Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis - Test2 - elhamkhani - TriplyDB

Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis

Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis

http://www.wikidata.org/entity/Q24537679

about

Zhangfei is a potent and specific inhibitor of the host cell factor-binding transcription factor Luman Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element A novel protein, Luman/CREB3 recruitment factor, inhibits Luman activation of the unfolded protein response A novel isoform of human LZIP negatively regulates the transactivation of the glucocorticoid receptor BBF2H7, a novel transmembrane bZIP transcription factor, is a new type of endoplasmic reticulum stress transducer CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P.The liver-enriched transcription factor CREB-H is a growth suppressor protein underexpressed in hepatocellular carcinoma Genetic interactions due to constitutive and inducible gene regulation mediated by the unfolded protein response in C. elegans.Endoplasmic reticulum stress and type 2 diabetes Advances and New Concepts in Alcohol-Induced Organelle Stress, Unfolded Protein Responses and Organ Damage The proprotein convertases and their implication in sterol and/or lipid metabolism Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins PARM-1 is an endoplasmic reticulum molecule involved in endoplasmic reticulum stress-induced apoptosis in rat cardiac myocytes.Transcriptional profiling of chondrodysplasia growth plate cartilage reveals adaptive ER-stress networks that allow survival but disrupt hypertrophy DC-STAMP knock-down deregulates cytokine production and T-cell stimulatory capacity of LPS-matured dendritic cells.The neuronal host cell factor-binding protein Zhangfei inhibits herpes simplex virus replication.Sensing nerve injury at the axonal ER: activated Luman/CREB3 serves as a novel axonally synthesized retrograde regeneration signal.Site-specific proteolysis of the transcriptional coactivator HCF-1 can regulate its interaction with protein cofactors.Endoplasmic reticulum association and N-linked glycosylation of the human Nrf3 transcription factor.Human leucine zipper protein sLZIP induces migration and invasion of cervical cancer cells via expression of matrix metalloproteinase-9.Hypopigmentation and maternal-zygotic embryonic lethality caused by a hypomorphic mbtps1 mutation in mice Knockdown of CREB3/Luman by shRNA in Mouse Granulosa Cells Results in Decreased Estradiol and Progesterone Synthesis and Promotes Cell Proliferation.Crimean-Congo hemorrhagic fever virus glycoprotein processing by the endoprotease SKI-1/S1P is critical for virus infectivity An orchestrated program regulating secretory pathway genes and cargos by the transmembrane transcription factor CREB-H.Endoplasmic reticulum stress: signaling the unfolded protein response.Association of the cellular coactivator HCF-1 with the Golgi apparatus in sensory neurons.The endoplasmic reticulum and the unfolded protein response Regulation of the transcriptome by ER stress: non-canonical mechanisms and physiological consequences.Expression pattern implicates a potential role for luman recruitment factor in the process of implantation in uteri and development of preimplantation embryos in mice.Signalling pathways in the unfolded protein response: development from yeast to mammals.A CREB3-ARF4 signalling pathway mediates the response to Golgi stress and susceptibility to pathogens.Regulated intramembrane proteolysis: signaling pathways and biological functions.The signalling from endoplasmic reticulum-resident bZIP transcription factors involved in diverse cellular physiology.Current drug discovery strategies against arenavirus infections.The role of the unfolded protein response in diabetes mellitus.Roles of regulated intramembrane proteolysis in virus infection and antiviral immunity.DC-STAMP, the key fusion-mediating molecule in osteoclastogenesis.The essential biology of the endoplasmic reticulum stress response for structural and computational biologists.The neuroimmunology of degeneration and regeneration in the peripheral nervous system.JAB1/CSN5 inhibits the activity of Luman/CREB3 by promoting its degradation.

