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Chm7 and Heh1 form a nuclear envelope subdomain for nuclear pore complex quality control

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Outgoing claims: the papers this work cites, builds on, or argues with.

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Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae

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The ImageJ ecosystem: An open platform for biomedical image analysis

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Additional vectors for PCR-based gene tagging inSaccharomyces cerevisiae andSchizosaccharomyces pombe using nourseothricin resistance

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Bimolecular fluorescence complementation analysis system for in vivo detection of protein–protein interaction in Saccharomyces cerevisiae

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T-coffee: a novel method for fast and accurate multiple sequence alignment 1 1Edited by J. Thornton

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Multifunctional yeast high-copy-number shuttle vectors

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Functional Architecture of the Cell's Nucleus in Development, Aging, and Disease

inferredcites →https://doi.org/10.1016/j.ceb.2016.03.009openalex-snapshot

A model for coordinating nuclear mechanics and membrane remodeling to support nuclear integrity

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Functional Reconstitution of ESCRT-III Assembly and Disassembly

inferredcites →https://doi.org/10.1016/j.cell.2008.11.037openalex-snapshot

Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells

inferredcites →https://doi.org/10.1016/j.cell.2010.04.036openalex-snapshot

Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in Metazoa

inferredcites →https://doi.org/10.1016/j.cell.2012.03.032openalex-snapshot

Nuclear Envelope Budding Enables Large Ribonucleoprotein Particle Export during Synaptic Wnt Signaling

inferredcites →https://doi.org/10.1016/j.cell.2012.04.028openalex-snapshot

Functional Repurposing Revealed by Comparing S. pombe and S. cerevisiae Genetic Interactions

inferredcites →https://doi.org/10.1016/j.cell.2012.08.039openalex-snapshot

The Endosomal Sorting Complex ESCRT-II Mediates the Assembly and Architecture of ESCRT-III Helices

inferredcites →https://doi.org/10.1016/j.cell.2013.02.046openalex-snapshot

Enclosing Chromatin: Reassembly of the Nucleus after Open Mitosis

inferredcites →https://doi.org/10.1016/j.cell.2013.07.037openalex-snapshot

Identification of Long-Lived Proteins Reveals Exceptional Stability of Essential Cellular Structures

inferredcites →https://doi.org/10.1016/j.cell.2013.10.055openalex-snapshot

Integrated Structural Analysis of the Human Nuclear Pore Complex Scaffold

inferredcites →https://doi.org/10.1016/j.cell.2014.09.012openalex-snapshot

Surveillance of Nuclear Pore Complex Assembly by ESCRT-III/Vps4

inferredcites →https://doi.org/10.1016/j.cell.2015.10.017openalex-snapshot

Relaxation of Loaded ESCRT-III Spiral Springs Drives Membrane Deformation

inferredcites →https://doi.org/10.1016/j.celrep.2013.03.015openalex-snapshot

Torsin Mediates Primary Envelopment of Large Ribonucleoprotein Granules at the Nuclear Envelope

inferredcites →https://doi.org/10.1016/j.devcel.2004.09.003openalex-snapshot

ESCRT-II, an Endosome-Associated Complex Required for Protein Sorting

inferredcites →https://doi.org/10.1016/j.devcel.2006.03.013openalex-snapshot

Structural Basis for Budding by the ESCRT-III Factor CHMP3

inferredcites →https://doi.org/10.1016/j.devcel.2008.05.014openalex-snapshot

Two Distinct Modes of ESCRT-III Recognition Are Required for VPS4 Functions in Lysosomal Protein Targeting and HIV-1 Budding

inferredcites →https://doi.org/10.1016/j.devcel.2008.08.013openalex-snapshot

Ordered Assembly of the ESCRT-III Complex on Endosomes Is Required to Sequester Cargo during MVB Formation

inferredcites →https://doi.org/10.1016/j.devcel.2009.07.008openalex-snapshot

Structure and Function of the ESCRT-II-III Interface in Multivesicular Body Biogenesis

inferredcites →https://doi.org/10.1016/j.devcel.2015.02.017openalex-snapshot

Nuclear Pore Basket Proteins Are Tethered to the Nuclear Envelope and Can Regulate Membrane Curvature

