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1 synthesis of correctly processed proteins in Pichia.
2 in Xenopus oocytes and for overexpression in Pichia.
3 and could be overexpressed and purified from Pichia.
4 S. cerevisiae Cse4 and the noncomplementing Pichia angusta ortholog showed that species specificity
6 tact monomeric ATP synthase from the fungus, Pichia angusta, has been solved by electron cryo-microsc
10 and was applied to two model microorganisms, Pichia augusta and Escherichia coli, cultivated on (13)C
11 rsion to prokaryote (E. coli)- or eukaryote (Pichia)-based codon usage dramatically improved the leve
13 ric Sup35p, containing the Sup35NM region of Pichia, can be turned into a prion in S. cerevisiae by o
15 ased on P. falciparum, Escherichia coli, and Pichia codon usage and expressed recombinant F2 in E. co
18 d refolded from E. coli or produced from the Pichia expression system, is equivalent and mimics the f
22 cing the 5.8S internal transcribed spacer as Pichia fermentans, Wickerhamomyces anomalus and Candida
24 between another five more divergent species, Pichia guilliermondii, C. glabrata, C. zeylanoides, C. h
25 tes (Saccharomyces cerevisiae - KF551990 and Pichia gummiguttae - MCC 1273) and influence of jamun se
28 da parapsilosis, Torulaspora delbrueckii and Pichia kluyveri showed greater changes in the reducing s
30 fluence of Saccharomyces cerevisiae (Sc) and Pichia kudriavzevii (Pk) during on-farm fermentation on
31 light subunit LAT2 in detergent-solubilized Pichia membranes, allowing functional reconstitution of
36 ed as a non-covalent dimer from secretion in Pichia pastoris (115 mg/l) and was a potent inhibitor of
37 hains was tested with human LAL expressed in Pichia pastoris (phLAL) and CHO cells (chLAL), respectiv
38 ng mannose terminated human LAL expressed in Pichia pastoris (phLAL), purified, and administered by t
44 roteins from Escherichia coli (bacteria) and Pichia pastoris (yeast) immobilized in a microfluidic ch
49 bacter globiformis amine oxidase (AGAO), and Pichia pastoris amine oxidase (PPLO) have been examined.
50 gC2 and gD2 were produced in glycoengineered Pichia pastoris and administered intramuscularly as a bi
53 In this report, we described two systems (Pichia pastoris and baculovirus/Sf9 cells) for expressio
54 eport that MS is localized to the nucleus of Pichia pastoris and Candida albicans but is cytoplasmic
56 d N- and O-linked mannosylation in the yeast Pichia pastoris and compared them to their unglycosylate
59 1 and -DBL5 recombinant proteins produced in Pichia pastoris and developed a panel of seven chondroit
62 an in vitro cell-free ER-budding assay using Pichia pastoris and followed two endogenous PMPs, Pex11p
63 e redox enzyme was recombinantly produced in Pichia pastoris and homogeneously purified, and its gluc
64 d Rlm7, the AvrLm4-7 protein was produced in Pichia pastoris and its crystal structure was determined
66 tic properties of VKORC1L1 when expressed in Pichia pastoris and more particularly its susceptibility
67 and the former is additionally conserved in Pichia pastoris and Paracoccus denitrificans, suggesting
69 d Cys-less P-glycoproteins were expressed in Pichia pastoris and purified in high yield in detergent-
70 d this aquaporin in the methylotrophic yeast Pichia pastoris and purified the hexahistidine-tagged pr
71 ant human ABCG5 and ABCG8 genes in the yeast Pichia pastoris and purified the proteins to near homoge
73 .1) was produced in the methylotrophic yeast Pichia pastoris and purified to near-electrophoretic hom
76 rexpressed the human cytosolic ISCS in yeast Pichia pastoris and showed that the cytosolic form of IS
79 oduced in glycoengineered lines of the yeast Pichia pastoris and that antibody-mediated effector func
81 hesis, the candidate genes were expressed in Pichia pastoris and their activities measured with the b
84 S-7 cells and the methylotropic yeast strain Pichia pastoris and was shown capable of penetrating int
85 ing peptides were expressed recombinantly in Pichia pastoris and were tested for their ability to bin
87 Our results demonstrate the utility of using Pichia pastoris as an efficient eukaryotic host to expre
89 odium/D-glucose co-transporter 1 (hSGLT1) in Pichia pastoris as representative example of a useful st
90 DH mutants were recombinantly produced using Pichia pastoris as the host microorganism, and their IET
91 ry and expressed in the methylotrophic yeast Pichia pastoris at a secretion yield of approximately 10
92 lic forms of AMA1 that were both produced in Pichia pastoris at a sufficient economy of scale to be u
93 termined by autophagy receptors, such as the Pichia pastoris autophagy-related protein 30 (Atg30), wh
94 and pH 8.0 was purified from the engineered Pichia pastoris broth to homogeneity by anion exchange c
95 unaffected in most pex mutants of the yeast Pichia pastoris but is severely reduced in pex4 and pex2
96 lization pathway in the methylotrophic yeast Pichia pastoris by binding to Mxr1p response elements (M
97 romyces cerevisiae, the methylotrophic yeast Pichia pastoris can assimilate amino acids as the sole s
98 peroxisomal matrix, respectively, in living Pichia pastoris cells and followed by fluorescence micro
