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  1. Book ; Thesis: Über den Ursprung des Habsburger Familientypus

    Wendland, Bert

    eine medizin-historische Studie

    1996  

    Author's details von Bert Wendland
    Language German
    Size 142 Bl. : Ill., graph. Darst.
    Edition [Mikrofiche-Ausg.]
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Berlin, Humboldt-Univ., Diss., 1996
    Note Mikrofiche-Ausg.: 3 Mikrofiches : 24x
    HBZ-ID HT007172708
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    1996 MB 1391 order for loan Magazin

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  2. Article: Round-trip ticket: recycling to the plasma membrane requires RME-1.

    Wendland, B

    Nature cell biology

    2001  Volume 3, Issue 6, Page(s) E133–5

    MeSH term(s) Animals ; Calcium-Binding Proteins/chemistry ; Calcium-Binding Proteins/physiology ; Cell Membrane/physiology ; Cells, Cultured ; Phosphoproteins/chemistry ; Phosphoproteins/physiology ; Transport Vesicles/physiology
    Chemical Substances Calcium-Binding Proteins ; Phosphoproteins
    Language English
    Publishing date 2001-06
    Publishing country England
    Document type Comment ; News
    ZDB-ID 1474722-4
    ISSN 1476-4679 ; 1465-7392
    ISSN (online) 1476-4679
    ISSN 1465-7392
    DOI 10.1038/35078592
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: DePFth Perception in Clathrin-Mediated Endocytosis.

    Prosser, Derek C / Wendland, Beverly

    Developmental cell

    2016  Volume 37, Issue 5, Page(s) 387–388

    Abstract: The earliest stages of clathrin-coated structure (CCS) assembly involve the recruitment and stabilization of clathrin-binding adaptor proteins and the clathrin coat. In this issue of Developmental Cell, Ma et al. (2016) now identify transient protein ... ...

    Abstract The earliest stages of clathrin-coated structure (CCS) assembly involve the recruitment and stabilization of clathrin-binding adaptor proteins and the clathrin coat. In this issue of Developmental Cell, Ma et al. (2016) now identify transient protein interactions that form the basis of AP-2 adaptor complex stabilization, key to initiating CCS formation.
    MeSH term(s) Adaptor Protein Complex 2/chemistry ; Adaptor Protein Complex 2/metabolism ; Amino Acid Motifs ; Animals ; Clathrin/metabolism ; Coated Pits, Cell-Membrane/metabolism ; Endocytosis ; Humans ; Models, Biological
    Chemical Substances Adaptor Protein Complex 2 ; Clathrin
    Language English
    Publishing date 2016-06-06
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2016.05.017
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  4. Article ; Online: Novel "thrifty" models of increased eating behaviour.

    Levitan, Robert D / Wendland, Barbara

    Current psychiatry reports

    2013  Volume 15, Issue 11, Page(s) 408

    Abstract: The thrifty genotype and phenotype hypotheses were developed to explain the rapid increase in diabetes and obesity in developed countries around the world. Most subsequent "thrifty" research has focused on the early developmental origins of the metabolic ...

    Abstract The thrifty genotype and phenotype hypotheses were developed to explain the rapid increase in diabetes and obesity in developed countries around the world. Most subsequent "thrifty" research has focused on the early developmental origins of the metabolic syndrome and cardio-metabolic disease. The goal of this manuscript is to review an emerging line of research that uses a similar thrifty framework to understand the early developmental origins of eating-related phenotypes that have primary relevance to many psychiatric disorders. Given the important role of environmental adversity in various psychiatric disorders that involve overeating, and their early age of onset, it is likely that several thrifty mechanisms are relevant in this regard. Understanding the early origins of increased eating behaviour based on a thrifty model might point the way to highly targeted preventative interventions during critical periods of development, and provide a new way of addressing these common and difficult to treat disorders.
    MeSH term(s) Adaptation, Physiological ; Biological Evolution ; Energy Metabolism/genetics ; Energy Metabolism/physiology ; Feeding Behavior/physiology ; Gene-Environment Interaction ; Genotype ; Humans ; Obesity/genetics ; Obesity/physiopathology ; Phenotype ; Selection, Genetic
    Language English
    Publishing date 2013-09-22
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2055376-6
    ISSN 1535-1645 ; 1523-3812
    ISSN (online) 1535-1645
    ISSN 1523-3812
    DOI 10.1007/s11920-013-0408-x
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  5. Article: Epsins: adaptors in endocytosis?

    Wendland, Beverly

    Nature reviews. Molecular cell biology

    2002  Volume 3, Issue 12, Page(s) 971–977

    Abstract: Endocytic adaptor proteins select specific cargo for internalization by endocytosis through clathrin-coated pits or vesicles. Recent studies indicate that epsins might also be classified as adaptors. ...

