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1. Full Text NS2 protein of hepatitis C virus interacts with structural and non-structural proteins towards virus assembly
by Popescu, Costin-Ioan and Callens, Nathalie and Trinel, Dave and Roingeard, Philippe and Moradpour, Darius and Descamps, Véronique and Duverlie, Gilles and Penin, François and Héliot, Laurent and Rouillé, Yves and Dubuisson, Jean
PLoS Pathogens, ISSN 1553-7366, 2011, Volume 7, Issue 2, p. e1001278
Growing experimental evidence indicates that, in addition to the physical virion components, the non-structural proteins of hepatitis C virus (HCV) are... 
VIRAL-RNA REPLICATION | INSERTION SCANNING MUTAGENESIS | P7 PROTEIN | SUBCELLULAR-LOCALIZATION | MEMBRANE-PROTEIN | MICROBIOLOGY | SEMLIKI-FOREST-VIRUS | CORE PROTEIN | VIROLOGY | INFECTIOUS VIRUS | ENVELOPE GLYCOPROTEINS | CELL-CULTURE | PARASITOLOGY | Amino Acid Sequence | Protein Interaction Domains and Motifs - physiology | Humans | Cells, Cultured | Hepacivirus - genetics | Models, Molecular | Molecular Sequence Data | Viral Nonstructural Proteins - genetics | Viral Proteins - genetics | Virus Assembly - physiology | Viral Proteins - metabolism | Hepacivirus - metabolism | Tissue Distribution | Viral Nonstructural Proteins - chemistry | Models, Biological | Protein Interaction Domains and Motifs - genetics | Virus Assembly - genetics | Viral Envelope Proteins - chemistry | Viral Core Proteins - metabolism | Viral Envelope Proteins - metabolism | Protein Binding | Hepacivirus - physiology | Viral Nonstructural Proteins - metabolism | Physiological aspects | Research | RNA | Viral proteins | Hepatitis C virus | Health aspects | Proteins | Hepatitis | Cell culture | Lipids | Genomes
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2. Full Text Long Unfolded Linkers Facilitate Membrane Protein Import Through the Nuclear Pore Complex
by Anne C. Meinema and Justyna K. Laba and Rizqiya A. Hapsari and Renee Otten and Frans A. A. Mulder and Annemarie Kralt and Geert van den Bogaart and C. Patrick Lusk and Bert Poolman and Liesbeth M. Veenhoff
Science, ISSN 0036-8075, 7/2011, Volume 333, Issue 6038, pp. 90 - 93
Active nuclear import of soluble cargo involves transport factors that shuttle cargo through the nuclear pore complex (NPC) by binding to phenylalanine-glycine... 
Proteins | Nuclear pore | Microscopy | REPORTS | Nuclear membrane | Fluorescence | Amino acids | Imports | Scaffolds | Freight | Membrane proteins | ARCHITECTURE | TRANSPORT | DOMAIN | MULTIDISCIPLINARY SCIENCES | INTRACELLULAR TRAFFICKING | Nuclear Pore Complex Proteins - chemistry | Endoplasmic Reticulum - metabolism | Molecular Sequence Data | Recombinant Fusion Proteins - metabolism | Nuclear Pore Complex Proteins - genetics | Saccharomyces cerevisiae - metabolism | Membrane Proteins - metabolism | Active Transport, Cell Nucleus | Nuclear Proteins - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Membrane Proteins - genetics | Nuclear Pore Complex Proteins - metabolism | Karyopherins - chemistry | Nuclear Proteins - metabolism | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Nuclear Localization Signals | Nuclear Pore - metabolism | Nuclear Proteins - chemistry | Protein Folding | Nuclear Envelope - metabolism | Karyopherins - metabolism | Membrane Proteins - chemistry | Models, Biological | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Physiological aspects | Genetic aspects | Research | Phenylalanine | Protein binding
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3. Nuclear envelope dynamics in embryos and somatic cells
2002, ISBN 0306474395, 174
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4. Membrane trafficking in viral replication
by Marsh, Mark
2005, 1. Aufl., Current topics in microbiology and immunology, ISBN 3540214305, Volume 285., vi, 259
This CTMI volume deals with specific aspects of viral interactions with cellular membranes and includes chapters on viral entry, viral membrane fusion, viral... 