100 G/E56D/L72Y], was generated and expressed in Pichia pastoris cells in yields exceeding 100 mg/liter.
103 GT43-4, TaGT47-13, TaGT75-3, and TaGT75-4 in Pichia pastoris confirmed that these proteins form a com
107 thod is demonstrated on a flux experiment of Pichia pastoris employing two different tracers, i.e., 1
109 otein obtained by heterologous expression in Pichia pastoris exhibited greater XET activity against x
110 a streamlined workflow for the generation of Pichia pastoris expression strains, reducing the timelin
111 eine-rich domain of PyP140/RON4 by using the Pichia pastoris expression system and characterized the
112 alone or domain 9 alone were expressed in a Pichia pastoris expression system and tested for their a
113 erologous expression of this cDNA clone in a Pichia pastoris expression system led to the secretion i
115 To investigate this hypothesis, we used a Pichia pastoris expression system to produce large amoun
116 binant human MD-2 (rhMD-2) was produced in a Pichia pastoris expression system, and the interaction b
118 engineering of the DNA encoding VCP into the Pichia pastoris expression system, were used to localize
122 nt maize chitinase, rChiA, was purified from Pichia pastoris extracellular medium by differential pre
123 ernal standardization by fully (13)C labeled Pichia pastoris extracts enabled absolute quantification
126 CS proteins expressed in Escherichia coli or Pichia pastoris for their ability to induce immunity and
128 nt protein to be expressed in Yeast (such as Pichia pastoris GS115) and purified rapidly and easily w
130 lasminogen (amino acids 93-470) expressed in Pichia pastoris had physical properties (molecular size,
133 protein expressed in the methylotropic yeast Pichia pastoris indicate that it catalyzes the 4-epimeri
140 nd NOP-1 protein heterologously expressed in Pichia pastoris is labeled by using all-trans [3H]retina
143 (EPAO), Pisum sativum amine oxidase (PSAO), Pichia pastoris lysyl oxidase (PPLO), bovine plasma amin
145 uman pancreatic alpha-amylase, concanavalin, Pichia pastoris lysyl oxidase, and Klebsiella pneumoniae
148 ood yields cultivating the heterologous host Pichia pastoris on the 5L bioreactor scale (reUmChlE; 45
149 uffy binding-like (DBL) domains expressed in Pichia pastoris or var2csa plasmid DNA and sera were scr
150 the interaction between Pex19p and all known Pichia pastoris Pex proteins by the yeast two-hybrid ass
153 e report the cloning and characterization of Pichia pastoris PEX19 by complementation of a peroxisome
157 in of rat neural agrin (AgG3z8) expressed in Pichia pastoris promoted AChR clustering on surface of C
159 e effects of bile acids on ATP hydrolysis in Pichia pastoris purified ABCG5/G8 and found that they st
160 se mutation in a cysteine protease, G79E, in Pichia pastoris resulted in an unstable precursor protei
161 ologous expression of this gene in the yeast Pichia pastoris resulted in the production of a beta-1,4
162 P2, sLRP3, and sLRP4) have been expressed in Pichia pastoris SMD1168 with constitutive coexpression o
163 inant Tum-5 produced in Escherichia coli and Pichia Pastoris specifically inhibited proliferation and
164 ructosidase (BfrA) secreted by a recombinant Pichia pastoris strain was optimally immobilised on Glyo
165 oped a platform using genetically engineered Pichia pastoris strains designed to secrete multiple pro
167 mutant) were overproduced recombinantly in a Pichia pastoris system, they displayed the dual inhibito
168 in and expressed in the methylotrophic yeast Pichia pastoris to obtain a post-translationally modifie
169 ed and expressed in the methylotrophic yeast Pichia pastoris to probe for the proposed phosphatidylch
170 Here, we established an expression system in Pichia pastoris to recombinantly produce and purify Cx43
171 on of the glycosylation pathway in the yeast Pichia pastoris to secrete a human glycoprotein with uni
172 xpanded its utility by engineering the yeast Pichia pastoris to secrete human glycoproteins with full
174 into the genome of the methylotrophic yeast Pichia pastoris under the control of an AOX promoter and
175 s expressed as a secreted soluble protein in Pichia pastoris under the regulation of alcohol oxidase
176 s nivalis agglutinin; GNA) were expressed in Pichia pastoris using native signal peptides, or the Sac
177 s were observed against both rh-Endo and the Pichia pastoris vector, but no allergic reactions were o
180 e recombinant protein expressed in the yeast Pichia pastoris was found to have activity against the i
