Rvs167

Localization of Rvs167 BAR domain A Schematic of Rvs protein complex

Localization of Rvs167 in the absence of membrane curvature Single

Rvs167 BAR domains need membrane curvature to localize to endocytic

RVS161 and RVS167 have identical synthetic genetic interactions A

Rvs167 molecules interact independently of Rvs161 and Gvp36 a

Interaction of yeast Rvs167 and Pho85 cyclindependent kinase complexes

BAR Domain Proteins Rvs161 and Rvs167 Contribute to Candida albicans

Structurebased mutations generated in Rvs161 and Rvs167 A Homology

Rvs167 molecules interact independently of Rvs161 and Gvp36 a

Expression of RVS167 constructs in vivo A Western blot analysis

Structurebased mutations generated in Rvs161 and Rvs167 A Homology

Ysc84 and Rvs167 bind to a common site on Las17 A Yeast twohybrid

Bzz1 and Rvs167 regulate NPF association with the coat in absence of

Yeast lacking the amphiphysin family protein Rvs167 is sensitive to

Yeast Dynamin Vps1 and Amphiphysin Rvs167 Function Together During

Interaction of yeast Rvs167 and Pho85 cyclindependent kinase complexes

Rvs167 BAR domains need membrane curvature to localize to endocytic

BAR Domain Proteins Rvs161 and Rvs167 Contribute to Candida albicans

A Truncated alleles of Rvs167 and Inn1 were used to show that the

Localization of Rvs167 BAR domain A Schematic of Rvs protein complex

Interaction of yeast Rvs167 and Pho85 cyclindependent kinase complexes

Expression of RVS167 constructs in vivo A Western blot analysis

Interaction of yeast Rvs167 and Pho85 cyclindependent kinase complexes

Yeast lacking the amphiphysin family protein Rvs167 is sensitive to

The deletion of SUR4 in rvs167 mutants does not remediate actin

Effect of RVS167 constructs on fluidphase endocytotic uptake of

Yeast lacking the amphiphysin family protein Rvs167 is sensitive to

PDF Yeast lacking the amphiphysin family protein Rvs167 is sensitive

BAR Domain Proteins Rvs161 and Rvs167 Contribute to Candida albicans

RCSB PDB MAMABAKCEPC0528 Predicted interaction between RVS167 and YP077

The rvs161 rvs167 BAR domain mutants show defects in endocytosis A

Structurebased mutations generated in Rvs161 and Rvs167 A Homology

RVS161 and RVS167 have identical synthetic genetic interactions A

Hof1 and Rvs167 Have Redundant Roles in Actomyosin Ring Function during

Localization of Rvs167GFP in rvs161 rvs167 mutants A Maximum

Hof1 and Rvs167 Have Redundant Roles in Actomyosin Ring Function during

The rvs161 rvs167 BAR domain mutants show defects in endocytosis A

Localization of Rvs167GFP in rvs161 rvs167 mutants A Maximum

RVS161 and RVS167 have identical synthetic genetic interactions A

Slt2p is activated in rvs161 and rvs167 mutants A Immunoblot

RVS161 and RVS167 have identical synthetic genetic interactions A

Interaction of Rvs167p and Rvs161p A Schematic illustration of the

vps1Δ and rvs167Δ deletion. A: Left: Single frames from time-lapse ...

vps1 and rvs167 deletion A Left Single frames from timelapse

BiFC reveals different distributions and interactions for the three

Proper localization and stability of Rvs167p depends on the presence of

Amphiphysin AoRvs167Mediated Membrane Curvature Facilitates Trap

Characterization of the Yeast Amphiphysins Rvs161p and Rvs167p Reveals

Rvs167GFP localization is perturbed by aureobasidin A AbA an

The Rsp5 Ubiquitin Ligase Binds to and Ubiquitinates Members of the

Dissecting BAR Domain Function in the Yeast Amphiphysins Rvs161 and

Cellular localization of Rvs167pGFP fusion protein Representative

Rvs167Rvs167 lattices form in rvs161 cells and their localization is

Characterization of the Yeast Amphiphysins Rvs161p and Rvs167p Reveals

Regulation of the Yeast Amphiphysin Homologue Rvs167p by

rvs167Δ but not vps1Δ changes coat movement. (A) Left: One thousand ...

rvs167 but not vps1 changes coat movement A Left One thousand

Eight representative tetrads depicting A rvs167 iqg11 synthetic

Regulation of the Yeast Amphiphysin Homologue Rvs167p by

Twohybrid analysis The interaction of Rvs167p pEGRVS167 with actin

Endocytic dynamics in WT and rvs167-sh3Δ cells. A,B: Averaged centroid ...