Viruses | Viral envelopes | Reproduction | Biological transport | Biomedicine | Virology
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5. Full Text A mammalian KASH domain protein coupling meiotic chromosomes to the cytoskeleton
by Horn, Henning F and Kim, Dae In and Wright, Graham D and Wong, Esther Sook Miin and Stewart, Colin L and Burke, Brian and Roux, Kyle J
Journal of Cell Biology, ISSN 0021-9525, 2013, Volume 202, Issue 7, pp. 1023 - 1039
Chromosome pairing is an essential meiotic event that ensures faithful haploidization and recombination of the genome. Pairing of homologous chromosomes is... 
STRUCTURED ILLUMINATION | FISSION YEAST | ZEBRAFISH ZYGOTE | LINC COMPLEX | SPINDLE POLE BODY | ENVELOPE | ACTIN CYTOSKELETON | NUCLEAR-MEMBRANE PROTEIN | C. ELEGANS | BOUQUET FORMATION | CELL BIOLOGY | Meiosis - physiology | RNA, Small Interfering - genetics | Spermatocytes - metabolism | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Molecular Sequence Data | Male | Immunoenzyme Techniques | Cell Cycle Proteins - antagonists & inhibitors | Telomere-Binding Proteins - genetics | Microtubules - metabolism | Cell Nucleus - metabolism | HEK293 Cells | Cell Cycle Proteins - genetics | Female | Membrane Proteins - metabolism | Nuclear Proteins - genetics | Telomere-Binding Proteins - metabolism | Real-Time Polymerase Chain Reaction | Cytoplasmic Dyneins - metabolism | Telomere - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Membrane Proteins - genetics | RNA, Messenger - genetics | Cell Cycle Proteins - metabolism | Cells, Cultured | Cytoplasmic Dyneins - genetics | In Situ Hybridization, Fluorescence | Nuclear Proteins - metabolism | Microtubule-Associated Proteins - antagonists & inhibitors | Reverse Transcriptase Polymerase Chain Reaction | Telomere-Binding Proteins - antagonists & inhibitors | Blotting, Western | Sequence Homology, Amino Acid | Nuclear Envelope - metabolism | Animals | Cell Nucleus - genetics | Membrane Proteins - antagonists & inhibitors | Nuclear Proteins - antagonists & inhibitors | Cytoskeleton - metabolism | Spermatocytes - cytology | Mice | HeLa Cells | Chromosome Pairing | Chromosomes | Analysis | Dynein | Protein binding
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6. Full Text Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
by Sklar, Joseph G and Wu, Tao and Kahne, Daniel and Silhavy, Thomas J
Genes and Development, ISSN 0890-9369, 10/2007, Volume 21, Issue 19, pp. 2473 - 2484
Integral beta-barrel proteins (OMPs) are a major class of outer membrane proteins in Gram-negative bacteria. In Escherichia coli, these proteins are... 
Periplasmic chaperones | Membrane biogenesis | Outer membrane proteins | HIGH-TEMPERATURE | EXPORT | outer membrane proteins | DEVELOPMENTAL BIOLOGY | periplasmic chaperones | membrane biogenesis | YAET COMPLEX | CELL BIOLOGY | OUTER-MEMBRANE PROTEINS | ENVELOPE-STRESS-RESPONSE | GRAM-NEGATIVE BACTERIA | BIOGENESIS | CELL-ENVELOPE | GENETICS & HEREDITY | GENE-EXPRESSION | SIGMA-FACTOR | Receptors, Virus - metabolism | Peptidylprolyl Isomerase - physiology | Porins - metabolism | Serine Endopeptidases - physiology | Bacterial Outer Membrane Proteins - analysis | Periplasmic Proteins - physiology | Escherichia coli Proteins - physiology | Porins - analysis | Heat-Shock Proteins - genetics | Periplasmic Proteins - genetics | Escherichia coli - metabolism | Serine Endopeptidases - genetics | Peptidylprolyl Isomerase - genetics | Escherichia coli Proteins - analysis | Carrier Proteins - physiology | DNA-Binding Proteins - physiology | Molecular Chaperones - genetics | Escherichia coli Proteins - metabolism | Receptors, Virus - analysis | DNA-Binding Proteins - genetics | Molecular Chaperones - physiology | Protein Folding | Carrier Proteins - genetics | Bacterial Outer Membrane Proteins - metabolism | Escherichia coli Proteins - genetics | Heat-Shock Proteins - physiology | Research Paper
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7. Full Text Viral proteins function as ion channels
by Wang, Kai and Xie, Shiqi and Sun, Bing
BBA - Biomembranes, ISSN 0005-2736, 2011, Volume 1808, Issue 2, pp. 510 - 515
Viral ion channels are short membrane proteins with 50–120 amino acids and play an important role either in regulating virus replication, such as virus entry,... 
