p53 domains: structure, oligomerization, and transformation. - Wikidata - wikimedia - TriplyDB

p53 domains: structure, oligomerization, and transformation.

p53 domains: structure, oligomerization, and transformation.

http://www.wikidata.org/entity/Q36662699

about

A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice p53 Activation following Rift Valley fever virus infection contributes to cell death and viral production Adenovirus E1B 55K represses p53 activation in vitro.Widely dispersed p53 mutation in respiratory epithelium. A novel mechanism for field carcinogenesis A new invertebrate member of the p53 gene family is developmentally expressed and responds to polychlorinated biphenyls.The DNA-binding domain mediates both nuclear and cytosolic functions of p53 Solution structure of the tetrameric minimum transforming domain of p53 Modification of two distinct COOH-terminal domains is required for murine p53 activation by bacterial Hsp70 p53 oligomerization and DNA looping are linked with transcriptional activation The dihedral symmetry of the p53 tetramerization domain mandates a conformational switch upon DNA binding Interaction of p53 with its consensus DNA-binding site Two p53 tetramers bind one consensus DNA response element Noncanonical DNA motifs as transactivation targets by wild type and mutant p53 Human cytomegalovirus and human herpesvirus 6 genes that transform and transactivate The C-terminal domain of p53 recognizes DNA damaged by ionizing radiation.A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking.Targeting protein inactivation through an oligomerization chain reaction p53 Isoforms: An Intracellular Microprocessor?Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain.Analysis of p53-regulated gene expression patterns using oligonucleotide arrays Human cytomegalovirus mtrII oncoprotein binds to p53 and down-regulates p53-activated transcription.Inhibition of parvovirus minute virus of mice replication by a peptide involved in the oligomerization of nonstructural protein NS1.Regulation of p53 oligomerization by Ras superfamily protein RBEL1A The expression of the KAI1 gene, a tumor metastasis suppressor, is directly activated by p53 Mouse bites dogma: how mouse models are changing our views of how P53 is regulated in vivo.Functional interactions between Sae2 and the Mre11 complex.The p53 tumor suppressor participates in multiple cell cycle checkpoints.Role of cysteine residues in regulation of p53 function.Efficient repression of endogenous major histocompatibility complex class II expression through dominant negative CIITA mutants isolated by a functional selection strategy.Reciprocal interference between the sequence-specific core and nonspecific C-terminal DNA binding domains of p53: implications for regulation p53--a natural cancer killer: structural insights and therapeutic concepts.Systems biophysics of gene expression.Knitting and untying the protein network: modulation of protein ensembles as a therapeutic strategy.Allosteric modulation of protein oligomerization: an emerging approach to drug design.Role of heteroduplex joints in the functional interactions between human Rad51 and wild-type p53.DNA Structure and Polymerase Fidelity: A New Role for A-DNA.Control of gene expression by modulated self-assembly.Investigations of the supercoil-selective DNA binding of wild type p53 suggest a novel mechanism for controlling p53 function.p53-mediated DNA renaturation can mimic strand exchange.Binding to the naturally occurring double p53 binding site of the Mdm2 promoter alleviates the requirement for p53 C-terminal activation.

P2860

Q22008520-A07E1F16-FC56-411D-ACAA-FC5FA1595E2C Q24319790-37566FAD-8C85-4D16-ACFB-F9CBC81F9BC2 Q24523301-3D5DB853-CA6C-4F3F-8409-A6165D281C42 Q24561466-10475ADE-F5A6-4BFF-BF32-C1C282EA2684 Q24816168-C33FA235-61DA-48F7-81BE-2A0F90475B87 Q27683709-D056A7A2-FFCB-4831-906C-150040BD8B20 Q27730258-D0BC723B-980D-4E42-B51B-FAF6D8E73658 Q28298073-65027643-EB78-4FDE-B06B-36DDA62E6C1C Q28639938-772C8881-80A6-4A39-ADA9-05466A78AB4F Q28639955-939EF944-CEF4-4ABF-8249-7E728C2B7FD6 Q28639970-A202E501-62A1-4CC7-97C6-E5E59A32081D Q30837439-77D046A4-0712-4119-9B30-AA85A0CD6581 Q33361623-BEEBEFD9-471F-46EB-82FB-E8BF57E08AC0 Q33558299-DE2AB900-D2E9-4979-89F8-2B4748A89C33 Q33846651-F346D9C3-489D-47A1-B929-CFD1FAA57059 Q33890625-67FA6F9F-B1F6-46CB-BF27-8D774A3AAA06 Q34011368-F5192160-16F4-44B8-BFD6-216B745C1666 Q34202703-F06A1D8F-5526-4AAB-A32A-B859C7557DA6 Q34250237-E89D4310-6475-4B3F-BF96-C5B59B263C0D Q35191756-34987DEB-7FA7-4C5B-B73E-2E205841C555 Q35873729-B0F523F4-8C1C-48CB-B781-188B7D5C3B84 Q35895337-2C693778-1EFE-405F-A007-76227480F1D7 Q36075403-750C213B-9D71-45C7-BE65-88AD479C4C72 Q36309832-D8BC323D-770A-45D8-BB6E-9B1ACF5AF826 Q36436702-9A52EE11-10A2-466D-8C20-1268591AED23 Q36470516-9777F19D-193A-4BF5-A517-D99DBE7EA201 Q36495323-5A7A5BAD-6419-4FC1-BA40-52430EEE19CA Q36552986-B6DB3B1F-5AA6-49F2-A692-AA1FEB93967E Q36569540-EF5EA857-0319-477B-B834-6A1091CDCDD0 Q36573345-9796ED32-551B-4795-A45A-DD5751BE81AC Q36597458-52B95B83-25DF-4F88-970B-95A8AC4440B2 Q36939727-E3C6F82A-E4A4-4D81-9785-84B9FE042F75 Q37383647-BDC9E516-963E-4449-8005-C8EE54A87429 Q38208847-575F47DB-158D-41FB-9322-37A7F84F0B7F Q38308128-2C3B7FBD-9FF1-4271-AB91-C06E6699F9CD Q38316929-9B1F58D0-F751-4D53-B389-2D0019ADAA8F Q38319284-38DBC30C-67D7-43C2-AB86-B7031FD75552 Q38336535-AE3A592B-B97F-4A0D-B5D1-2896228CCF18 Q38342661-9C447E31-0F00-4A64-8E8E-5A20189F52E3 Q38760748-8BF601FB-DD47-411B-BF10-E4411EBD98D5

