et a/., 1993). Its sequence (GenBank accession number L03721) predicts a 20.3 kDa protein with inner membrane localization (Jander et al., 1994).
Escherichia coli DsbC
Authors: Missiakis D , Zapun A , Creighton T E , Raina S 
Published: November 2023

Abstract
The sequence of the dsbC gene (Swiss-Prot accession number P21892) predicts a 25 kDa protein (Missiakas et al., 1994). The amino acid sequence homology between DsbC, other members of the thioredoxin superfamily is restricted to around the active site, with the following conserved motif, FXXXXCXXC. Except for this, the amino acid sequence of DsbC does not show any strong homology with other thiol—disulfide oxidoreductases from Escherichia coli, such as thioredoxin or DsbA, nor with the eukaryotic protein disulfide isomerase (PDI) proteins. Escherichia coli DsbC shares limited sequence homology with TcpG, the Vibrio cholerae DsbA homologue (Missiakas et al., 1994). A DsbC homologue has been described in Erwinia chrysanthemi (66% identical to E. coli DsbC; Shevchik etal., 1994.
Saccharomyces cerevisiae Eug1
Authors: Stevens T H 
Published: November 2023

Abstract
EUG1 (ER protein unnecessary for growth under standard laboratory conditions) was named for its observed mutant phenotype (Tachibana, Stevens, 1992). Overproduction or deletion of the EUG1 gene appears to have no effect on cell viability or function. Yeast cells deleted for EUG1 grow with wild-type rates on rich or minimal media at temperatures from 18 to 40°C, can grow anaerobically. Sporulation is not affected in homozygous eug1& cells, nor is the transport of vacuolar, secreted proteins through the secretory pathway.
Trypanosoma brucei BiP
Authors: Craig E A 
Published: November 2023

Abstract
African trypanosomes of the T. brucei species (Order Kinetoplastida) are parasitic protozoa that are the causative agents of 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). They are digenetic parasites living alternately in the bloodstream of the mammalian host, the midgut, mouthparts of the insect vector, the tsetse fly. Complex differentiation processes occur at each stage of the life cycle, survival in the mammalian host is dependent on the sequential expression of different variant surface glycoproteins (VSG) in a process called antigenic variation. VSG is the major cell surface secretory product of bloodstream trypanosomes comprising 10-20% of total cell protein.
Drosophila melanogaster ninaA
Authors: Zuker C S , Rutherford S L 
Published: November 2023

Abstract
ninaA mutants were originally isolated based on their visual defect by William Pak and co-workers (Pak 1979). Mutant flies can have as much as a 100-fold reduction in Rh1 rhodopsin levels, leading to a dramatic loss of light sensitivity and loss of the prolonged depolarizing after potential (nina = neither inactivation nor after potential) (Larivee etal. 1981; Stephenson etal. 1983); this is a physiological assay that is sensitive to relative rhodopsin levels.
Mammalian cydophilin D
Authors: Livi G P , Bergsma DJ 
Published: November 2023

Abstract
For human cyclophilin D: hCyP3 (Bergsma et al., 1991), Cyp-D (Schneider etal., 1994). Human cyclophilin D is encoded by a cDNA (GenBank accession number M80254) cloned from a Jurkat T cell cDNA library using the cyclophilin A-coding sequence as the probe (Bergsma et al., 1991). The 841 bp nucleotide sequence contains a 621 bp open reading frame predicting a protein of 207 amino acids. Southern blot analysis of human genomic DNA probed with the cyclophilin D cDNA reveals a band pattern consistent with the existence of a single copy gene (Bergsma et al., 1991).
Saccharomyces cerevisiae FKBP12
Authors: Dolinski K , Heitman J 
Published: November 2023

Abstract
The yeast FKBP12 protein was purified by FK506-affinity chromatography and sequenced (Heitman et al., 1991a; Koltin et al., 1991; Wiederrecht et al., 1991). The gene encoding FKBP12, FPR1 (Genbank accession number M60877), was cloned by screening yeast genomic libraries with a PCR product obtained with degenerate oligonucleotide primers based on protein sequence (Heitman et al., 1991a; Wiederrecht et al., 1991). The FPR1 gene was also isolated by complementation of an fpr1 mutation (Koltin et al., 1991). The FPR1 gene encodes a 114 residue protein with a molecular weight of 12 kDa. The protein sequences of yeast and human FKBP12 are 54% identical (Heitman etal., 1991a).
Mammalian FKBP13
Authors: Nigam S K , Burakoff S J 
Published: November 2023