P2860

Q24294669-B02AFC9E-964C-4717-89B1-FCBD1BCEBBD0 Q24301000-8D600A1C-7E54-41AB-BC1D-3739F102DDDB Q24317491-9F56301D-9476-4834-A0AA-EEFF7C22B906 Q24318529-7075C83F-466D-4628-B3E6-B2437C0838F9 Q24337349-F83A87D5-1A43-403B-B46C-4AE384A5BEBD Q24338672-10809A7D-569C-4F81-BE3B-7DA0F5CA64BC Q24805822-8678DFBE-B3C8-4070-967C-90769ED8ED09 Q24815740-E2354AAF-2613-47D7-9DEF-BAA6E2A4F488 Q26864238-22BEE80B-E831-41C6-AE17-987E08DFA42B Q28082366-E4F39105-BEBA-48F4-9DFB-FDA4123629F1 Q28258161-7367CEA7-F56B-4B9C-AFD9-88EF89E44EA3 Q33262919-A139C101-3411-464A-9112-EC8601124687 Q33543763-BA5B8497-22AB-492E-8189-F3FC7730E53F Q34026175-96C4118C-B19A-47D9-9953-80B61B53EE1B Q34041998-56A1931D-3CEB-4BAA-9E8A-84F426A9EC61 Q34466767-2475DD39-B009-42EC-85C2-8E6AEE74F10F Q34526352-FC8DD646-AD49-481C-8871-ADE9A9900ED2 Q34547044-08988DE3-05E9-42AB-BE04-46D7EA91B113 Q34708452-3BD68B79-7971-4C23-8327-D75AD2EEBD40 Q35605069-CBC48CBC-5CF4-4AEA-BCDC-31E05778227F Q35914983-CF1EC026-3A65-4FF9-998B-89751DDEA48A Q36223723-542DE4E1-33FD-4DAC-90B2-5A1AF39E531D Q36315764-1DFCAD66-AC7D-4BD9-B872-2C7D63D8B7EB Q36673609-3D2FF475-E043-40DB-B5AB-C952BC56F98D Q36844431-76C39940-6E33-41CE-A650-4219FBC9FE31 Q36898912-230D3733-8319-4E59-A1FB-9276A66184CB Q37006310-D3D2B39D-9B3D-4D0C-8ADC-03C04D5E1EAB Q37352508-BE80A7B2-EBC2-4FD1-8F22-528AEA1BA678 Q37602123-95FA225C-37CB-4679-A40C-BFE47E40C815 Q37622607-BDDF16A5-50DB-4DA1-9659-CA0893AD69FD Q37663300-D73B2DF5-2D6A-4695-BD44-B2E2F38CBDA1 Q37847814-45991FFE-AD8C-4E2E-B079-0442997A23E2 Q37860033-BC79BD35-1335-4056-879D-84A442AAB374 Q38067504-D71FEF91-9926-4EF8-8AFB-5E9585E1B439 Q38093057-EFD9D442-9349-4CB4-8671-2F7A879DD367 Q38149888-3490808B-E732-4AC0-9BA9-08901FDAD1FF Q38178193-3EFB679F-1F97-4CF0-A009-50F8796EEC1E Q38201042-F4D6EE22-3F34-49AF-8321-73102D53B2CE Q38253020-9D875EF2-A88A-4917-87B9-B4F2EAAB6591 Q38316360-30C82A0E-9FAC-4660-ADF1-6FA108FF5E33

P2860

Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis

http://www.wikidata.org/entity/Q24537679

description

2002 nî lūn-bûn

@nan

2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Luman, the cellular counterpar ...... ated intramembrane proteolysis

