Different conformations of nascent polypeptides during translocation across the ER membrane - Test2 - elhamkhani - TriplyDB

Different conformations of nascent polypeptides during translocation across the ER membrane

Different conformations of nascent polypeptides during translocation across the ER membrane

http://www.wikidata.org/entity/Q24795321

about

The Brichos domain of prosurfactant protein C can hold and fold a transmembrane segment X-ray structure of a protein-conducting channel High-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C.The Brichos domain-containing C-terminal part of pro-surfactant protein C binds to an unfolded poly-val transmembrane segment Multi-omic data integration enables discovery of hidden biological regularities.Control of translocation through the Sec61 translocon by nascent polypeptide structure within the ribosome.A folding zone in the ribosomal exit tunnel for Kv1.3 helix formation.Positive charges of translocating polypeptide chain retrieve an upstream marginal hydrophobic segment from the endoplasmic reticulum lumen to the translocon.Cotranslational Protein Folding inside the Ribosome Exit Tunnel.Ribosome exit tunnel can entropically stabilize alpha-helices.Free energy of nascent-chain folding in the translocon.Stepwise insertion and inversion of a type II signal anchor sequence in the ribosome-Sec61 translocon complex.Polytopic membrane protein folding at L17 in the ribosome tunnel initiates cyclical changes at the translocon Alteration of CFTR transmembrane span integration by disease-causing mutations.Glycosylation of prion strains in transmissible spongiform encephalopathies.A little help from my friends: quality control of presecretory proteins in bacteria Versatility of the endoplasmic reticulum protein folding factory.Formation of transmembrane helices in vivo--is hydrophobicity all that matters?Electrostatics in the ribosomal tunnel modulate chain elongation rates.Tertiary interactions within the ribosomal exit tunnel.Transmembrane segments form tertiary hairpins in the folding vestibule of the ribosome.Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.Membrane protein integration into the endoplasmic reticulum.BRICHOS domain associated with lung fibrosis, dementia and cancer--a chaperone that prevents amyloid fibril formation?Viroporins, Examples of the Two-Stage Membrane Protein Folding Model.NMR Investigation of Structures of G-protein Coupled Receptor Folding Intermediates.The α-helical structure of prodomains promotes translocation of intrinsically disordered neuropeptide hormones into the endoplasmic reticulum.Structural features within the nascent chain regulate alternative targeting of secretory proteins to mitochondria.alpha-Helical domains promote translocation of intrinsically disordered polypeptides into the endoplasmic reticulum Folding and Intramembraneous BRICHOS Binding of the Prosurfactant Protein C Transmembrane Segment Polypeptide binding specificities of Saccharomyces cerevisiae oligosaccharyltransferase accessory proteins Ost3p and Ost6p.Early encounters of a nascent membrane protein: specificity and timing of contacts inside and outside the ribosome.The anthrax toxin channel: a barrel of LFs.Protein folding taking shape. Workshop on molecular chaperones.A biphasic pulling force acts on transmembrane helices during translocon-mediated membrane integration.Protein unfolding is not a prerequisite for endoplasmic reticulum-to-cytosol dislocation.Folding zones inside the ribosomal exit tunnel.The Sec61/SecY complex is inherently deficient in translocating intrinsically disordered proteins.

P2860

Q24643585-B0C49DE6-AC50-4F58-B1DE-92534C69B27A Q27642744-BA9980C5-A0B0-483C-AA13-61BE64D00831 Q27677103-07A87147-8A71-4880-B8D9-D009723A158A Q28241042-141918AB-D250-4118-AF47-334A66216531 Q31139124-E3445AA3-6C5D-4C62-ADB1-39D3036082B9 Q33334739-3AE895EF-6804-4F50-9A34-BEF751F44199 Q33831957-F57116F2-692A-4729-96DA-12C678025A73 Q33907071-94F20F66-6978-4525-BA63-659C65EEA894 Q34044778-C2A47676-B17F-4C1E-B90D-91F4B9E5964B Q34245046-1B00C3CB-5682-47DD-A111-B048047BA01C Q34999575-FB435338-493B-4586-B518-C813B6357FA7 Q35235093-0F6D2284-5648-481C-BEC4-097280A80339 Q35276847-B1510450-F38A-4472-9600-AE048904625E Q35579788-3523B51C-06CA-4434-B48F-2F1D6713F7B0 Q35794935-02A2476B-BB59-4B46-A252-9C1F8A6636D3 Q35933897-95E6C301-B062-4377-8287-871DACA65F89 Q36242585-472E32D9-2C8B-4A99-BFBA-7EA35934A191 Q36793407-94251087-3906-4B34-9085-A849F77CADB2 Q37127214-307A44A8-E4EC-463B-9BC3-AA52FFDB5A36 Q37161999-F5CBAAC7-12D1-43D9-960A-D53300761FB7 Q37412726-2A156871-ECC3-4FE2-8226-1596BEB34000 Q37627987-7DEC5252-0493-4EF4-8E43-392C304CBAA8 Q37876968-6EEBDBB9-C3C2-4681-8C3A-457DE8511F4A Q37888775-91B22BA7-D9FE-49C3-82D9-55D1C8096C81 Q38541409-66871A06-3107-49DF-AD65-D5780F8E66EB Q39173136-A3C38D76-4528-4EE1-A260-F40A956A9C6A Q39175147-EA44A488-49F5-4920-9A34-9299E7872F8A Q39582237-EF11B22A-B751-44BB-95DB-8B18B2E20D3A Q39832083-C5D09A7D-EE01-4593-989D-2F567CF598B4 Q41153895-688886AF-1EAF-4858-9B54-53AE685E85C1 Q42069308-41C7A755-546B-4844-97A7-E64AF221E566 Q42250702-BE3B5FDE-4603-4A6E-B31F-BEF43327E6F7 Q42707642-026862AA-951F-45AF-9845-865C26DC3F77 Q42724601-701A9D27-123A-4867-9544-4C09AD01DBD5 Q42944586-5B3F7E66-5831-40BD-BD16-1D9134F585C3 Q44249690-B070AC34-2451-488A-9941-DFE9CE9402DA Q46813554-28E25F25-5F38-4AC4-87F3-8B6B78832227 Q47586836-3C3C4598-27FA-4ACF-933B-9B42C3D80CB5

