Identification of intrinsic order and disorder in the DNA repair protein XPA. - Wikidata - wikimedia - TriplyDB

Identification of intrinsic order and disorder in the DNA repair protein XPA.

Identification of intrinsic order and disorder in the DNA repair protein XPA.

http://www.wikidata.org/entity/Q36640580

about

Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B Structural basis for the recruitment of ERCC1-XPF to nucleotide excision repair complexes by XPA Intrinsically Disordered Side of the Zika Virus Proteome Aberrant mobility phenomena of the DNA repair protein XPA Natively unfolded proteins: a point where biology waits for physics Unstructural biology of the Dengue virus proteins.Understanding protein non-folding.Intrinsic disorder in spondins and some of their interacting partners.The MULTICOM toolbox for protein structure prediction High-throughput characterization of intrinsic disorder in proteins from the Protein Structure Initiative.Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners.A large nonconserved region of the tethering protein Leashin is involved in regulating the position, movement, and function of Woronin bodies in Aspergillus oryzae Molecular characterization and functional activity of an IL-15 antagonist MutIL-15/Fc human fusion protein.A new structural insight into XPA-DNA interactions.Intrinsic disorder and functional proteomics.Nucleotide excision repair by dual incisions in plants.Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1 Utilization of protein intrinsic disorder knowledge in structural proteomics.Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs.Functions of disordered regions in mammalian early base excision repair proteins.Mass spectrometry methods for intrinsically disordered proteins.Disorder in the lifetime of a protein Conformation of a plasmid replication initiator protein affects its proteolysis by ClpXP system.Modulation of the structural integrity of helix F in apomyoglobin by single amino acid replacements.The intrinsic disorder status of the human hepatitis C virus proteome.Intracellular assembly of cyanophage Syn5 proceeds through a scaffold-containing procapsid.Simple sequence in brain and nervous system specific proteins.Bacterial cupredoxin azurin hijacks cellular signaling networks: Protein-protein interactions and cancer therapy.A novel two-dimensional electrophoresis technique for the identification of intrinsically unstructured proteins.Stop codon readthrough generates a C-terminally extended variant of the human vitamin D receptor with reduced calcitriol response.Disulfide bonds and disorder in granulin-3: An unusual handshake between structural stability and plasticity.Accurate prediction of disorder in protein chains with a comprehensive and empirically designed consensus

P2860

Q27000495-6E5723CE-F68D-4DCF-9E16-CBD0B7875672 Q27643704-F90AB7F6-3841-4293-B8BE-05D541C58578 Q27648846-1B70FD0A-3199-465B-9393-CB1D6923013E Q27926249-A2AB5DFF-672B-4BBF-84A1-F3AECA04C6B7 Q28367384-A8E146DF-7969-41E6-9CBA-DBB219A69FFA Q29616416-DDD5C9A3-6864-4E44-909D-A7A0E43A376E Q30375946-CAB577F5-9ACA-4233-86EA-7B5DAE5FEC87 Q30385084-51DA1294-67CF-4836-8E1B-4A02B0B26C66 Q30399043-4DAAF610-2668-4227-9E39-496B83806745 Q30416170-462FED5E-ECB5-496A-8C49-1FE8277555EB Q30417432-45DFC378-5935-4FB1-BFDA-9DE77FAB6DD2 Q33325589-FFB22FF7-ADB4-457D-9711-846C9E51D7B6 Q34057060-43D4CFEB-1C7A-4CB3-8A8A-C820D3D0CA1E Q34545655-4EC9F2DA-EB6E-4249-87B1-FFB8FFCC4AF1 Q34706807-F6BF0CF4-E60F-4987-B3E3-E9093929CFDA Q35632957-3AC1C1FE-A268-4FBF-AC79-A051EEC941DD Q36866140-555B5A3A-62B6-40C4-B12B-2EFC7EE602C5 Q37369361-D84C82F2-AF06-49AF-B2D5-52132EF35B92 Q37633034-D27D44F6-3455-4828-833B-63D424D2C8AE Q37649607-7BCBC092-B7B4-4DB1-AE22-8956F3BC73C7 Q37780480-0C6EBF1C-A620-45C3-8BB3-880B4565BD00 Q38056343-C1256F24-5116-4A76-9503-E012DA5F686E Q38779717-CE4AF04B-C435-438D-B89C-B6B74DADDCE3 Q42064722-854297C2-8676-444C-8B90-F5FC503E11E4 Q42154324-8C7A6FEE-CC74-4422-BBBC-3CBAA9D3750F Q42223133-E780AF14-34A3-4ADB-BE26-EDCFD626D59B Q42707017-AB60E17B-BAD1-4EF0-9A75-D4FD45F9F618 Q45296624-1F896C47-F541-4A6B-93F3-DABD69A2A0CB Q46299094-275F2EB8-9313-45C8-96E4-86BF31279E53 Q46751790-D820662E-48CB-4126-8F23-70FF1730BA91 Q47547464-A500F630-54F2-4663-A8E3-92AE3A5D9373 Q50947419-B762A3B0-EB1E-48CC-8589-8EF8CD9AEC52 Q56992931-1B7BAB4A-243A-4200-AFB3-AE283BEDB031