@ast

Luman, the cellular counterpar ...... ated intramembrane proteolysis

@en

Luman, the cellular counterpar ...... ated intramembrane proteolysis

@nl

type

label

Luman, the cellular counterpar ...... ated intramembrane proteolysis

@ast

Luman, the cellular counterpar ...... ated intramembrane proteolysis

@en

Luman, the cellular counterpar ...... ated intramembrane proteolysis

@nl

prefLabel

Luman, the cellular counterpar ...... ated intramembrane proteolysis

@ast

Luman, the cellular counterpar ...... ated intramembrane proteolysis

@en

Luman, the cellular counterpar ...... ated intramembrane proteolysis

@nl

P1433

Q24537679-1327A9FE-CA29-4558-A7B8-E94909C54D08

P1476

Q24537679-ED47E882-7F37-444A-839A-F048A58D17F0

P2093

Q24537679-45A02981-ECD5-4370-A9AC-F2B1040DD7E5

Q24537679-498EBB96-827E-4159-A003-4E020845E821

Q24537679-97AA65B5-B84D-4685-89BD-0ADF59C9EABC

Q24537679-A2D3E7D8-AE63-4E13-8437-1A8E373D6743

Q24537679-B28FD213-A782-49C7-AABA-E15C73ED60F7

Q24537679-D071513A-2F7A-43DE-9B5C-8AD3BB935EED

P2860

Q24537679-01ED2F41-D990-4E8B-A9BE-6F68B4BCF709

Q24537679-08CADF9F-B5C2-4024-894A-13EF9D008EFB

Q24537679-0E24FE19-DE16-4738-A458-077E3388F576

Q24537679-0FE396DC-2708-4B5D-8774-B1EE4B65E7F5

Q24537679-1A54BAC7-7DFC-4B05-A510-D8740859630A

Q24537679-1CE023A9-FC1F-4E30-BFC9-1340D51C2D19

Q24537679-21E07B13-69E0-4F42-8BCC-9705D4C62B4A

Q24537679-262232CB-270C-40B9-8C04-E6EFDFF040CA

Q24537679-2794D365-8BC5-4F18-A7B0-60A9114F2E0F

Q24537679-2FB568FA-82BB-42C1-87EC-D512621C5143

P304

Q24537679-B4B8472B-5EC9-4B26-A1D9-EDD0DCFF3726

P31

Q24537679-BB22CBCA-1B53-4092-8DFB-6FAA91184819

P356

Q24537679-CC1FB7B2-516A-44BD-81AF-875CA9A66CE9

P407

Q24537679-BA9B5E39-4333-4477-A1D8-AE1293A85317

P433

Q24537679-DD176CA9-D25D-4035-8719-BA7D99B83F90

P478

Q24537679-F11F22DB-D0A6-4B63-BE79-845856C69219

P50

Q24537679-727C4832-1F11-49E1-B247-A080011830D1

P577

Q24537679-AC61D975-95D8-4AF6-9EEA-CF932D2E409D

P698

Q24537679-3F0DCACE-783A-490C-9430-B2BB3DD8A18F

P921

Q24537679-55E19D4C-ADDA-4688-AD8F-4C647528A337

Q24537679-9E383E78-C6F2-4EBA-A0D4-0DDCC09F87C3

P932

Q24537679-56511EF9-48D3-43E2-9FF6-E0502624DEDC

P356

MCB.22.16.5639-5649.2002

P1433

Molecular and Cellular Biology

P1476

Luman, the cellular counterpar ...... ated intramembrane proteolysis

@en

P2093

Camilo Raggo

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

Erin Smith-Windsor

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

Julie Stirling

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

Noreen Rapin

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

Peter O'Hare

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

Philipe Gobeil

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

P2860

Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells

Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors

Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress

Potential role for luman, the cellular homologue of herpes simplex virus VP16 (alpha gene trans-inducing factor), in herpesvirus latency

Hepatitis C virus core protein-induced loss of LZIP function correlates with cellular transformation

ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1

ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs

SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis

Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein

Interaction of ATF6 and serum response factor

P304

5639-5649

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

P31

scholarly article

P356

10.1128/MCB.22.16.5639-5649.2002

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

P407

P433

16

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

P478

22

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

P50

P577

2002-08-01T00:00:00Z

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

P698

12138176

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

P921

P932

133973

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