Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiae. - Wikidata - awgldk - TriplyDB

Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiae.

Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiae.

http://www.wikidata.org/entity/Q38358778

about

Progress in metabolic engineering of Saccharomyces cerevisiae Engineering of promoter replacement cassettes for fine-tuning of gene expression in Saccharomyces cerevisiae.Parallel analysis of tetramerization domain mutants of the human p53 protein using PCR colonies.Imbalance of heterologous protein folding and disulfide bond formation rates yields runaway oxidative stress.Genome-scale modeling of the protein secretory machinery in yeast pH responsive granulocyte colony-stimulating factor variants with implications for treating Alzheimer's disease and other central nervous system disorders.Combined strategies for improving expression of Citrobacter amalonaticus phytase in Pichia pastoris.Alteration of chaperonin60 and pancreatic enzyme in pancreatic acinar cell under pathological condition.Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview.Production of heterologous proteins using the fission-yeast (Schizosaccharomyces pombe) expression system.Metabolic engineering of recombinant protein secretion by Saccharomyces cerevisiae.The effect of the unfolded protein response on the production of recombinant proteins in plants.Overexpression of BiP in tobacco alleviates endoplasmic reticulum stress.Calnexin overexpression increases manganese peroxidase production in Aspergillus niger.Different expression systems for production of recombinant proteins in Saccharomyces cerevisiae Parallel competition analysis of Saccharomyces cerevisiae strains differing by a single base using polymerase colonies.Modulation of Aspergillus awamori thaumatin secretion by modification of bipA gene expression.A Novel Potential Signal Peptide Sequence and Overexpression of ER-Resident Chaperones Enhance Heterologous Protein Secretion in Thermotolerant Methylotrophic Yeast Ogataea thermomethanolica.PDI improves secretion of redox-inactive beta-glucosidase.The molecular biology of secreted enzyme production by fungi.Decreased secretion and unfolded protein response up-regulation are correlated with intracellular retention for single-chain antibody variants produced in yeast.Cell viability and secretion of active proteins in Schizosaccharomyces pombe do not require the chaperone function of calnexin.A novel high-throughput screen reveals yeast genes that increase secretion of heterologous proteins Overexpression of an archaeal protein in yeast: secretion bottleneck at the ER.Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments.Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control.Directed evolution of a stable scaffold for T-cell receptor engineering.Comparison of Yeasts as Hosts for Recombinant Protein Production.

P2860

Q28757069-EAE30568-E22E-46DF-861C-85FBCAA35FEC Q33252664-C7D07B3D-144F-4BF3-9239-3D79C589B4CF Q33377080-392B427A-6986-44B0-ACAB-EF13546AABD8 Q34180434-442F61B8-CE5E-401D-82DA-750DEF16603C Q34718110-DB9073DD-E9AE-43C5-A667-0D34F66DF8AB Q35602819-E7A01C68-8280-4581-A09E-FA551477377D Q35789552-5B60205D-8CD7-4A43-8956-6DAC9F13F723 Q36491579-76C6A0DD-AF6D-4B14-BB32-52C114BE28DB Q36569895-FF3E36D6-C1D2-4655-9CE2-73C7925F8993 Q37521198-9D26A4DE-C98C-4550-9D1C-E1579C9E5B8D Q38005467-DFF4131D-C8A6-4F96-AACB-6B695E85EBBA Q38245992-40268540-E085-47AE-96FA-9DD69C6FFE19 Q38327294-DBDE8A8F-3892-4AB9-83CA-D0BD8B28C1AE Q39649798-9814EA1A-EE5E-418F-A456-7B463EE650CB Q39674543-4D2D49C9-5B4A-48D0-98F1-F4197F07C6AB Q39808927-EE606C9B-E5E8-4935-9421-2E4C618BBE7F Q40130451-3A907EA5-8B29-4192-B409-51E7B3155994 Q40372971-2BF986FF-E941-4248-9A60-BAC6851D190B Q41192015-FF1D3557-7594-4CEF-A9AA-7B06AD10AB62 Q41661096-91B871B0-9127-4E8E-9B70-12AAB0A25145 Q41839763-9E253DED-9450-4CCC-AB99-D2E8DA1F1B8D Q41965156-C1296773-5010-4229-B701-37D706A51B28 Q42111270-A4ED0C9B-D583-4FC7-80FB-518EAF1A2942 Q44124225-BBE089E8-4474-4E4B-BAB3-1F43072926DC Q47692442-2C84079B-5622-4284-B5DD-2590FE253C8D Q47792459-C9CAD824-8B49-43E0-AA37-D19EDF8B6A8C Q54045046-3BD9DB74-F731-440D-9A3A-55A4CB33CEB9 Q55717914-7620FCCB-21EC-4D4D-AE67-61DEE51306E4