Viral ion channels | HIV-1 | Picornavirus | Coronavirus | Influenza | HCV | PBCV-1 | COXSACKIEVIRUS 2B PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | HEPATITIS-C-VIRUS | M2 PROTEIN | ESCHERICHIA-COLI-CELLS | BIOPHYSICS | INFLUENZA-A VIRUS | CORONAVIRUS ENVELOPE PROTEIN | MODULATING CYCLOPHILIN LIGAND | VPU PROTEIN | M-2 PROTON CHANNEL | INTEGRAL MEMBRANE GLYCOPROTEIN | Viral Matrix Proteins - genetics | Humans | Ion Channels - genetics | Ion Channels - drug effects | Viral Proteins - metabolism | Potassium Channels - metabolism | Viral Nonstructural Proteins - chemistry | Human Immunodeficiency Virus Proteins - chemistry | Viral Envelope Proteins - metabolism | Viral Matrix Proteins - metabolism | Viral Proteins - drug effects | Ion Channels - chemistry | Antiviral Agents - pharmacology | Viral Envelope Proteins - genetics | Viral Proteins - chemistry | Viral Regulatory and Accessory Proteins - genetics | Viral Nonstructural Proteins - genetics | Viral Proteins - genetics | Viral Regulatory and Accessory Proteins - metabolism | Potassium Channels - genetics | Host-Pathogen Interactions | Human Immunodeficiency Virus Proteins - metabolism | Animals | Ion Channels - metabolism | Viral Matrix Proteins - chemistry | Viral Envelope Proteins - chemistry | Human Immunodeficiency Virus Proteins - genetics | Potassium Channels - chemistry | Viral Nonstructural Proteins - metabolism | Viral Regulatory and Accessory Proteins - chemistry | Virus diseases | Ion channels | Viral proteins | Hepatitis C virus | Membrane proteins
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8. Full Text MAJIN Links Telomeric DNA to the Nuclear Membrane by Exchanging Telomere Cap
by Shibuya, Hiroki and Hernández-Hernández, Abrahan and Morimoto, Akihiro and Negishi, Lumi and Höög, Christer and Watanabe, Yoshinori
Cell, ISSN 0092-8674, 11/2015, Volume 163, Issue 5, pp. 1252 - 1266
In meiosis, telomeres attach to the inner nuclear membrane (INM) and drive the chromosome movement required for homolog pairing and recombination. Here, we... 
ATTACHMENT | MAMMALIAN TELOMERES | DOMAIN PROTEIN MPS3 | MEIOTIC CHROMOSOME DYNAMICS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENVELOPE | MEIOSIS | PROPHASE | SYNAPTONEMAL COMPLEX | BOUQUET FORMATION | ANCHOR TELOMERES | CELL BIOLOGY | Testis - metabolism | Microtubule-Associated Proteins - genetics | Humans | Molecular Sequence Data | Male | Telomere-Binding Proteins - genetics | Cell Cycle Proteins - genetics | Membrane Proteins - metabolism | Telomere - metabolism | Telomere-Binding Proteins - metabolism | Amino Acid Sequence | Membrane Proteins - genetics | Apoptosis Regulatory Proteins - chemistry | Mice, Inbred C57BL | Cell Cycle Proteins - metabolism | Nuclear Proteins - metabolism | Meiosis | Nuclear Proteins - chemistry | Apoptosis Regulatory Proteins - metabolism | Carrier Proteins - genetics | Nuclear Envelope - metabolism | Sequence Alignment | Animals | Carrier Proteins - metabolism | Membrane Proteins - chemistry | Mice | Telomere-Binding Proteins - chemistry | Proteins | Molecular biology | Chromosomes | DNA
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9. Full Text Quantitative Brightness Analysis of Protein Oligomerization in the Nuclear Envelope
by Hennen, Jared and Hur, Kwang-Ho and Saunders, Cosmo A and Luxton, G. W. Gant and Mueller, Joachim D
Biophysical Journal, ISSN 0006-3495, 07/2017, Volume 113, Issue 1, pp. 138 - 147
Brightness analysis of fluorescence fluctuation experiments has been used to successfully measure the oligomeric state of proteins at the plasma membrane, in... 
