Dictyostelium macroautophagy mutants vary in the severity of their developmental defects. - Wikidata - wikimedia - TriplyDB

Dictyostelium macroautophagy mutants vary in the severity of their developmental defects.

Dictyostelium macroautophagy mutants vary in the severity of their developmental defects.

http://www.wikidata.org/entity/Q52094720

about

siRNA screening of the kinome identifies ULK1 as a multidomain modulator of autophagy Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery Dissection of Francisella-Host Cell Interactions in Dictyostelium discoideum.Control of cellular physiology by TM9 proteins in yeast and Dictyostelium.TipC and the chorea-acanthocytosis protein VPS13A regulate autophagy in Dictyostelium and human HeLa cells Autophagy in mammalian development and differentiation mTOR regulation of autophagy Autophagy in cell death: an innocent convict?Accelerated cell death in Podospora autophagy mutants Vacuole membrane protein 1 is an endoplasmic reticulum protein required for organelle biogenesis, protein secretion, and development Role of ATG8 and autophagy in programmed nuclear degradation in Tetrahymena thermophila The induction of autophagy by mechanical stress.Dictyostelium discoideum as a Novel Host System to Study the Interaction between Phagocytes and Yeasts Mycobacterium marinum antagonistically induces an autophagic response while repressing the autophagic flux in a TORC1- and ESX-1-dependent manner.Autophagy in unicellular eukaryotes An overview of the molecular mechanism of autophagy.Unconventional secretion of AcbA in Dictyostelium discoideum through a vesicular intermediate RpkA, a highly conserved GPCR with a lipid kinase domain, has a role in phagocytosis and anti-bacterial defense.Heteromeric p97/p97R155C complexes induce dominant negative changes in wild-type and autophagy 9-deficient Dictyostelium strains Autophagy and cell death in model organisms.Intertwined pathways of programmed cell death in immunity.The autophagic machinery ensures nonlytic transmission of mycobacteria.Autophagy as a therapeutic target in cancer.Genetic control of morphogenesis in Dictyostelium.Autophagy inhibitors as a potential antiamoebic treatment for Acanthamoeba keratitis.Global transcriptional responses to cisplatin in Dictyostelium discoideum identify potential drug targets Autophagy in metazoans: cell survival in the land of plenty.Lack of Ecological and Life History Context Can Create the Illusion of Social Interactions in Dictyostelium discoideum Molecular mechanisms and regulation of specific and nonspecific autophagy pathways in yeast.The inositol 1,4,5-trisphosphate receptor is required to signal autophagic cell death.JNK protects Drosophila from oxidative stress by trancriptionally activating autophagy A beta-tubulin mutation selectively uncouples nuclear division and cytokinesis in Tetrahymena thermophila Autophagy in protists.Autophagy and heart failure: a possible role for homocysteine.The crosstalk between autophagy and apoptosis: where does this lead?Function of the Dictyostelium discoideum Atg1 kinase during autophagy and development.Autophagy in Dictyostelium: Mechanisms, regulation and disease in a simple biomedical model.Methods to Monitor and Quantify Autophagy in the Social Amoeba Dictyostelium discoideum.

P2860

Q24314616-104D2C52-B065-4E81-A4B8-5B22266C0EFD Q24329236-4DC5A5FF-3EF6-4AA1-A8E6-9E715AD21CD0 Q24648105-488A1BF1-DBA6-4F5A-8E39-F595596815A1 Q24649645-C8D615D1-B17E-40D3-ADEC-C6C63E13F31B Q27323186-0A44E8C8-2BF0-406B-B153-3F7944CE060F Q27930803-78738DE4-BD1E-42C9-A227-4EABCED98F05 Q28118371-EDD37652-5445-49A3-8519-5A8D04C97FEB Q29615612-B370A752-71EC-422D-9FF9-7DC3E6FBB088 Q29616301-4D878AB7-8A2C-4FBA-AA1A-41D49844A4A2 Q29617604-1C42D1C6-54E6-4989-A059-DA9C34889BB6 Q30476381-7A04CEFF-56EB-4B70-9AC6-C3F63A1B28D5 Q30482868-A06E115D-A7E5-4A7A-89BB-B6DA16F4FF79 Q30512687-4579F818-E2FE-4681-91B7-BB6E0DD44502 Q30513403-C2E1563B-C24A-497A-AC24-8236A90882CA Q30825041-B87AEAC2-2183-4321-8F2B-F7B40954DBEF Q33611027-94D6BDA5-4422-45F3-8119-18CC17BEBAFE Q33632857-CC884737-EA82-4088-819C-5B73E9EF520D Q33703918-49A77041-BE2A-453F-802E-58BFDD1167A7 Q33983193-08948DFC-2BA3-45F3-A1FA-32ACC9AB118F Q34071924-54B864CC-8BB0-4BD0-BB71-B8F8EB733CCC Q34442393-CADC1DE4-E2B6-42FC-95E6-F95475AE5B89 Q34903178-88FA74E4-4291-4BBB-87B4-24DD7D3D6A62 Q35108580-30855804-93BD-4FDB-BFB0-6B8F30F4EBAD Q35128752-BDEEF199-C77E-4508-837A-C2BA01D05ACA Q35591562-B13BCA4B-7861-495E-B58A-475BD8FD1506 Q35731156-6569F676-C3D6-4553-AE45-2B3F1BBF520F Q35746102-1048A036-261D-466B-A8E9-E2E6138B6EE5 Q36024142-19037C47-56B8-43F1-8FF1-3744FD0870DB Q36146937-AF086659-57AE-4006-B299-36033D33B291 Q36224656-88487EF5-1AD5-4225-A927-3DACAF02F59E Q36288705-6E47AC45-6714-4F75-92D6-9DB7B44896E8 Q36438753-30E31A5A-0932-431B-B904-C2D12D429389 Q37361342-137DB3C2-1424-4DD6-A5E3-8B794684F292 Q37579825-74C18FF0-EBF2-496D-984C-A3EFDE800F19 Q37801802-5CD093E3-746D-4388-A99E-F8AA16B228E2 Q37930526-B3930C3C-C303-4F1C-BE94-D6FC0EDB0DA9 Q37982296-A9A8222F-D98F-472D-8AF2-178C0EAB0FFD Q38499872-65B0B3F1-DF52-40D4-B726-4C87E2C06265 Q38813809-C8ABB170-D16C-4AA4-933A-874868270EC7 Q39411013-27A43AA5-4C1C-410E-8E87-22792A7AABD9