Endocytic dynamics in WT and rvs167sh3 cells AB Averaged centroid

Characterizing the Sphingolipid Signaling Pathway That Remediates

Interaction of Rvs167p and Rvs161p A Schematic illustration of the

Regulation of membrane scission in yeast endocytosis Molecular

Synthetic lethal interactions between complementary pathways Proteins

Calmodulin Promotes NBAR DomainMediated Membrane Constriction and

Regulation of the Yeast Amphiphysin Homologue Rvs167p by

Regulation of membrane scission in yeast endocytosis Molecular

Regulation of the Yeast Amphiphysin Homologue Rvs167p by

Diploid selection plates from limited mating assays for rvs161 and

Schematic model showing the localization of nine proteins on an

Rvs161p and Rvs167p the Two Yeast Amphiphysin Homologs Function

Dissecting BAR Domain Function in the Yeast Amphiphysins Rvs161 and

Figure 1 from The Rsp5 Ubiquitin Ligase Binds to and Ubiquitinates

Identification and Characterization of Rvs162Rvs1673 a Novel NBAR

Rvs161p and Rvs167p the Two Yeast Amphiphysin Homologs Function

Three members of the yeast NBAR proteins family form heterogeneous

Endocytic dynamics is changed in rvs167-sh3Δ cells. (A, B) Centroid ...

Endocytic dynamics is changed in rvs167sh3 cells A B Centroid

Rvs167GFP does not localize in a polarized manner in the myo5 and

Spatiotemporal regulation of endocytic protein assembly by SH3 domains

Rvs161p and Rvs167p the Two Yeast Amphiphysin Homologs Function

Characterization of the Yeast Amphiphysins Rvs161p and Rvs167p Reveals

Full article Phosphorylation Regulates the Endocytic Function of the

The Rsp5 Ubiquitin Ligase Binds to and Ubiquitinates Members of the

Characterization of the Yeast Amphiphysins Rvs161p and Rvs167p Reveals

A Tetrad analysis of diploid yeast cells lacking one copy of HOF1 and

Subcellular structures on which BinAmphiphysinRvs167 BAR domain

Actin cytoskeleton distribution in the rvs1671 mutant strain

Identification and Characterization of Rvs162Rvs1673 a Novel NBAR

Pathogens Free FullText Amphiphysin AoRvs167Mediated Membrane

Subcellular structures on which BinAmphiphysinRvs167 BAR domain

Identification and Characterization of Rvs162Rvs1673 a Novel NBAR

An enriched CO 2 atmosphere stimulates invasive growth of the rvs161

Dissecting BAR Domain Function in the Yeast Amphiphysins Rvs161 and

Identiﬁcation and Characterization of Rvs162/Rvs167-3, a Novel N-BAR ...

Identication and Characterization of Rvs162Rvs1673 a Novel NBAR

Phenotypic analysis reveals a genetic interaction between Rvs1673 and

Regulation of the Yeast Amphiphysin Homologue Rvs167p by

Identification and Characterization of Rvs162Rvs1673 a Novel NBAR

Interaction of Rvs161p and Rvs167p is required for the stability of

Phenotypic analysis reveals a genetic interaction between Rvs1673 and

Dissecting BAR Domain Function in the Yeast Amphiphysins Rvs161 and

Spatiotemporal regulation of endocytic protein assembly by SH3 domains

Rvs167GFP does not localize in a polarized manner in the myo5 and

endocytosis arthrobotrys fungi nematode Pathogens MDPI

Regulation of the Yeast Amphiphysin Homologue Rvs167p by

The Rsp5 Ubiquitin Ligase Binds to and Ubiquitinates Members of the

Spatiotemporal regulation of endocytic protein assembly by SH3 domains

Characterization of the Yeast Amphiphysins Rvs161p and Rvs167p Reveals

Dissecting BAR domain function in the yeast Amphiphysins Rvs161 and

Regulation of membrane scission in yeast endocytosis Molecular

Effects of deletion of ORM2 on sphingolipid levels and SRE sensitivity

Actin cytoskeleton distribution in the rvs1671 mutant strain

Characterization of the Yeast Amphiphysins Rvs161p and Rvs167p Reveals

Regulation of membrane scission in yeast endocytosis Molecular

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