inferredcites →https://doi.org/10.1016/j.devcel.2015.04.027openalex-snapshot

Nup153 Recruits the Nup107-160 Complex to the Inner Nuclear Membrane for Interphasic Nuclear Pore Complex Assembly

inferredcites →https://doi.org/10.1016/j.jmb.2008.03.030openalex-snapshot

Structural Basis for Autoinhibition of ESCRT-III CHMP3

inferredcites →https://doi.org/10.1016/j.neuron.2005.11.010openalex-snapshot

Loss of the Dystonia-Associated Protein TorsinA Selectively Disrupts the Neuronal Nuclear Envelope

inferredcites →https://doi.org/10.1016/j.str.2008.06.010openalex-snapshot

Structure and Disassembly of Filaments Formed by the ESCRT-III Subunit Vps24

inferredcites →https://doi.org/10.1016/j.tcb.2012.07.003openalex-snapshot

Alternative nuclear transport for cellular protein quality control

inferredcites →https://doi.org/10.1016/j.tibs.2013.04.001openalex-snapshot

Poring over pores: nuclear pore complex insertion into the nuclear envelope

inferredcites →https://doi.org/10.1038/emboj.2009.408openalex-snapshot

ESCRT‐II coordinates the assembly of ESCRT‐III filaments for cargo sorting and multivesicular body vesicle formation

inferredcites →https://doi.org/10.1038/emboj.2012.256openalex-snapshot

Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly

inferredcites →https://doi.org/10.1038/nature01898openalex-snapshot

RanGTP mediates nuclear pore complex assembly

inferredcites →https://doi.org/10.1038/nature05075openalex-snapshot

Karyopherin-mediated import of integral inner nuclear membrane proteins

inferredcites →https://doi.org/10.1038/nature06405openalex-snapshot

The molecular architecture of the nuclear pore complex

inferredcites →https://doi.org/10.1038/nature14408openalex-snapshot

Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing

inferredcites →https://doi.org/10.1038/nature14503openalex-snapshot

ESCRT-III controls nuclear envelope reformation

inferredcites →https://doi.org/10.1038/nature14506openalex-snapshot

Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus

inferredcites →https://doi.org/10.1038/nature15381openalex-snapshot

In situ structural analysis of the human nuclear pore complex

inferredcites →https://doi.org/10.1038/nature15548openalex-snapshot

Autophagy mediates degradation of nuclear lamina

inferredcites →https://doi.org/10.1038/nprot.2015.053openalex-snapshot

The Phyre2 web portal for protein modeling, prediction and analysis

inferredcites →https://doi.org/10.1038/nsmb.1621openalex-snapshot

Structural basis for ESCRT-III protein autoinhibition

inferredcites →https://doi.org/10.1038/nsmb1194openalex-snapshot

A general amphipathic α-helical motif for sensing membrane curvature

inferredcites →https://doi.org/10.1038/sj.embor.7400889openalex-snapshot

MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly

inferredcites →https://doi.org/10.1042/bj20060897openalex-snapshot

CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and functions in the endosomal sorting pathway

inferredcites →https://doi.org/10.1073/pnas.0603788103openalex-snapshot

Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding

inferredcites →https://doi.org/10.1073/pnas.0801567105openalex-snapshot

ALIX-CHMP4 interactions in the human ESCRT pathway

inferredcites →https://doi.org/10.1074/jbc.274.32.22646openalex-snapshot

Nup192p Is a Conserved Nucleoporin with a Preferential Location at the Inner Site of the Nuclear Membrane

inferredcites →https://doi.org/10.1080/19491034.2015.1035844openalex-snapshot

ESCRTs breach the nuclear border

inferredcites →https://doi.org/10.1083/jcb.123.2.275openalex-snapshot

A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic.

inferredcites →https://doi.org/10.1083/jcb.133.6.1141openalex-snapshot

Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p.

inferredcites →https://doi.org/10.1083/jcb.135.2.329openalex-snapshot

In vivo nuclear transport kinetics in Saccharomyces cerevisiae: a role for heat shock protein 70 during targeting and translocation.

