The human papillomavirus E7-E2 interaction mechanism in vitro reveals a finely tuned system for modulating available E7 and E2 proteins.
about
Ordered self-assembly mechanism of a spherical oncoprotein oligomer triggered by zinc removal and stabilized by an intrinsically disordered domainSequence evolution of the intrinsically disordered and globular domains of a model viral oncoprotein.Conformational dissection of a viral intrinsically disordered domain involved in cellular transformation.Minute time scale prolyl isomerization governs antibody recognition of an intrinsically disordered immunodominant epitopeThe papillomavirus E2 proteinsTumor suppressor or oncogene? A critical role of the human papillomavirus (HPV) E2 protein in cervical cancer progression.
P2860
The human papillomavirus E7-E2 interaction mechanism in vitro reveals a finely tuned system for modulating available E7 and E2 proteins.
description
2009 nî lūn-bûn
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2009年の論文
@ja
2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
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2009年學術文章
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name
The human papillomavirus E7-E2 ...... available E7 and E2 proteins.
@en
The human papillomavirus E7-E2 ...... available E7 and E2 proteins.
@nl
type
label
The human papillomavirus E7-E2 ...... available E7 and E2 proteins.
@en
The human papillomavirus E7-E2 ...... available E7 and E2 proteins.
@nl
prefLabel
The human papillomavirus E7-E2 ...... available E7 and E2 proteins.
@en
The human papillomavirus E7-E2 ...... available E7 and E2 proteins.
@nl
P2093
P356
P1433
P1476
The human papillomavirus E7-E2 ...... available E7 and E2 proteins.
@en
P2093
Clara Smal
Diana E Wetzler
Karina I Dantur
Leonardo G Alonso
Lucia B Chemes
Mariano Dellarole
María M Garcia-Alai
P304
11939-11949
P356
10.1021/BI901415K
P407
P577
2009-12-01T00:00:00Z