Abstract
FKBP13 was originally isolated from bovine thymus by use of a rapamycin affinity matrix (Jin etal., 1991).
A cDNA clone isolated from a human colon carcinoma cell library (GenBank accession number M65128) encodes a protein of 141 amino acids and a molecular weight of 13 200 Da in agreement with the molecular mass estimated by SDS-PAGE (Jin et al., 1991). Sequence analysis revealed 51% nucleotide homology and 43% amino acid homology to FKBP12 (Jin et al., 1991; see entry p. 420). There is a particuarly strong homology with the PPIase active and drug-binding site of FKBP12, suggesting both similarity of higher structure and molecular mechanism. However, the binding affinity of FK506 for FKBP13 (£,=55 nM) is roughly 50-fold less than for FKBP12, suggesting that it may not be an in vivo target of the drug (Bram et al., 1993). The gene for a yeast homlolog, FKB2, is 57% identical to its human counterpart (Partaledis etal., 1992; Partaledis and Berlin 1993; see entry p. 411).
Drosophila melanogaster dodo
Authors: Maleszka R , Miklos G L Gabor 
Published: November 2023

Abstract
The dodo gene (dod) was identified in the functional analysis of the flightless (fli) region at the base of the X chromosome in Drosophila (Maleszka et al., 1996; see Fig. 1). The genomic analysis was followed by the sequencing of a number of dodo cDNAs from larval and pupal libraries that revealed the existence of two classes of dodo transcripts differing in the lengths of their 3’-untranslated regions. The longer transcript is 1013 bp in length.
The hsp70 genes of mice, men
Authors: Tavaria M , Kola I , Anderson R L 
Published: November 2023

Abstract
Genes encoding proteins of the HSP70 family have been identified, cloned from numerous species, ranging from bacteria to humans. Phylogenetic analysis reveals that these genes have been highly conserved during evolution (Rensing, Maier, 1994). Despite being first identified as stress-inducible proteins, many of these isoforms are expressed in the absence of stress. The constitutively expressed isoforms are expressed throughout the cell, are concentrated at sites of protein synthesis, translocation. These HSP70 proteins act as molecular chaperones which, in association with other molecular chaperones, oversee the folding process of newly synthesized, transported proteins (see reviews by Gething, Sambrook, 1992; Hartl, Martin 1995; this volume, overview of HSP70, p. 3). The role of the stressinducible HSP70 isoforms is less well understood, although increasing evidence supports the long-held belief that these isoforms are involved in the protection and/or repair of stress-induced protein damage.
Vertebrate p23
Authors: Johnson J L 
Published: November 2023

Abstract
p23 is a Hsp90-binding protein that is a component of mature steroid receptor complexes. p23 forms a complex with Hsp90 and immunophilins that is disrupted by the Hsp90-binding agent geldanamycin. p23, or the p23 complex, is necessary for the formation of mature steroid receptor complexes, and may be involved in several diverse signal transduction pathways.
p23 was found to coimmunoprecipitate with inactive chick progesterone receptor complexes, along with Hsp90, p60, and the immunophilins FKBP52, FKBP54 and Cyp40 (Smith et al., 1990; Smith and Toft, 1993; for review see p. 518). Monoclonal and peptide-directed polyclonal antibodies were used to isolate a chicken cDNA from an expression library (Johnson etal., 1994).
The role of molecular chaperones in DNA replication
Authors: ów A Wawrzyn , ícz M Zyl 
Published: November 2023