P2860

Identification of intrinsic order and disorder in the DNA repair protein XPA.

http://www.wikidata.org/entity/Q36640580

description

2001 nî lūn-bûn

@nan

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

2001年论文

@zh

2001年论文

@zh-cn

name

Identification of intrinsic order and disorder in the DNA repair protein XPA.

@ast

Identification of intrinsic order and disorder in the DNA repair protein XPA.

@en

type

label

Identification of intrinsic order and disorder in the DNA repair protein XPA.

@ast

Identification of intrinsic order and disorder in the DNA repair protein XPA.

@en

prefLabel

Identification of intrinsic order and disorder in the DNA repair protein XPA.

@ast

Identification of intrinsic order and disorder in the DNA repair protein XPA.

@en

P1433

Q36640580-E3841557-786F-4027-BAB5-65EC4A3CA1B8

P1476

Q36640580-675DC4AE-D109-46A8-A271-64BD7084C597

P2093

Q36640580-28003A99-B81C-42BC-9CAD-677232A91EEE

Q36640580-2B8B8DA5-5E81-43B2-BFB9-B9D5DFADDF30

Q36640580-2F1C2078-B0CA-4E89-A48B-025B5DB39B95

Q36640580-3A82DFE9-990F-4101-980F-CBAAE8FA007C

Q36640580-5DE21D4E-C58B-4DF3-8959-CC3231564107

Q36640580-A55778FB-D130-4A00-9674-4855885B199E

Q36640580-B3A822A8-36E4-4DFE-8D58-D38E5BBC1908

Q36640580-B416E98A-599F-4708-A99B-18C1A436299A

Q36640580-E2D2319E-12B8-4529-B268-1A0E93786F5A

P2860

Q36640580-0233AD3C-224C-46FE-B81C-0A5CF55EB649

Q36640580-050A647E-27AE-46BD-BF29-3A9D74ACBD48

Q36640580-05DB8407-CB09-4613-8893-655F70E59259

Q36640580-17D1B4B9-8943-482C-AE7D-C9A951273F35

Q36640580-1D6A56D1-21ED-44D4-9F92-EC6D6C1F83C2

Q36640580-233715DA-44FF-4F29-A205-DADDDEEB4ED6

Q36640580-2D6CC8AC-37E5-4F15-BBE5-697D7F108C73

Q36640580-3A5DD6D0-74C3-4C10-8428-8EFFB9F4CF36

Q36640580-3F8AA15B-CF23-42DE-94EC-491E94EA7FEB

Q36640580-462264F0-2E1D-45BD-848F-B14DC37E89A3

P304

Q36640580-A08EBBB6-F041-4677-A3A6-731802E62B48

P31

Q36640580-CF0AA897-50DA-4ABF-85EA-DCDB1DF62AA5

P356

Q36640580-0215EA57-A244-4CB8-91B4-03664E9FC123

P433

Q36640580-67E9BCF5-C3F5-4217-A26B-D4BF6187C103

P478

Q36640580-D4F54DDC-8FAB-4A65-8653-86E9E30058A8

P577

Q36640580-87D8BB88-2151-4C68-B1F0-0222F87E7A32

P5875

Q36640580-EA6C504B-0F5F-4EFC-90BC-FA975F33478A

P698

Q36640580-C36BDF8B-6534-4849-B95F-4DDAE40E8684

P932

Q36640580-9D5AECDD-D150-46BD-A5BA-29BE28A00613

P356

P1433

Protein Science

P1476

Identification of intrinsic order and disorder in the DNA repair protein XPA.

@en

P2093

A K Dunker

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

A L Kimzey

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

C D Masselon

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

C J Brown

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

E C Garner

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

E J Ackerman

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

J E Bruce

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

L M Iakoucheva

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

R D Smith

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

P2860

Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex

Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies

NMR structure of the mouse prion protein domain PrP(121-231)

Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA

Mutational analysis of the structure and function of the xeroderma pigmentosum group A complementing protein. Identification of essential domains for nuclear localization and DNA excision repair

Empirical predictions of protein conformation

Protein complexes in nucleotide excision repair

Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure

P304

560-571

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

P31

scholarly article

P356

10.1110/PS.29401

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

P433

3

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

P478

10

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

P577

2001-03-01T00:00:00Z

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

P5875

26020386

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

P698

11344324

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

P932

2374143

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