P2860

Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiae.

http://www.wikidata.org/entity/Q38358778

description

1996 nî lūn-bûn

@nan

1996年の論文

@ja

1996年学术文章

@wuu

1996年学术文章

@zh-cn

1996年学术文章

@zh-hans

1996年学术文章

@zh-my

1996年学术文章

@zh-sg

1996年學術文章

@yue

1996年學術文章

@zh

1996年學術文章

@zh-hant

name

Reduction of BiP levels decrea ...... n in Saccharomyces cerevisiae.

@en

type

label

Reduction of BiP levels decrea ...... n in Saccharomyces cerevisiae.

@en

prefLabel

Reduction of BiP levels decrea ...... n in Saccharomyces cerevisiae.

@en

P1433

Q38358778-9BE58D2C-6B07-46C4-A52A-597850D0EB27

P1476

Q38358778-46B47C23-6610-4B9F-BC1B-8B635DEA2F57

P2093

Q38358778-BA51EDDC-DD42-4A79-AE9A-5C1718DB20FB

Q38358778-BB3DABA1-6706-4F6B-ABB8-253152BF00BD

Q38358778-E9351E1A-DBF2-40AE-BC36-627A91B129D8

P2860

Q38358778-01A89165-4159-4AE2-9D2F-CEDAF6E407F4

Q38358778-031F397C-A789-44DC-9D0B-6F6DE7880C8B

Q38358778-07521F1D-B0CA-4D78-9012-E0DE8904DF73

Q38358778-07F2B01E-1541-4760-B3FE-83F9EC3ED1B6

Q38358778-14C4B286-D30D-44B8-807C-CF70689B19B9

Q38358778-26B8F5B7-8A5D-41B2-9F88-B81BE9E09A65

Q38358778-2E7F8EB8-B6C5-460B-9D52-76F48F121537

Q38358778-3908BDE3-E45B-419A-9F4F-6F1F54BC88CE

Q38358778-46DDF08A-9E1A-4A86-ABAD-9F106331F574

Q38358778-513C1F8E-C1A8-45FC-BBDE-158600A2FD6C

P304

Q38358778-BA04D31D-8B65-47CB-A61D-CEFF0EEA7FD3

P31

Q38358778-B6F57641-9D06-4FB9-A0DE-6D53B9110A8F

P356

Q38358778-9A27DDAB-9A53-4E60-B042-C80409163428

P407

Q38358778-0D549115-8E55-4E92-A234-EDC27148EB17

P433

Q38358778-D630DD1C-D06F-46E7-84D5-6869C7BF612F

P478

Q38358778-6164650C-6201-4FEF-88EB-2786F51DB07A

P50

Q38358778-4CE55982-C316-4D77-B2DA-B85D3D9A1113

P577

Q38358778-A509EF67-9EB6-4D30-B8F7-EDE9C1BD9BFD

P5875

Q38358778-7A34A9B5-C868-4480-8902-7B8982D9426C

P698

Q38358778-63338BE1-DDF5-4EFC-8D97-2E0210A8D6E5

P921

Q38358778-9696DE44-AA0D-4512-B9E4-E4ED65811D8A

P356

JBC.271.17.10017

P1433

Journal of Biological Chemistry

P1476

Reduction of BiP levels decrea ...... on in Saccharomyces cerevisiae

@en

P2093

A C Voegler

http://www.w3.org/2001/XMLSchema#string

J A Bockhaus

http://www.w3.org/2001/XMLSchema#string

K D Wittrup

http://www.w3.org/2001/XMLSchema#string

P2860

The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins

Prevention of pre-PCR mis-priming and primer dimerization improves low-copy-number amplifications

Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport.

Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p.

KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene.

Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast

Immunoglobulin heavy chain binding protein

BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast

Protein folding in the cell

The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins

P304

10017-10022

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.271.17.10017

http://www.w3.org/2001/XMLSchema#string

P407

P433

17

http://www.w3.org/2001/XMLSchema#string

P478

271

http://www.w3.org/2001/XMLSchema#string

P50

Anne S Robinson

P577

1996-04-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

14573116

http://www.w3.org/2001/XMLSchema#string

P698

8626555

http://www.w3.org/2001/XMLSchema#string

P921

Saccharomyces cerevisiae