Abstract
The role of the DnaK/DnaJ/GrpE molecular chaperones has been described in detail for a few DNA replication systems, namely, A, mini-F, mini-P1 and oriC plasmid DNA replication. Only in the case of the A DNA replication system has it been shown that the DnaK/DnaJ/GrpE chaperone machine is directly involved in the initiation process. In all other cases, the DnaK/DnaJ/GrpE chaperones activate the initiation proteins but do not participate during the final DNA replication initiation event. Recently, studies on the bacteriophage Mu DNA replication have suggested that this system could be another example of the direct involvement of molecular chaperones (in this case Clp ATPase) in the initiation process (Levchenko etal., 1995; Kruklitis etal., 1996).
Functions of molecular chaperone proteins in the biogenesis of mitochondria
Authors: Langer T , Neupert W , Schwarz E 
Published: November 2023

Abstract
Molecular chaperone proteins bind non-native protein structures and stabilize them against aggregation. By this means, they affect multiple cellular processes, ranging from folding of newly synthesized polypeptides emerging from ribosomes, cellular protein trafficking, translocation across intracellular membranes, the reactivation of heat- denatured proteins and proteolytic breakdown. This is exemplified by mitochondria whose biogenesis depends on the activity of various chaperone systems. In the cytosol, molecular chaperone proteins maintain nuclear-encoded preproteins in a conformation allowing subsequent membrane translocation. The mitochondrial Hsp70 machinery mediates the vectorial translocation of nuclear encoded preproteins across the mitochondrial membranes. In the mitochondrial matrix space, the Hsp70 and Hsp60 chaperone systems ensure proper folding of newly imported proteins and the proteolytic breakdown of misfolded polypeptides. In addition to these ‘housekeeping’ functions, chaperone activity is required to maintain mitochondrial functions during heat stress. Thus, studying mitochondrial biogenesis, a wide range of chaperone functions have been identified and their modes of action were subsequently characterized at the molecular level. This review will focus on the multiple roles of cytosolic and mitochondrial chaperones in various processes of mitochondrial biogenesis.
Protein translocation into the endoplasmic reticulum
Authors: Lyman S K , Schekman R 
Published: November 2023

Abstract
Translocation of precursors into the endoplasmic reticulum (ER) may occur either cotranslationally, where the polypeptide is threaded through a proteinaceous pore as it spools off the ribosome; or post-translationally, where synthesis is completed before the polypeptide engages the pore. Recent advances have begun to form a coherent picture of the means by which proteins cross a lipid bilayer. In this review we examine progress towards defining the mechanism of protein translocation into the ER, with particular emphasis on the involvement of HSP70 proteins and their DnaJ-retated partners in translocation in Saccharomyces cerevisiae.
The pathway of assembly of the progesterone receptor
Authors: Smith D F 
Published: November 2023

Abstract
The PR assembly pathway minimally involves the following chaperone components: Hsp90, Hsc70, Hip, Hop (p60), p23, FKBP52, FKBP51, and Cyp40 (Smith etal., 1995 and references therein; also see the individual entries in this volume for these and other chaperones mentioned in this review). There is also genetic evidence from steroid receptor expression in yeast cells that Ydj1, a cytosolic DnaJ homolog, is required for proper function of steroid receptors (Caplan et al., 1995; Kimura et al., 1995).
Mammalian Prp73
Authors: Dice J F 
Published: November 2023

Abstract
Prp73 was identified as a cytosolic protein able to bind specifically to RNase S-peptide (residues 1-20 of RNase A), a known substrate for a selective pathway of lysosomal proteolysis (Chiang et al., 1989; Dice, 1990). Prp73 binds to RNase S-peptide-Sepharose with a Kd of approximately 5 /iM (Terlecky et al., 1992), was able to stimulate uptake, degradation of RNase S-peptide, RNase A by lysosomes (Chiang et al., 1989; Terlecky et al., 1992).
Mammalian Pbp74
Authors: Pierce S K , Dahlseid J 
Published: November 2023

Abstract
Grp75 (Mizzen et al., 1989); P71 (Leustek et al., 1989); C3H strain-specific antigen (CSA) (Michikawa etal., 1993); mortalin (Wadhwa et al., 1993a); mtHsp70 (Webster etal., 1994); mthsp75 (Bhattacharyya etal., 1995).
STCH
Authors: Kaye FJ , Otterson G A , Flynn G C 
Published: November 2023