P2860

p53 domains: structure, oligomerization, and transformation.

http://www.wikidata.org/entity/Q36662699

description

1994 nî lūn-bûn

@nan

1994年の論文

@ja

1994年論文

@yue

1994年論文

@zh-hant

1994年論文

@zh-hk

1994年論文

@zh-mo

1994年論文

@zh-tw

1994年论文

@wuu

1994年论文

@zh

1994年论文

@zh-cn

name

p53 domains: structure, oligomerization, and transformation.

@ast

p53 domains: structure, oligomerization, and transformation.

@en

type

label

p53 domains: structure, oligomerization, and transformation.

@ast

p53 domains: structure, oligomerization, and transformation.

@en

prefLabel

p53 domains: structure, oligomerization, and transformation.

@ast

p53 domains: structure, oligomerization, and transformation.

@en

P1433

Q36662699-43CC80DB-9FE0-475D-B64F-08DEC4451836

P1476

Q36662699-C73DCD57-5A28-4CD3-92FE-989309EDAB62

P2093

Q36662699-0C279FC0-0451-4E1B-A689-287842B7C924

Q36662699-11F8E9A5-C327-45D6-8A3C-59051D54373F

Q36662699-1FA4AA65-45D2-40D2-911B-5896C1F8BFB8

Q36662699-7D0BDAF4-3DC6-4C99-83AF-85E3F5DC71BE

Q36662699-7D8D3BCE-8708-4497-A167-EB6E018B74CB

Q36662699-7F5BBA8C-BA34-40BE-8DAD-3E801FE78752

Q36662699-C4F0EB77-8147-4B74-801F-5A76BEBE9FC6

Q36662699-CB47CD17-89BC-46F9-A7E3-EE415FB16752

P2860

Q36662699-0ADF3CBC-C6A2-46BD-9DBB-8F32DCD699B4

Q36662699-1313524F-C702-498F-9223-6DB2815C8C17

Q36662699-1584BC80-E91C-4984-BCAB-8D3C6806F827

Q36662699-1B6491F5-B567-4FE5-91BD-4CD217667E5F

Q36662699-255B40C0-1768-4EC0-974D-28A3B0BF2898

Q36662699-25A6C780-97AB-4B62-AC2B-B9346093DA38

Q36662699-277D2AB0-CF73-4422-BE00-EFE1D0C50FB1

Q36662699-3FC911E9-BA69-4B64-972C-BF5ED42D0625

Q36662699-4E10A596-9AE8-4D6D-A580-3071744B2DD8

Q36662699-4EF9921C-C071-45BA-A2CA-2C0E65A6FCAD

P304

Q36662699-E221B520-532C-4822-9FD6-F80689AA85ED

P31

Q36662699-06CE64CF-1220-4CFB-9C4C-D9179571B3B3

P356

Q36662699-5A58E890-7379-45CD-B843-EAB2E55D057B

P407

Q36662699-6D03233D-A8A1-4B95-98B5-28DFAACD3FBA

P433

Q36662699-D59A134F-C098-46AD-9A09-743BF1F3C993

P478

Q36662699-651D10B9-6B89-46CB-967F-DE8BF197EC2E

P577

Q36662699-3C6FA9E4-9F6D-470A-8FC0-70631ED4709C

P698

Q36662699-31CB8DC0-703D-4406-8708-9881DA363E11

P932

Q36662699-7C92C491-2AD6-42F4-A496-6F56F3601416

P356

P1433

Molecular and Cellular Biology

P1476

p53 domains: structure, oligomerization, and transformation.

@en

P2093

G Mayr

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

J E Stenger

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

J F Schwedes

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

M E Anderson

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

M Reed

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

P Tegtmeyer

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

P Wang

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

Y Wang

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

P2860

The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases

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

High-efficiency transformation of mammalian cells by plasmid DNA

WAF1, a potential mediator of p53 tumor suppression

Oncogenic forms of p53 inhibit p53-regulated gene expression

p53 mutations in human cancers

Wild-type p53 can inhibit oncogene-mediated focus formation

The transforming and suppressor functions of p53 alleles: effects of mutations that disrupt phosphorylation, oligomerization and nuclear translocation.

Tight DNA binding and oligomerization are dispensable for the ability of p53 to transactivate target genes and suppress transformation.

The p53 proto-oncogene can act as a suppressor of transformation.

P304

5182-5191

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

P31

scholarly article

P356

10.1128/MCB.14.8.5182

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

P407

P433

8

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

P478

14

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

P577

1994-08-01T00:00:00Z

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

P698

8035799

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

P932

359037

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