BIOPHYSICS | CUMULANT ANALYSIS | LINC COMPLEX | FORM | FLUORESCENCE FLUCTUATION SPECTROSCOPY | DISEASE | MEMBRANES | BINDING | LIVING CELLS | Spectrometry, Fluorescence - methods | Humans | Dermoscopy | Green Fluorescent Proteins - genetics | Intracellular Signaling Peptides and Proteins - metabolism | Transfection | Water - chemistry | Protein Domains | Membrane Proteins - metabolism | Microfilament Proteins - metabolism | Diffusion | Nuclear Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Microfilament Proteins - genetics | Green Fluorescent Proteins - metabolism | Membrane Proteins - genetics | Bacterial Proteins - genetics | Polymerization | Molecular Imaging - methods | Nuclear Proteins - metabolism | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Nuclear Envelope - metabolism | Algorithms | Cell Line, Tumor | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | Luminescent Proteins - metabolism | Oligomers | Fluorescence | Analysis | Cells | Biomedical engineering | Membrane proteins | Cell Biophysics
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10. Full Text Structure and immune recognition of trimeric pre-fusion HIV-1 Env
by Pancera, Marie and Pancera, Marie and Zhou, Tongqing and Zhou, Tongqing and Druz, Aliaksandr and Druz, Aliaksandr and Georgiev, Ivelin S and Georgiev, Ivelin S and Soto, Cinque and Soto, Cinque and Gorman, Jason and Gorman, Jason and Huang, Jinghe and Huang, Jinghe and Acharya, Priyamvada and Acharya, Priyamvada and Chuang, Gwo-Yu and Chuang, Gwo-Yu and Ofek, Gilad and Ofek, Gilad and Stewart-Jones, Guillaume B. E and Stewart-Jones, Guillaume B.E and Stuckey, Jonathan and Stuckey, Jonathan and Bailer, Robert T and Bailer, Robert T and Joyce, M. Gordon and Joyce, M Gordon and Louder, Mark K and Louder, Mark K and Tumba, Nancy and Tumba, Nancy and Yang, Yongping and Yang, Yongping and Zhang, Baoshan and Zhang, Baoshan and Cohen, Myron S and Cohen, Myron S and Haynes, Barton F and Haynes, Barton F and Mascola, John R and Mascola, John R and Morris, Lynn and Morris, Lynn and Munro, James B and Munro, James B and Blanchard, Scott C and Blanchard, Scott C and Mothes, Walther and Mothes, Walther and Connors, Mark and Connors, Mark and Kwong, Peter D and Kwong, Peter D and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature, ISSN 0028-0836, 10/2014, Volume 514, Issue 7253, pp. 455 - 461
The human immunodeficiency virus type 1 (HIV-1) envelope (Env) spike, comprising three gp120 and three gp41 subunits, is a conformational machine that... 