    Abstract Endocytic adaptor proteins select specific cargo for internalization by endocytosis through clathrin-coated pits or vesicles. Recent studies indicate that epsins might also be classified as adaptors.
    MeSH term(s) Adaptor Proteins, Vesicular Transport/metabolism ; Animals ; Binding Sites ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Nucleus/metabolism ; Clathrin/metabolism ; Endocytosis/physiology ; Models, Biological ; Neuropeptides/genetics ; Neuropeptides/metabolism ; Protein Structure, Tertiary ; Receptors, Cell Surface/metabolism ; Ubiquitin/metabolism ; Vesicular Transport Proteins ; Yeasts/physiology
    Chemical Substances Adaptor Proteins, Vesicular Transport ; Carrier Proteins ; Clathrin ; Neuropeptides ; Receptors, Cell Surface ; Ubiquitin ; Vesicular Transport Proteins ; epsin
    Language English
    Publishing date 2002
    Publishing country England
    Document type Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/nrm970
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  6. Article ; Online: Conserved roles for yeast Rho1 and mammalian RhoA GTPases in clathrin-independent endocytosis.

    Prosser, Derek C / Wendland, Beverly

    Small GTPases

    2012  Volume 3, Issue 4, Page(s) 229–235

    Abstract: Eukaryotic cells use numerous endocytic pathways for nutrient uptake, protein turnover and response to the extracellular environment. While clathrin-mediated endocytosis (CME) has been extensively studied in yeast and mammalian cells, recent studies in ... ...

    Abstract Eukaryotic cells use numerous endocytic pathways for nutrient uptake, protein turnover and response to the extracellular environment. While clathrin-mediated endocytosis (CME) has been extensively studied in yeast and mammalian cells, recent studies in higher eukaryotes have described multiple clathrin-independent endocytic pathways that depend upon Rho family GTPases and their effector proteins. In contrast, yeast cells have been thought to rely solely on CME. In a recent study, we used CME-defective yeast cells lacking clathrin-binding endocytic adaptor proteins in a genetic screen to identify novel factors involved in endocytosis. This approach revealed the existence of a clathrin-independent endocytic pathway involving the GTPase Rho1, which is the yeast homolog of RhoA. Further characterization of the yeast Rho1-mediated endocytic pathway suggested that the Rho1 pathway requires additional proteins that appear to play conserved roles in RhoA-dependent, clathrin-independent endocytic pathways in mammalian cells. Here, we discuss the parallels between the yeast Rho1-dependent and mammalian RhoA-dependent endocytic pathways, as well as the applications of yeast as a model for studying clathrin-independent endocytosis in higher eukaryotes.
    MeSH term(s) Animals ; Clathrin/physiology ; Endocytosis/physiology ; Fungal Proteins/physiology ; Humans ; Yeasts/physiology ; rhoA GTP-Binding Protein/physiology
    Chemical Substances Clathrin ; Fungal Proteins ; rhoA GTP-Binding Protein (EC 3.6.5.2)
    Language English
    Publishing date 2012-12-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2682247-7
    ISSN 2154-1256 ; 2154-1248
    ISSN (online) 2154-1256
    ISSN 2154-1248
    DOI 10.4161/sgtp.21631
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  7. Article ; Online: Actin and endocytosis in budding yeast.

    Goode, Bruce L / Eskin, Julian A / Wendland, Beverly

    Genetics

    2015  Volume 199, Issue 2, Page(s) 315–358

    Abstract: Endocytosis, the process whereby the plasma membrane invaginates to form vesicles, is essential for bringing many substances into the cell and for membrane turnover. The mechanism driving clathrin-mediated endocytosis (CME) involves > 50 different ... ...

    Abstract Endocytosis, the process whereby the plasma membrane invaginates to form vesicles, is essential for bringing many substances into the cell and for membrane turnover. The mechanism driving clathrin-mediated endocytosis (CME) involves > 50 different protein components assembling at a single location on the plasma membrane in a temporally ordered and hierarchal pathway. These proteins perform precisely choreographed steps that promote receptor recognition and clustering, membrane remodeling, and force-generating actin-filament assembly and turnover to drive membrane invagination and vesicle scission. Many critical aspects of the CME mechanism are conserved from yeast to mammals and were first elucidated in yeast, demonstrating that it is a powerful system for studying endocytosis. In this review, we describe our current mechanistic understanding of each step in the process of yeast CME, and the essential roles played by actin polymerization at these sites, while providing a historical perspective of how the landscape has changed since the preceding version of the YeastBook was published 17 years ago (1997). Finally, we discuss the key unresolved issues and where future studies might be headed.
    MeSH term(s) Actin Cytoskeleton/metabolism ; Actins/metabolism ; Biological Transport ; Cell Membrane/metabolism ; Clathrin/metabolism ; Endocytosis ; Saccharomycetales/physiology ; Transport Vesicles/metabolism
    Chemical Substances Actins ; Clathrin
    Language English
    Publishing date 2015-02
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2167-2
    ISSN 1943-2631 ; 0016-6731
    ISSN (online) 1943-2631
    ISSN 0016-6731
    DOI 10.1534/genetics.112.145540
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  8. Article ; Online: Pan1 regulates transitions between stages of clathrin-mediated endocytosis.

