Functional chimeras between the catalytic domains of the mycobacterial adenylyl cyclase Rv1625c and a Paramecium guanylyl cyclase.

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Characterization of phylogenetically distant members of the adenylate cyclase family from mycobacteria: Rv1647 from Mycobacterium tuberculosis and its orthologue ML1399 from M. leprae Mycobacterial adenylyl cyclases: biochemical diversity and structural plasticity.

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Functional chimeras between the catalytic domains of the mycobacterial adenylyl cyclase Rv1625c and a Paramecium guanylyl cyclase.

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2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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name

Functional chimeras between th ...... a Paramecium guanylyl cyclase.

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Functional chimeras between th ...... a Paramecium guanylyl cyclase.

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Functional chimeras between th ...... a Paramecium guanylyl cyclase.

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Functional chimeras between th ...... a Paramecium guanylyl cyclase.

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Functional chimeras between th ...... a Paramecium guanylyl cyclase.

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Functional chimeras between th ...... a Paramecium guanylyl cyclase.

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Functional chimeras between th ...... a Paramecium guanylyl cyclase.

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Joachim E Schultz

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Jürgen U Linder

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

Lucila I Castro

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

Ying-Lan Guo

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P2860

Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS

Interaction of Gsalpha with the cytosolic domains of mammalian adenylyl cyclase

Adenylyl cyclase Rv1625c of Mycobacterium tuberculosis: a progenitor of mammalian adenylyl cyclases

Eukaryotic-like adenylyl cyclases in Mycobacterium tuberculosis H37Rv: cloning and characterization

Adenylyl cyclase Rv1264 from Mycobacterium tuberculosis has an autoinhibitory N-terminal domain

Mutational analysis of the Mycobacterium tuberculosis Rv1625c adenylyl cyclase: residues that confer nucleotide specificity contribute to dimerization

Inhibition of adenylyl and guanylyl cyclase isoforms by the antiviral drug foscarnet.

Construction of a soluble adenylyl cyclase activated by Gs alpha and forskolin.

The class III adenylyl cyclases: multi-purpose signalling modules.

Guanylyl cyclases with the topology of mammalian adenylyl cyclases and an N-terminal P-type ATPase-like domain in Paramecium, Tetrahymena and Plasmodium.

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151-154

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scholarly article

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10.1016/J.FEBSLET.2004.05.025

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English

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1-3

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2004-06-01T00:00:00Z

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8510517

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15196937

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Functional chimeras between the catalytic domains of the mycobacterial adenylyl cyclase Rv1625c and a Paramecium guanylyl cyclase.

about

P2860

P2860

Functional chimeras between the catalytic domains of the mycobacterial adenylyl cyclase Rv1625c and a Paramecium guanylyl cyclase.

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