inferredcites →https://doi.org/10.1083/jcb.149.5.1027openalex-snapshot

Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

inferredcites →https://doi.org/10.1083/jcb.153.4.709openalex-snapshot

A Link between the Synthesis of Nucleoporins and the Biogenesis of the Nuclear Envelope

inferredcites →https://doi.org/10.1083/jcb.200203079openalex-snapshot

Karyopherins in nuclear pore biogenesis

inferredcites →https://doi.org/10.1083/jcb.200209116openalex-snapshot

The Ran GTPase cycle is required for yeast nuclear pore complex assembly

inferredcites →https://doi.org/10.1083/jcb.200608141openalex-snapshot

Simple kinetic relationships and nonspecific competition govern nuclear import rates in vivo

inferredcites →https://doi.org/10.1083/jcb.200702120openalex-snapshot

The yeast integral membrane protein Apq12 potentially links membrane dynamics to assembly of nuclear pore complexes

inferredcites →https://doi.org/10.1083/jcb.200707031openalex-snapshot

Plasma membrane deformation by circular arrays of ESCRT-III protein filaments

inferredcites →https://doi.org/10.1083/jcb.200806174openalex-snapshot

ER membrane–bending proteins are necessary for de novo nuclear pore formation

inferredcites →https://doi.org/10.1083/jcb.200910043openalex-snapshot

Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution

inferredcites →https://doi.org/10.1083/jcb.201007076openalex-snapshot

Live imaging of single nuclear pores reveals unique assembly kinetics and mechanism in interphase

inferredcites →https://doi.org/10.1083/jcb.201012154openalex-snapshot

POM121 and Sun1 play a role in early steps of interphase NPC assembly

inferredcites →https://doi.org/10.1083/jcb.201304047openalex-snapshot

Inheritance of yeast nuclear pore complexes requires the Nsp1p subcomplex

inferredcites →https://doi.org/10.1083/jcb.201305115openalex-snapshot

The transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1

inferredcites →https://doi.org/10.1083/jcb.201310114openalex-snapshot

Coordinated binding of Vps4 to ESCRT-III drives membrane neck constriction during MVB vesicle formation

inferredcites →https://doi.org/10.1083/jcb.201402003openalex-snapshot

Breaching the nuclear envelope in development and disease

inferredcites →https://doi.org/10.1083/jcb.201403108openalex-snapshot

Structural analysis and modeling reveals new mechanisms governing ESCRT-III spiral filament assembly

inferredcites →https://doi.org/10.1083/jcb.201412024openalex-snapshot

Altering nuclear pore complex function impacts longevity and mitochondrial function in S. cerevisiae

inferredcites →https://doi.org/10.1091/mbc.7.12.1921openalex-snapshot

GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function.

inferredcites →https://doi.org/10.1091/mbc.e02-08-0483openalex-snapshot

Piecemeal Microautophagy of Nucleus in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1091/mbc.e03-05-0275openalex-snapshot

Importin β Negatively Regulates Nuclear Membrane Fusion and Nuclear Pore Complex Assembly

inferredcites →https://doi.org/10.1091/mbc.e06-06-0525openalex-snapshot

The Karyopherin Kap95 Regulates Nuclear Pore Complex Assembly into Intact Nuclear Envelopes In Vivo

inferredcites →https://doi.org/10.1091/mbc.e08-01-0012openalex-snapshot

Capture of AT-rich Chromatin by ELYS Recruits POM121 and NDC1 to Initiate Nuclear Pore Assembly

inferredcites →https://doi.org/10.1091/mbc.e09-02-0150openalex-snapshot

Importin β Regulates the Seeding of Chromatin with Initiation Sites for Nuclear Pore Assembly

inferredcites →https://doi.org/10.1091/mbc.e09-02-0152openalex-snapshot

Transportin Regulates Major Mitotic Assembly Events: From Spindle to Nuclear Pore Assembly

inferredcites →https://doi.org/10.1091/mbc.e09-05-0403openalex-snapshot

Structural Basis of Ist1 Function and Ist1–Did2 Interaction in the Multivesicular Body Pathway and Cytokinesis

inferredcites →https://doi.org/10.1091/mbc.e09-07-0572openalex-snapshot

Assembly of the AAA ATPase Vps4 on ESCRT-III

inferredcites →https://doi.org/10.1091/mbc.e10-06-0554openalex-snapshot

Lumenal interactions in nuclear pore complex assembly and stability

inferredcites →https://doi.org/10.1091/mbc.e14-07-1239openalex-snapshot

A novel function for theCaenorhabditis eleganstorsin OOC-5 in nucleoporin localization and nuclear import