    Bradford, Mary Katherine / Whitworth, Karen / Wendland, Beverly

    Molecular biology of the cell

    2015  Volume 26, Issue 7, Page(s) 1371–1385

    Abstract: Endocytosis is a well-conserved process by which cells invaginate small portions of the plasma membrane to create vesicles containing extracellular and transmembrane cargo proteins. Dozens of proteins and hundreds of specific binding interactions are ... ...

    Abstract Endocytosis is a well-conserved process by which cells invaginate small portions of the plasma membrane to create vesicles containing extracellular and transmembrane cargo proteins. Dozens of proteins and hundreds of specific binding interactions are needed to coordinate and regulate these events. Saccharomyces cerevisiae is a powerful model system with which to study clathrin-mediated endocytosis (CME). Pan1 is believed to be a scaffolding protein due to its interactions with numerous proteins that act throughout the endocytic process. Previous research characterized many Pan1 binding interactions, but due to Pan1's essential nature, the exact mechanisms of Pan1's function in endocytosis have been difficult to define. We created a novel Pan1-degron allele, Pan1-AID, in which Pan1 can be specifically and efficiently degraded in <1 h upon addition of the plant hormone auxin. The loss of Pan1 caused a delay in endocytic progression and weakened connections between the coat/actin machinery and the membrane, leading to arrest in CME. In addition, we determined a critical role for the central region of Pan1 in endocytosis and viability. The regions important for endocytosis and viability can be separated, suggesting that Pan1 may have a distinct role in the cell that is essential for viability.
    MeSH term(s) Amino Acid Motifs ; Clathrin/metabolism ; Endocytosis/physiology ; Microfilament Proteins/metabolism ; Microfilament Proteins/physiology ; Protein Binding ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae Proteins/metabolism ; Saccharomyces cerevisiae Proteins/physiology
    Chemical Substances Clathrin ; Microfilament Proteins ; PAN1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2015-04-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E14-11-1510
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  9. Article ; Online: Endocytic adaptors--social networking at the plasma membrane.

    Reider, Amanda / Wendland, Beverly

    Journal of cell science

    2011  Volume 124, Issue Pt 10, Page(s) 1613–1622

    Abstract: Receptor-mediated endocytosis is a dynamic process that is crucial for maintaining plasma membrane composition and controlling cell-signaling pathways. A variety of entry routes have evolved to ensure that the vast array of molecules on the cell surface ... ...

    Abstract Receptor-mediated endocytosis is a dynamic process that is crucial for maintaining plasma membrane composition and controlling cell-signaling pathways. A variety of entry routes have evolved to ensure that the vast array of molecules on the cell surface can be differentially internalized by endocytosis. This diversity has extended to include a growing list of endocytic adaptor proteins, which are thought to initiate the internalization process. The key function of adaptors is to select the proteins that should be removed from the cell surface. Thus, they have a central role in defining the physiology of a cell. This has made the study of adaptor proteins a very active area of research that is ripe for exciting future discoveries. Here, we review recent work on how adaptors mediate endocytosis and address the following questions: what characteristics define an endocytic adaptor protein? What roles do these proteins fulfill in addition to selecting cargo and how might adaptors function in clathrin-independent endocytic pathways? Through the findings discussed in this Commentary, we hope to stimulate further characterization of known adaptors and expansion of the known repertoire by identification of new adaptors.
    MeSH term(s) Adaptor Proteins, Vesicular Transport/metabolism ; Adaptor Proteins, Vesicular Transport/physiology ; Cell Membrane/metabolism ; Clathrin/metabolism ; Clathrin/physiology ; Endocytosis/physiology ; Humans
    Chemical Substances Adaptor Proteins, Vesicular Transport ; Clathrin
    Language English
    Publishing date 2011-05-02
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.073395
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    Zs.MG 14: Show issues

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  10. Article ; Online: Cell biology: How to don a coat.

    Traub, Linton M / Wendland, Beverly

    Nature

    2010  Volume 465, Issue 7298, Page(s) 556–557

    MeSH term(s) Adaptor Protein Complex 2/metabolism ; Carrier Proteins/metabolism ; Cell Membrane/metabolism ; Clathrin-Coated Vesicles/metabolism ; Endocytosis ; Fatty Acid-Binding Proteins ; Humans ; Membrane Proteins ; Proteins/chemistry ; Proteins/genetics ; Proteins/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Adaptor Protein Complex 2 ; Carrier Proteins ; FCHO1 protein, human ; FCHO2 protein, human ; Fatty Acid-Binding Proteins ; Membrane Proteins ; Proteins ; Saccharomyces cerevisiae Proteins ; Syp1 protein, S cerevisiae
    Language English
    Publishing date 2010-06-03
    Publishing country England
    Document type News
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/465556a
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    Zs.MG 9: Show issues
    Zs.MO 244: Show issues

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