Abstract
Stch was isolated from a human cDNA library derived from the K562 erythroleukemia cell line, its sequence (GenBank/EMBL accession number U04735) predicts a peptide of 471 amino acids (Otterson et al., 1994). The STCH product contains a unique hydrophobic leader sequence, shares homology within the N-terminal domains of the HSP70 gene family (33% identity, 43% homology to both human Hsp70, BiP ATPase domains).
Mammalian Hsp110
Authors: Easton D P , Subjeck J R 
Published: November 2023

Abstract
Although the Hsp110 designation is now highly prevalent, the protein has also been referred to as Hsp107 (Landry et al., 1982), Hsp112 (Tomasovic et al., 1983), Hsp105 (Hatayama etal., 1994).
Escherichia coli CbpA
Authors: Mizuno T , Ueguchi C 
Published: November 2023

Abstract
CbpA was first identified, purified as an E. coli DNA- binding protein that could preferentially bind to a synthetic curved DNA sequence by means of a DNA-binding gel shift assay in the presence of an excess amount of a non-curved competitor sequence (Ueguchi et al., 1994). The curved DNA sequence, used as the probe, contains (dA)5 stretches which were designed so as to be phased at 10 bp intervals in the DNA helix (c. 200 bp).
Saccharomyces cerevisiae Ydjl
Authors: Cyr D M , Caplan AJ 
Published: November 2023

Abstract
Ydj1 was identified independently by two laboratories. Caplan, Douglas (1991) identified Ydj1 as a component of a protein extract generated from the nuclear matrix of Saccharomyces cerevisiae. Atencio, Yaffe (1992) identified a protein identical to Ydj1, Mas5p, in a search for proteins that facilitate the transport of proteins into mitochondria.
Saccharomyces cerevisiae Sec63p
Authors: Brodsky J L 
Published: November 2023

Abstract
The SEC63 gene was isolated initially in genetic selections for temperature-sensitive mutants in yeast that accumulate an untranslocated hybrid protein when shifted to the non-permissive temperature (Toyn et al., 1988; Rothblatt et al., 1989). The gene was also obtained in a selection for temperature-sensitive mutants that mislocalize a nuclear-targeted fusion protein at the non-permissive temperature (Sadler et al., 1989; Bossie et al., 1992). Disruption of SEC63 indicates that the gene product is essential for spore germination (Sadler etal., 1989).
Drosophila melanogaster Tid56
Authors: Kurzik-Dumke U , Debes A , Gundacker D 
Published: November 2023

Abstract
The starting material for the identification of the Drosophila melangaster tumour suppressor gene lethal(2) tumorous imaginal discs [l(2)tid] was a mutant, l(2)tid1, generated via EMS mutagenesis, characterized by neoplastic growth of imaginal discs (Kurzik-Dumke etal., 1992) . The l(2)tid gene was mapped genetically to the position 104 ± 1 cM on the right arm of the second chromosome (Kurzik-Dumke et al., 1992). The cytogenetic locus was further determined by deletion mapping, an extensive chromosome walk encompassing the bands 59D-60A (Kurzik-Dumke et al.,
Auxillin
Authors: Eisenberg A , Greene L E 
Published: November 2023

Abstract
Auxilin was first isolated from bovine brain clathrin- coated vesicles by Ahle, Ungewickell (1990). It was purified from a Tris extract of clathrin-coated vesicles by first separating the assembly protein fraction from clathrin by gel chromatography, then purifying the auxilin by hydroxyapatite chromatography followed by Superose 6 gel chromatography. Clathrin-coated vesicles, formed during receptor-mediated endocytosis, are composed primarily of clathrin, assembly proteins (or adaptins). The latter proteins promote the assembly of clathrin into clathrin coats. Auxilin was originally identified as a minor assembly protein (Ahle, Ungewickell, 1990; Lindner, Ungewickell, 1992), but more recently it has been identified as a cofactor necessary for the Hsc70-dependent dissociation of clathrin from clathrin cages (Ungewickell etal., 1995).
Mammalian Mtj
Authors: Lassie M W , Zetter B R , Brightman S E , Blatch G L 
Published: November 2023

Abstract
The cDNA encoding Mtj1 was isolated from an M27 Lewis lung carcinoma expression library (Brightman et al., 1995). Antibodies used for the screen were prepared against 50-60 kDa proteins that were retained on a hydrophobic peptide affinity column (YVGVAPG).
Saccharomyces cerevisiae Mge1
Authors: Laloraya S , Craig E A 
Published: November 2023

