A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.

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A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.

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A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.

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A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.

@en

A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.

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A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.

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A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.

@nl

P1476

A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.

@en

P2093

Caralyn E Flack

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

John S Parkinson

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

P2860

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

Design of a minimal protein oligomerization domain by a structural approach

Structure of Concatenated HAMP Domains Provides a Mechanism for Signal Transduction

The mechanisms of HAMP-mediated signaling in transmembrane receptors

HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors

Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation

A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants

The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins

P304

E3519-E3528

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P31

scholarly article

P356

10.1073/PNAS.1721554115

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P407

English

P433

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P478

115

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P577

2018-03-26T00:00:00Z

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P698

29581254

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P921

chemoreceptor

P932

5899470

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