P2860

Dictyostelium macroautophagy mutants vary in the severity of their developmental defects.

http://www.wikidata.org/entity/Q52094720

description

2004 nî lūn-bûn

@nan

2004年の論文

@ja

2004年学术文章

@wuu

2004年学术文章

@zh

2004年学术文章

@zh-cn

2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

2004年學術文章

@zh-hant

name

Dictyostelium macroautophagy mutants vary in the severity of their developmental defects.

@en

Dictyostelium macroautophagy mutants vary in the severity of their developmental defects.

@nl

type

label

Dictyostelium macroautophagy mutants vary in the severity of their developmental defects.

@en

Dictyostelium macroautophagy mutants vary in the severity of their developmental defects.

@nl

prefLabel

Dictyostelium macroautophagy mutants vary in the severity of their developmental defects.

@en

Dictyostelium macroautophagy mutants vary in the severity of their developmental defects.

@nl

P1433

Q52094720-1EEB567D-0D83-43CB-A061-F51F1F490BFE

P1476

Q52094720-12B21345-38BC-4588-A054-CDE531CB0629

P2093

Q52094720-014177B8-9D1E-47D8-BFFB-06462AF6B7BF

Q52094720-17E788A9-14ED-41E4-BB44-F6FEB70164DF

Q52094720-B80DDCD8-7B23-4D42-AEA6-82DD9977937B

Q52094720-D27C8387-AB66-4F83-9F2B-B4426FCD9ED5

Q52094720-D5841854-CAAA-4127-8EA3-CFDB006E832C

P2860

Q52094720-014D8AF4-02A7-407C-8E24-81992A0CA584

Q52094720-018E14E9-975C-41C2-9FA1-69D3090DFDA5

Q52094720-01D01F89-01F6-4668-AB8B-057483EF07AE

Q52094720-083A3D8E-9614-45B9-B9EA-64A8BFAB47F8

Q52094720-0CBA2162-55A8-4FBF-B444-AB5C01824D6D

Q52094720-0F61206E-0E61-4405-BEBF-F8AD3FD7C1FB

Q52094720-164BA0E6-B775-4D60-9A84-F0FF2090CB1B

Q52094720-1C38BAF2-B88F-484B-B37F-3222E02C0134

Q52094720-2072CA6C-6144-4019-B484-DCB9BA69B745

Q52094720-2C76AD6F-A517-4363-B63A-6BBD7D74A84C

P304

Q52094720-9E1ACCC2-A62C-47C1-A34C-B829934B676A

P31

Q52094720-721812ED-F5A0-43DE-88F1-5F4D970E824B

P356

Q52094720-1A0F7B23-1FAB-49BD-9647-932ACDA8A107

P407

Q52094720-BB715233-5196-4E90-8292-F5A484B75CAB

P433

Q52094720-94EA6F8D-40A0-4396-8850-011AF5F4CF6E

P478

Q52094720-9B304D63-1B2E-41E0-B4C7-F2361E4E8D1F

P577

Q52094720-865F7A41-155E-4793-A504-8FAE8505C443

P698

Q52094720-D7A87876-4D1B-4B36-86A4-BEB6D959C88D

P356

P1433

Journal of Biological Chemistry

P1476

Dictyostelium macroautophagy mutants vary in the severity of their developmental defects.

@en

P2093

Grant P Otto

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

Mary Y Wu

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

Nevzat Kazgan

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

O Roger Anderson

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

Richard H Kessin

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

P2860

Glucose-induced autophagy of peroxisomes in Pichia pastoris requires a unique E1-like protein

The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3

Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network

The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation

Formation process of autophagosome is traced with Apg8/Aut7p in yeast

Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells

The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway

AUT1, a gene essential for autophagocytosis in the yeast Saccharomyces cerevisiae

Tor-mediated induction of autophagy via an Apg1 protein kinase complex

Predicting coiled coils from protein sequences

P304

15621-15629

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

P31

scholarly article

P356

10.1074/JBC.M311139200

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

P407

P433

15

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

P478

279

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

P577

2004-01-21T00:00:00Z

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

P698

14736886

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