182 herapy, an Fv-p53 fusion protein produced in Pichia pastoris was tested on CT26.CL25 colon cancer cel
184 ress this, we expressed human CFH mutants in Pichia pastoris We found that recombinant I62-CFH (prote
186 ed in overexpressing PfCRT to high levels in Pichia pastoris yeast by synthesizing a codon-optimized
191 s of 27,653 Daltons, was expressed in yeast (Pichia pastoris) and purified by anion exchange column c
192 In Komagataella phaffii (formerly called Pichia pastoris) specifically, the indirect traffic of P
194 study of expression of the RK gene in yeast (Pichia pastoris), COS-1 cells and in an HEK293 stable ce
195 lus nidulans) and in a methylotrophic yeast (Pichia pastoris), the latter expression system producing
197 ; EC1.6.6.1) were cytosolically expressed in Pichia pastoris, a methylotrophic yeast, using spinach (
198 CPTI and CPTII were separately expressed in Pichia pastoris, a yeast with no endogenous CPT activity
199 es were expressed in Escherichia coli and in Pichia pastoris, and analyzed for monoclonal antibody an
200 n domain 11, expressed these mutant forms in Pichia pastoris, and determined binding kinetics with hu
201 ic human cysteine protease, was expressed in Pichia pastoris, and its physicokinetic properties were
204 he polypeptide was recombinantly produced in Pichia pastoris, and the three-dimensional structure was
205 genesis-defective (pex) mutants of the yeast Pichia pastoris, AOX fails to assemble into active octam
206 and a deglycosylated form, both expressed in Pichia pastoris, are investigated and compared as biocat
208 of a form of P. falciparum AMA1, produced in Pichia pastoris, by vaccinating Aotus vociferans monkeys
209 Purified recombinant PHACS, expressed in Pichia pastoris, contains bound pyridoxal-5'-phosphate (
211 we report that, when expressed in the yeast Pichia pastoris, full-length ataxin-3 enabled almost nor
212 coprotein (Pgp; mouse MDR3) was expressed in Pichia pastoris, grown in fermentor culture, and purifie
214 man bile salt-stimulated lipase expressed in Pichia pastoris, hen ovalbumin, bovine fetuin, bovine th
215 lypeptide ABC transporter TAPL, expressed in Pichia pastoris, into lipid vesicles (liposomes) and per
216 A. fumigatus Cu,Zn SOD has been expressed in Pichia pastoris, is enzymatically active, and has bioche
217 a water transporting aquaporin of the yeast Pichia pastoris, is suggested to be gated by chemo-mecha
218 (AOXI) promoter of the methylotrophic yeast, Pichia pastoris, is used widely for the production of re
219 ressed this gene heterologously in the yeast Pichia pastoris, obtaining a relatively high yield of 2.
220 alpha2beta1, alpha2beta2, and alpha2beta3 in Pichia pastoris, purified the complexes, and compared th
221 d recombinant PI8 in the methylotropic yeast Pichia pastoris, purified the inhibitor to homogeneity,
222 ssed different variants of MDR3 in the yeast Pichia pastoris, purified the proteins via tandem affini
223 n was expressed recombinantly in E. coli and Pichia pastoris, resulting in unglycosylated and mannosy
224 common with a glycosylated form expressed in Pichia pastoris, the [(15)N,(1)H]-correlation spectra of
227 AT2) heterodimers overexpressed in the yeast Pichia pastoris, together with docking analysis and cros
228 almitoyltransferase I (L-CPT I) expressed in Pichia pastoris, two contiguous discrete sequences withi
229 er liter levels in the methylotrophic yeast, Pichia pastoris, using the methanol oxidase promoter.
230 A binding domain [BoNT/A(Hc)], expressed in Pichia pastoris, was developed as a vaccine candidate fo
231 f human recombinant cathepsin F, produced in Pichia pastoris, was processed to its active mature form
232 ion assays of BdCSLF6 expressed in the yeast Pichia pastoris, we also demonstrate that the catalytic
233 e isolation of peroxisomal import mutants in Pichia pastoris, we have isolated a mutant (pex7) that i
234 e this idea, we examined two budding yeasts: Pichia pastoris, which has coherent Golgi stacks, and Sa
287 pecies were synthesized in the yeast species Pichia pastoris: K195M, K199M, F211V, W214L, R218M, R222
289 n three yeast species, Candida parapsilosis, Pichia philodendra and Candida salmanticensis, is charac
290 ations, the antibodies generated against the Pichia-produced protein prevented the binding of recombi
292 coccus, Filobasidium, Kloeckera, Malassezia, Pichia, Sporidiobolus, Rhodotorula, Zygosaccharomyces, a
295 tive sequence contains Ile at position 116 ( Pichia stipitis OYE 2.6) revealed that this enzyme's ste
298 n the heterologous system, overproduction of Pichia Sup35p or Sup35NM induced formation of the prion