ENVELOPE GLYCOPROTEIN TRIMERS | B-CELL RESPONSES | POTENT NEUTRALIZATION | NEUTRALIZING ANTIBODY | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | IMMUNODEFICIENCY-VIRUS TYPE-1 | INFLUENZA-VIRUS | CORE STRUCTURE | DEPENDENT EPITOPE | EBOLA-VIRUS | HIV Envelope Protein gp120 - genetics | HIV Envelope Protein gp41 - genetics | Protein Subunits - immunology | HIV Envelope Protein gp41 - immunology | Humans | Protein Multimerization | AIDS Vaccines - immunology | Molecular Sequence Data | Crystallography, X-Ray | HIV Envelope Protein gp41 - chemistry | Virus Internalization | Genetic Variation | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | Antibodies, Neutralizing - immunology | HIV Antibodies - immunology | Protein Structure, Quaternary | Polysaccharides - chemistry | HIV Envelope Protein gp120 - chemistry | Protein Subunits - genetics | Amino Acid Sequence | Membrane Fusion | Models, Molecular | Glycosylation | Polysaccharides - immunology | AIDS Vaccines - chemistry | Immune Evasion | Protein Subunits - chemistry | Structural Homology, Protein | Cohort Studies | Physiological aspects | HIV antibodies | Viral proteins | Structure | Health aspects | Infections | Immunology | Peptides | Human immunodeficiency virus--HIV | Crystals | X-ray crystallography | HIV infections | Protein function predictions | Protein vaccines | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES
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11. Full Text The Ancient Gamete Fusogen HAP2 Is a Eukaryotic Class II Fusion Protein
by Fédry, Juliette and Liu, Yanjie and Péhau-Arnaudet, Gérard and Pei, Jimin and Li, Wenhao and Tortorici, M. Alejandra and Traincard, François and Meola, Annalisa and Bricogne, Gérard and Grishin, Nick V and Snell, William J and Rey, Félix A and Krey, Thomas
Cell, ISSN 0092-8674, 02/2017, Volume 168, Issue 5, pp. 904 - 915.e10
Sexual reproduction is almost universal in eukaryotic life and involves the fusion of male and female haploid gametes into a diploid cell. The sperm-restricted... 
Chlamydomonas reinhardtii | gamete fusion | crystal structure | sexual reproduction | virus entry | HAP2 | transmission-blocking malaria vaccine | lipid insertion | class II fusion protein | membrane fusion | SEXUAL REPRODUCTION | VIRUS ENVELOPE PROTEIN | FERTILIZATION | GENE | CRYSTAL-STRUCTURE | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEMLIKI-FOREST-VIRUS | GLYCOPROTEIN | GCS1 | CHLAMYDOMONAS | CELL BIOLOGY | Membrane Fusion Proteins - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Plasmodium - metabolism | Plasmodium - cytology | Recombinant Proteins - chemistry | Crystallography, X-Ray | Recombinant Proteins - genetics | Chlamydomonas - metabolism | Protozoan Proteins - genetics | Membrane Fusion Proteins - metabolism | Biological Evolution | Plant Proteins - genetics | Sequence Alignment | Protozoan Proteins - metabolism | Membrane Fusion Proteins - genetics | Plant Proteins - chemistry | Chlamydomonas - cytology | Germ Cells - chemistry | Protein Domains | Protozoan Proteins - chemistry | Plant Proteins - metabolism | Germ Cells - metabolism | Proteins | Viral antibodies | Antibodies | Plants | Cells | Malaria | Malaria vaccine | Crystals | Structure
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12. Full Text KASH protein Syne-2/Nesprin-2 and SUN proteins SUN1/2 mediate nuclear migration during mammalian retinal development
by Yu, Juehua and Lei, Kai and Zhou, Min and Craft, Cheryl M and Xu, Gezhi and Xu, Tian and Zhuang, Yuan and Xu, Rener and Han, Min
Human Molecular Genetics, ISSN 0964-6906, 03/2011, Volume 20, Issue 6, pp. 1061 - 1073
Nuclear movement relative to cell bodies is a fundamental process during certain aspects of mammalian retinal development. During the generation of... 
NEURONAL MIGRATION | CELLS | CONE PHOTORECEPTORS | EMBRYONIC MOUSE RETINA | BIOCHEMISTRY & MOLECULAR BIOLOGY | MEMBRANE PROTEIN | ENVELOPE | GENETICS & HEREDITY | MICE | ACTIN CYTOSKELETON | DIFFERENTIATION | DROSOPHILA EYE | Microtubule-Associated Proteins - chemistry | Retina - metabolism | Retina - growth & development | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Male | Telomere-Binding Proteins - genetics | Nerve Tissue Proteins - chemistry | Cell Nucleus - metabolism | Retina - cytology | Female | Membrane Proteins - metabolism | Nuclear Proteins - genetics | Telomere-Binding Proteins - metabolism | Protein Structure, Tertiary | Photoreceptor Cells - cytology | Membrane Proteins - genetics | Mice, Inbred C57BL | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Nerve Tissue Proteins - genetics | Retina - chemistry | Mice, Knockout | Nerve Tissue Proteins - metabolism | Animals | Membrane Proteins - chemistry | Photoreceptor Cells - metabolism | Mice | Telomere-Binding Proteins - chemistry | Cell Movement
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