Posttranslational Modifications of Chloroplast Proteins: An Emerging Field. - Test2 - elhamkhani - TriplyDB

Posttranslational Modifications of Chloroplast Proteins: An Emerging Field.

Posttranslational Modifications of Chloroplast Proteins: An Emerging Field.

http://www.wikidata.org/entity/Q38441683

about

Immunotherapy using algal-produced Ara h 1 core domain suppresses peanut allergy in mice.Plant-based vaccines for oral delivery of type 1 diabetes-related autoantigens: Evaluating oral tolerance mechanisms and disease prevention in NOD mice.Post-translational Modifications in Regulation of Chloroplast Function: Recent Advances.Expression and functional evaluation of biopharmaceuticals made in plant chloroplasts.Golgi-to-plastid trafficking of proteins through secretory pathway: Insights into vesicle-mediated import toward the plastids Proteomic Analysis of a Fraction with Intact Eyespots of Chlamydomonas reinhardtii and Assignment of Protein Methylation.LIGHT-INDUCED RICE1 Regulates Light-Dependent Attachment of LEAF-TYPE FERREDOXIN-NADP+ OXIDOREDUCTASE to the Thylakoid Membrane in Rice and Arabidopsis.Dynamic N-glycoproteome analysis of maize seedling leaves during de-etiolation using Concanavalin A lectin affinity chromatography and a nano-LC-MS/MS-based iTRAQ approach.Serine and threonine residues of plant STN7 kinase are differentially phosphorylated upon changing light conditions and specifically influence the activity and stability of the kinase.

P2860

Q37343952-B0A7515A-3652-4D10-AC87-E685EA293D88 Q37638227-4F0EBA55-94ED-478F-AA79-04583F240F1C Q37660837-DBCD8B6E-ADA4-483F-AE96-79E8DE53D1FA Q39147640-FAC18182-93BC-40F3-B73F-4F62249DA30E Q41412743-20BC1F7A-E379-4398-A54D-7406D2D7BD99 Q41970805-773431E4-4920-4A33-8015-987B2E3A5BE5 Q46585513-EE016DF5-DC73-40EE-90DF-1F4FC838BFF1 Q47753257-50B15DAA-0403-454D-9629-338E2AB07953 Q50239353-CF915685-57F5-4537-A4CF-466B005B431A

P2860

Posttranslational Modifications of Chloroplast Proteins: An Emerging Field.

http://www.wikidata.org/entity/Q38441683

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Posttranslational Modifications of Chloroplast Proteins: An Emerging Field.

@en

type

label

Posttranslational Modifications of Chloroplast Proteins: An Emerging Field.

@en

prefLabel

Posttranslational Modifications of Chloroplast Proteins: An Emerging Field.

@en

P1433

Q38441683-FCB9F8F2-C56B-4CFF-9A7F-15B066E0C1C3

P1476

Q38441683-5720B1D2-F192-4047-B997-B9CEF307FC65

P2093

Q38441683-01959ED4-0E9C-40A3-B2CB-1F094CB21F5C

Q38441683-662338D3-0095-47D7-A67B-CD6FA6706504

Q38441683-D70D695D-14ED-433A-9650-943B3CD5D8F3

P2860

Q38441683-03117A07-FBCF-44AF-8C88-5A72A0CEE52A

Q38441683-04002184-C2F4-4F35-9A15-3472E860AD15

Q38441683-048DBF67-E26B-4C60-8C65-560ABD5DB0D2

Q38441683-0C25CFBB-EB7C-47C4-B536-8108B8CCFAD3

Q38441683-12024AB0-C48E-4446-896F-788E9174E60D

Q38441683-132F0831-202E-4A3A-A9FF-77BA0EB61B0B

Q38441683-13391E09-6AD4-4BB2-9522-B08D892E4429

Q38441683-13F81310-5CE3-4918-B9A7-593A13CB9B55

Q38441683-143B33AC-4508-4598-BCA6-C02650DFCAB6

Q38441683-17331969-26F7-4F16-8FE0-43CB335A328E

P304

Q38441683-816E35F9-CE5B-4D8D-B7FD-2DCAFA9A3810

P31

Q38441683-D82527AF-38A5-4C64-93F5-320A60942E95

P356

Q38441683-FE4A8A20-6AC2-4124-B869-21BCFAC74244

P407

Q38441683-04D995E8-B66C-4DDD-8DBD-5B81D1AF6DEE

P433

Q38441683-30AF02E1-6C63-4748-9CE1-AE084F91A096

P478

Q38441683-9D9CBCF0-C85F-443E-A996-BEF1178ADB1D

P50

Q38441683-81CB5776-BF15-4FCC-BDB4-D78BAAC08651

Q38441683-8ADD0D19-705C-42AF-9CDF-2CB48D43D3AE

Q38441683-D9E657CE-E28C-4F0C-821B-68D6601AC124

P577

Q38441683-5702DB75-28FB-4D34-BE53-2764D953F38C

P698

Q38441683-33D32F81-18B2-4936-999F-6DAAF6F37CCB

P932

Q38441683-B5D1DABE-BFAF-4130-B479-DEC355A7C644

P356

P1433

Plant Physiology

P1476

Posttranslational Modifications of Chloroplast Proteins: An Emerging Field

@en

P2093

Minna M Koskela

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

Nina Lehtimäki

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

Paula Mulo

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

P2860

Translating the Histone Code

The functional diversity of protein lysine methylation

N-Terminal Acetylation Acts as an Avidity Enhancer Within an Interconnected Multiprotein Complex

Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p.

Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-α-acetylation features

Affinity purification of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilon N-methyltransferase

Sorting signals, N-terminal modifications and abundance of the chloroplast proteome

Role of plastid protein phosphatase TAP38 in LHCII dephosphorylation and thylakoid electron flow

Uncovering the protein lysine and arginine methylation network in Arabidopsis chloroplasts

Global analysis of lysine acetylation suggests the involvement of protein acetylation in diverse biological processes in rice (Oryza sativa)

P304

768-775

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

P31

scholarly article

P356

10.1104/PP.15.00117

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

P407

P433

3

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

P478

168

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

P50

Minna M Koskela

Nina Lehtimäki

P577

2015-04-24T00:00:00Z

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

P698

25911530

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

P932

4741338

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