Allan M. Weissman mainly investigates Cell biology, Biochemistry, Ubiquitin, Ubiquitin ligase and Ubiquitin-conjugating enzyme. The Cell biology study combines topics in areas such as T cell and Lateral inhibition. His work in the fields of Biochemistry, such as Transfection, COS cells and Plant hormone, overlaps with other areas such as Baculoviral IAP repeat-containing protein 3 and Lateral root.
His studies in Ubiquitin integrate themes in fields like Thymocyte, Endoplasmic reticulum, Auxin and Proteasome. As a part of the same scientific study, Allan M. Weissman usually deals with the Ubiquitin ligase, concentrating on Apoptosis and frequently concerns with Mitochondrion and Proteolysis. His Ubiquitin-conjugating enzyme study also includes fields such as
His scientific interests lie mostly in Ubiquitin, Cell biology, Biochemistry, Ubiquitin ligase and Molecular biology. His primary area of study in Ubiquitin is in the field of Ubiquitin-conjugating enzyme. His Cell biology research is multidisciplinary, incorporating perspectives in Receptor and Transmembrane protein.
His Biochemistry study combines topics in areas such as Cell culture and Biophysics. His work on Ubiquitin-Protein Ligases as part of general Ubiquitin ligase study is frequently linked to Proto-Oncogene Proteins c-mdm2, therefore connecting diverse disciplines of science. His studies deal with areas such as Tyrosine phosphorylation, CD8, Gene and T-cell receptor as well as Molecular biology.
His primary scientific interests are in Ubiquitin, Cell biology, Ubiquitin ligase, Biochemistry and Ubiquitin-conjugating enzyme. His Ubiquitin study integrates concerns from other disciplines, such as Saccharomyces cerevisiae, Protein degradation and Proteasome. His study in the field of Endoplasmic reticulum, Mitochondrion and Structural biology is also linked to topics like Quality.
His Ubiquitin ligase research includes elements of Molecular biology and Actin. His research integrates issues of Protein structure, Plasma protein binding and Allosteric regulation in his study of Ubiquitin-conjugating enzyme. He has researched Protein structure in several fields, including Ring finger and Ubiquitin-Protein Ligases.
Allan M. Weissman spends much of his time researching Protein structure, Cell biology, Ubiquitin-conjugating enzyme, Ubiquitin and Ubiquitin ligase. His study in Protein structure is interdisciplinary in nature, drawing from both Ring finger, Protein degradation, Function, Endoplasmic reticulum and Endoplasmic-reticulum-associated protein degradation. His Ring finger research incorporates elements of Structural biology, Ubiquitin-Protein Ligases, Allosteric regulation and RING finger domain.
His Cell biology research includes themes of Binding domain and Biochemistry. His Ubiquitin ligase research incorporates themes from Amino acid, Deubiquitinating enzyme, Protease and Microbiology.
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RING finger proteins: mediators of ubiquitin ligase activity.
Claudio A.P Joazeiro;Allan M Weissman.
RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination
Kevin L. Lorick;Jane P. Jensen;Shengyun Fang;Albert M. Ong.
Proceedings of the National Academy of Sciences of the United States of America (1999)
Mdm2 Is a RING Finger-dependent Ubiquitin Protein Ligase for Itself and p53
Shengyun Fang;Jane P. Jensen;Robert L. Ludwig;Karen H. Vousden.
Journal of Biological Chemistry (2000)
Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli.
Yili Yang;Shengyun Fang;Jane P. Jensen;Allan M. Weissman.
Mind Bomb Is a Ubiquitin Ligase that Is Essential for Efficient Activation of Notch Signaling by Delta
Motoyuki Itoh;Cheol-Hee Kim;Gregory Palardy;Takaya Oda.
Developmental Cell (2003)
Ubiquitin and the control of protein fate in the secretory and endocytic pathways.
Juan S. Bonifacino;Allan M. Weissman.
Annual Review of Cell and Developmental Biology (1998)
HECT and RING finger families of E3 ubiquitin ligases at a glance
Meredith B. Metzger;Ventzislava A. Hristova;Allan M. Weissman.
Journal of Cell Science (2012)
SINAT5 promotes ubiquitin-related degradation of NAC1 to attenuate auxin signals
Qi Xie;Hui-Shan Guo;Geza Dallman;Shengyun Fang.
Antigen activation of murine T cells induces tyrosine phosphorylation of a polypeptide associated with the T cell antigen receptor
Lawrence E. Samelson;Maitray D. Patel;Allan M. Weissman;Joe B. Harford.
The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
Shengyun Fang;Marco Ferrone;Cuihong Yang;Jane P. Jensen.
Proceedings of the National Academy of Sciences of the United States of America (2001)
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