P2860

Different conformations of nascent polypeptides during translocation across the ER membrane

http://www.wikidata.org/entity/Q24795321

description

2000 nî lūn-bûn

@nan

2000 թուականին հրատարակուած գիտական յօդուած

@hyw

2000 թվականին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

Different conformations of nas ...... ocation across the ER membrane

@ast

Different conformations of nas ...... ocation across the ER membrane

@en

Different conformations of nas ...... ocation across the ER membrane

@nl

type

label

Different conformations of nas ...... ocation across the ER membrane

@ast

Different conformations of nas ...... ocation across the ER membrane

@en

Different conformations of nas ...... ocation across the ER membrane

@nl

prefLabel

Different conformations of nas ...... ocation across the ER membrane

@ast

Different conformations of nas ...... ocation across the ER membrane

@en

Different conformations of nas ...... ocation across the ER membrane

@nl

P1433

Q24795321-14F6FDA2-F3E4-446D-8FA7-E336AACB40AE

P1476

Q24795321-08FFE65C-31CA-467D-8926-6875F19467E2

P2093

Q24795321-533CD306-D186-4806-A8BC-48F63C223A20

Q24795321-6E36ED28-BD7A-422A-998C-902DB9CB3C34

P2860

Q24795321-076B6282-37DF-45D5-9A08-ED57E84E7C26

Q24795321-1A4CBD42-D314-4AA4-99DF-EAC00FD5F3D2

Q24795321-2259F225-F508-414C-B316-6CDCBBCCD449

Q24795321-319DE81A-A0AA-402C-B0B7-BCAC520291CD

Q24795321-4FE3C9FE-B30E-427C-AABC-3A63FF4A3AF3

Q24795321-672FCBC7-632D-486C-8720-97440C599A71

Q24795321-77F609DE-F2CC-467B-BAA4-E9241C7AAF1D

Q24795321-9BC8110B-7B4A-402A-A83C-0883749F77AC

Q24795321-A45C3380-97FC-490B-86AB-7FBE5E4982D6

Q24795321-AEAFE18D-8674-474D-854D-3F4C81DDBD1F

P2888

Q24795321-5BAC1FFB-687A-4162-BF89-D0DF422823DC

P304

Q24795321-C6C61D5B-BFBB-4D8A-8BEA-24278E3483C5

P31

Q24795321-08B397EF-D8F7-4C51-87F0-5F5794C44773

P3181

Q24795321-D694BB31-8F5D-437A-AE13-3085A13382C8

P356

Q24795321-0C0B30EA-B7B4-4E08-BF0C-9E0FAC602C97

P407

Q24795321-895B474C-6862-4A50-ADEF-FB8691BF9515

P433

Q24795321-B374FBFC-0E03-4AC5-B493-465C93F9E382

P478

Q24795321-837C3735-773F-4C76-8A93-EE140388F68F

P50

Q24795321-A7E3734E-DDCF-4A43-A193-FEE1A4EE6852

Q24795321-CF587884-A709-4428-AD90-873F3A3FC4A9

P577

Q24795321-CA13AF83-CFF2-443C-8D89-01D5E1D914D2

P5875

Q24795321-ACA2D740-1ADF-4881-8051-E61AC1D278C3

P6179

Q24795321-23682937-D7CA-4DAF-9AD8-41B74CC189B8

P698

Q24795321-0B25ED4E-4431-4817-8BA0-A2C300E0BFAF

P921

Q24795321-40BAB961-0D59-4647-B10D-A9F725F8F8D6

P932

Q24795321-FBD3A0BF-0ADD-41AA-9B83-CB983F414FF2

P3181

P356

P1433

BMC Cell Biology

P1476

Different conformations of nas ...... ocation across the ER membrane

@en

P2093

I Nilsson

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

P Whitley

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

P2860

Internally located cleavable signal sequences direct the formation of Semliki Forest virus membrane proteins from a polyprotein precursor

The structural basis of ribosome activity in peptide bond synthesis

A transmembrane helix dimer: structure and implications

Rapid and efficient site-specific mutagenesis without phenotypic selection

Initiation of translation in prokaryotes and eukaryotes

The translocon: a dynamic gateway at the ER membrane.

Recent advances in the understanding of membrane protein assembly and structure.

A survey of left-handed polyproline II helices

A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain.

Conformational preferences of amino acids in globular proteins.

P2888

P304

3

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

P31

scholarly article

P3181

2801528

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

P356

10.1186/1471-2121-1-3

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

P407

P433

1

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

P478

1

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

P50

Ismael Mingarro

Gunnar von Heijne

P577

2000-01-01T00:00:00Z

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

P5875

12152928

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

P6179

1029252800

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

P698

11178101

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

P921

P932

29064

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