Výsledky vyhledávání - "Joan E. Garbarino"

Cancer mutations and targeted drugs can disrupt dynamic signal encoding by the Ras-Erk pathway

Autor: Amit J. Sabnis, Joan E. Garbarino, Lukasz J. Bugaj, Wendell A. Lim, Amir Mitchell, Trever G. Bivona, Jared E. Toettcher

Publikováno v: Science (New York, N.Y.), vol 361, iss 6405

INTRODUCTION Signaling pathways, such as the Ras-Erk (extracellular signal-regulated kinase) pathway, encode information through both their amplitude and dynamics. Differences in signal duration and frequency can lead to distinct cellular output deci

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d92aacbb1d2ec9186bbbb93003982872
https://escholarship.org/uc/item/3zc349g3

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Structure and Functional Role of Dynein's Microtubule-Binding Domain

Autor: Joan E. Garbarino, Ronald A. Milligan, Ronald D. Vale, Wesley E. Shipley, Andrew P. Carter, Carol Cho, Elizabeth M. Wilson-Kubalek, I. R. Gibbons

Publikováno v: Science. 322:1691-1695

Dynein motors move various cargos along microtubules within the cytoplasm and power the beating of cilia and flagella. An unusual feature of dynein is that its microtubule-binding domain (MTBD) is separated from its ring-shaped AAA+ adenosine triphos

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8984ca5ac2061336bd5a0641c8f8860
https://doi.org/10.1126/science.1164424

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The role of ubiquitin in plant senescence and stress responses

Autor: Joan E. Garbarino, William R. Belknap

Publikováno v: Trends in Plant Science. 1:331-335

Ubiquitin is a small, highly conserved protein found in all eukaryotes. Within the cell, ubiquitin is covalently linked to substrate proteins, often targeting them for degradation via the ubiquitin pathway. This pathway has been demonstrated to be re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ce2f40190d9422f2e053f0b3fa33782f
https://doi.org/10.1016/s1360-1385(96)82593-0

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Isolation of a Polyubiquitin Promoter and Its Expression in Transgenic Potato Plants

Autor: T. Oosumi, W. R. Belknap, Joan E. Garbarino

Publikováno v: Plant Physiology. 109:1371-1378

A polyubiquitin clone (ubi7) was isolated from a potato (Solanum tuberosum) genomic library using a copy-specific probe from a stress-induced ubiquitin cDNA. The genomic clone contained a 569-bp intron immediately 5[prime] to the initiation codon for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e63ac6c88547c45f1f1042bb6a3603e
https://doi.org/10.1104/pp.109.4.1371

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Recruitment interactions can override catalytic interactions in determining the functional identity of a protein kinase

Autor: Wendell A. Lim, Joan E. Garbarino, Angela P. Won

The yeast Saccharomyces cerevisae has four distinct mitogen-activated protein kinase kinases (MAPKKs), each of which has a distinct functional identity characterized by communication with specific upstream and downstream partners to form distinct fun

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13e5d8c50ffaad28916d4aabf5ffa8d6
https://europepmc.org/articles/PMC3116413/

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Rapid Diversification of Cell Signaling Phenotypes by Modular Domain Recombination

Autor: Sergio G. Peisajovich, Wendell A. Lim, Joan E. Garbarino, Ping Wei

Domain Swaps to Phenotype Shifts For natural selection there must be mechanisms that create phenotypic diversity, presumably from relatively simple molecular changes in an organism. Peisajovich et al. (p. 368 ) tested the extent to which changes in p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eeaa58d0926b82475e8299c5e0211b64
https://europepmc.org/articles/PMC2975375/

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The Affinity of the Dynein Microtubule-Binding Domain is Modulated by the Conformation of its Coiled-Coil Stalk*

Autor: Andrew P. Carter, I. R. Gibbons, Joan E. Garbarino, Samara L. Reck-Peterson, Ronald D. Vale, Carol E. Tan

The microtubule-binding domain (MTBD) of dynein is separated from the AAA (ATPase with any other activity) core of the motor by an approximately 15-nm stalk that is predicted to consist of an antiparallel coiled coil. However, the structure of this c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68cf81545585ef253ada1e2e51f1e4ce
https://europepmc.org/articles/PMC1464088/

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Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein

Autor: Joan E. Garbarino, I. R. Gibbons

Publikováno v: BMC Genomics, Vol 3, Iss 1, p 18 (2002)
BMC Genomics

Background The largest open reading frame in the Saccharomyces genome encodes midasin (MDN1p, YLR106p), an AAA ATPase of 560 kDa that is essential for cell viability. Orthologs of midasin have been identified in the genome projects for Drosophila, Ar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65393e51418c5294fbba64b3e99b1532
http://www.biomedcentral.com/1471-2164/3/18

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