Abstract
Yge1 (yeast GrpE, Ikeda et al., 1994; Nakai et al., 1994), GrpEp (Bolliger etal., 1994), mitochondrial GrpE (mt-GrpE).
MGE1 was found in the GenBank database based on its similarity to E. coli grpE (Bolliger et al., 1994; Laloraya et al., 1994). It was also found as a gene (YGE1) that, when present in multiple copies, conferred resistance to staurosporine, a protein kinase C inhibitor (Ikeda etal., 1994).
Mammalian mitochondrial GrpE
Authors: Naylor D J , Hoogenraad N J , Hoj P B 
Published: November 2023

Abstract
The amino acid sequence deduced from the cDNA sequence of rat liver mt-GrpE (GenBank accession number U62940; Naylor et al. 1996) reveals a precursor protein of 217 amino acids (c. 24.3 kDa) with a 27 residue N-terminal targeting sequence, which upon mitochondrial protein import is proteolytically removed to generate the mature protein of 190 amino acids (c. 21.3 kDa). The nucleotide sequences of two partial cDNA clones from human white blood cells (TIGR EST#121800), normal foreskin melanocyctes (Genbank accession number N28384), together encode a precursor protein of 217 amino acids. A partial mouse cDNA clone (GenBank accession number W08216) has also been isolated.
Mammalian Hsp90
Authors: Jakob U , Buchner J 
Published: November 2023

Abstract
The alternative names of members of the Hsp90 family correspond to their apparent molecular weight on SDS-PAGE, depend on the context in which they have been identified: Hsp84/Hsp86 (mouse; Moore et al., 1989), Hsp85 (L929-cells; Lanks, 1989), Hsp89/Hsp90 (HeLa cells; Welch, Feramisco, 1982).
Saccharomyces cerevisiae Hsp10
Authors: Hohfeld J 
Published: November 2023

Abstract
Chaperonin 10, cpn10 (Rospert et al., 1993a). Since this entry focuses on mitochondrial cpn10 which cooperates with Hsp60 in the matrix compartment, the term Hsp10 will be used throughout the text. The nuclear HSP10 gene of S. cerevisiae (GenBank accession number X75754) encodes a polypeptide of 106 amino acids with a deduced molecular mass of 11 374 Da (Rospert et al., 1993a; Hohfeld, Hartl, 1994). Hsp10 displays a native mass of about 80 kDa reflecting the assembly of seven subunits to a homo-oligomeric ring structure characteristic of GroES, its homologues (Mande et al., 1996; Hunt etal., 1996).
Mammalian Cpn10
Authors: Viitanen P V 
Published: November 2023

Abstract
Mammalian mt-cpn1O (Lubben et al., 1990); heat shock protein 10 (HSP10), (Hartman et al., 1992); early pregnancy factor (EPF) (Cavanagh, Morton, 1994). The nucleotide sequences of mammalian CPN10 cDNAs cloned from rat (Ryan et al., 1994), cow (Pilkington, Walker, 1993), mouse (Dickson et al., 1994), human (Monzini et al., 1994) (GenBank accession numbers X71429, X69556, U09659, X75821, respectively) predict proteins of 102 amino acid residues (calculated molecular mass of c.10.8 kDa).
CCTδ
Authors: Kubota H , Willison K 
Published: November 2023

Abstract
The yeast homologue of CCT3 is also called Anc2p (Vinh, Drubin, 1994) or Cct4p (Kubota etal., 1995a).
A temperature-sensitive mutant called anc2-1 shows abnormal actin organization in budding yeast, a null allele of the gene is a recessive lethal (Vinh, Drubin, 1994).
CCTζ
Authors: Kubota H , Willison K 
Published: November 2023

Abstract
The human homologue of CCT£ is also called TCP20 (Li et al., 1994). The yeast homologue of CCT£ is also called Tcp20p (Li etal., 1994) or Cct6p (Kubota etal., 1995a). A null allele of the yeast homologue of Cctlj gene is a recessive lethal (Li etal., 1994).