inferredcites →https://doi.org/10.1091/mbc.e15-01-0053openalex-snapshot

Nuclear pore complex integrity requires Lnp1, a regulator of cortical endoplasmic reticulum

inferredcites →https://doi.org/10.1093/emboj/17.11.2982openalex-snapshot

The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function

inferredcites →https://doi.org/10.1093/emboj/20.18.5176openalex-snapshot

Sorting of proteins into multivesicular bodies: ubiquitin‐dependent and ‐independent targeting

inferredcites →https://doi.org/10.1093/emboj/21.11.2664openalex-snapshot

The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion

inferredcites →https://doi.org/10.1111/j.1600-0854.2007.00584.xopenalex-snapshot

Structure/Function Analysis of Four Core ESCRT‐III Proteins Reveals Common Regulatory Role for Extreme C‐Terminal Domain

inferredcites →https://doi.org/10.1126/science.1124196openalex-snapshot

Nuclear Pores Form de Novo from Both Sides of the Nuclear Envelope

inferredcites →https://doi.org/10.1126/science.1161070openalex-snapshot

Helical Structures of ESCRT-III Are Disassembled by VPS4

inferredcites →https://doi.org/10.1126/science.1217421openalex-snapshot

Extremely Long-Lived Nuclear Pore Proteins in the Rat Brain

inferredcites →https://doi.org/10.1126/science.aad8305openalex-snapshot

Structure and membrane remodeling activity of ESCRT-III helical polymers

inferredcites →https://doi.org/10.1128/ec.00101-15openalex-snapshot

Yeast Integral Membrane Proteins Apq12, Brl1, and Brr6 Form a Complex Important for Regulation of Membrane Homeostasis and Nuclear Pore Complex Biogenesis

inferredcites →https://doi.org/10.1128/mcb.16.12.7161openalex-snapshot

A Yeast Acetyl Coenzyme A Carboxylase Mutant Links Very-Long-Chain Fatty Acid Synthesis to the Structure and Function of the Nuclear Membrane-Pore Complex

inferredcites →https://doi.org/10.1128/mcb.23.2.534-542.2003openalex-snapshot

Binding Dynamics of Structural Nucleoporins Govern Nuclear Pore Complex Permeability and May Mediate Channel Gating

inferredcites →https://doi.org/10.1146/annurev-biochem-072909-101058openalex-snapshot

Membrane Fission Reactions of the Mammalian ESCRT Pathway

inferredcites →https://doi.org/10.1146/annurev.biophys.37.032807.125842openalex-snapshot

Bimolecular Fluorescence Complementation (BiFC) Analysis as a Probe of Protein Interactions in Living Cells

inferredcites →https://doi.org/10.1186/1472-6807-4-10openalex-snapshot

Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II

inferredcites →https://doi.org/10.1242/jcs.055046openalex-snapshot

Integral membrane proteins Brr6 and Apq12 link assembly of the nuclear pore complex to lipid homeostasis in the endoplasmic reticulum

inferredcites →https://doi.org/10.1242/jcs.111310openalex-snapshot

Class E compartments form in response to ESCRT dysfunction in yeast due to hyperactivity of the Vps21 Rab GTPase

inferredcites →https://doi.org/10.1242/jcs.158915openalex-snapshot

Nuclear pore targeting of the yeast Pom33 nucleoporin depends on karyopherin- and lipid-binding

inferredcites →https://doi.org/10.15252/embj.201592484openalex-snapshot

ESCRTs are everywhere

inferredcites →https://doi.org/10.1534/genetics.115.178939openalex-snapshot

Evidence for a Nonendosomal Function of the Saccharomyces cerevisiae ESCRT-III-Like Protein Chm7

inferredcites →https://doi.org/10.7554/elife.02184openalex-snapshot

Structure of cellular ESCRT-III spirals and their relationship to HIV budding

inferredcites →https://doi.org/10.7554/elife.12548openalex-snapshot

Structural basis for activation, assembly and membrane binding of ESCRT-III Snf7 filaments

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1016/j.cub.2016.07.039openalex-snapshot

Membrane Binding by CHMP7 Coordinates ESCRT-III-Dependent Nuclear Envelope Reformation

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