2000 - Member of the National Academy of Sciences
1998 - Fellow of the American Academy of Arts and Sciences
1984 - Fellow of Alfred P. Sloan Foundation
Richard H. Scheller mainly investigates Cell biology, Syntaxin, Synaptic vesicle, Munc-18 and Vesicle fusion. The various areas that Richard H. Scheller examines in his Cell biology study include Exocytosis, SNAP25, Vesicle docking, Synaptic vesicle docking and Membrane protein. His Exocytosis research is multidisciplinary, relying on both Lipid bilayer fusion and Neurotransmission.
Syntaxin is a subfield of Biochemistry that Richard H. Scheller investigates. His work deals with themes such as Amino acid, Molecular biology and Peptide sequence, which intersect with Synaptic vesicle. His Vesicle fusion research is multidisciplinary, incorporating perspectives in Synaptophysin, Soluble NSF attachment protein and Synaptotagmin 1.
The scientist’s investigation covers issues in Cell biology, Biochemistry, Synaptic vesicle, Vesicle and Syntaxin. His Cell biology research incorporates themes from Syntaxin 3, Exocytosis, Munc-18, Vesicle fusion and Membrane protein. He usually deals with Biochemistry and limits it to topics linked to Aplysia and Gene, Neuron, Peptide, Cleavage and Invertebrate hormone.
Richard H. Scheller has included themes like Amino acid, Biophysics, Neurotransmission and Neurotransmitter in his Synaptic vesicle study. His Vesicle study combines topics from a wide range of disciplines, such as Golgi apparatus and Intracellular. Within one scientific family, Richard H. Scheller focuses on topics pertaining to Lipid bilayer fusion under Syntaxin, and may sometimes address concerns connected to R-SNARE Proteins.
Richard H. Scheller focuses on Cell biology, Endosome, Biochemistry, GTPase and Antibody. His studies in Cell biology integrate themes in fields like Vesicle, Exocyst, Vesicle fusion and Membrane protein. His research investigates the connection with Vesicle and areas like Secretion which intersect with concerns in SNAP25 and Kiss-and-run fusion.
His Vesicle fusion study incorporates themes from STX1A, Syntaxin 3, Munc-18, Syntaxin 1 and SNARE complex assembly. His biological study spans a wide range of topics, including Transport protein, Endocytic cycle and Golgi apparatus. His research in Antibody intersects with topics in Cytotoxic T cell, Antigen and Pharmacology, Drug.
Richard H. Scheller mainly focuses on Cell biology, Biochemistry, Conjugate, Membrane protein and Endosome. The Cell biology study combines topics in areas such as Vesicle fusion and Exocyst. His Biochemistry study frequently links to adjacent areas such as Stereochemistry.
The study incorporates disciplines such as Kiss-and-run fusion, Vesicle, Exocytosis, Secretion and SNAP25 in addition to Membrane protein. Richard H. Scheller interconnects Transport protein, Adaptor Signaling Protein and Endocytic cycle, Endocytosis, Clathrin adaptor proteins in the investigation of issues within Endosome. He combines subjects such as Biophysics, Internalization and Endoplasmic reticulum with his study of Endocytosis.
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SNAREs--engines for membrane fusion.
Reinhard Jahn;Richard H. Scheller.
Nature Reviews Molecular Cell Biology (2006)
A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
Thomas Söllner;Mark K. Bennett;Sidney W. Whiteheart;Richard H. Scheller.
Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
L Maroteaux;JT Campanelli;RH Scheller.
The Journal of Neuroscience (1988)
SNARE-mediated membrane fusion.
Yu A. Chen;Richard H. Scheller.
Nature Reviews Molecular Cell Biology (2001)
A Core Complex of BBS Proteins Cooperates with the GTPase Rab8 to Promote Ciliary Membrane Biogenesis
Maxence V. Nachury;Alexander V. Loktev;Qihong Zhang;Christopher J. Westlake.
Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index
Jagath R Junutula;Helga Raab;Suzanna Clark;Sunil Bhakta.
Nature Biotechnology (2008)
Defective Neuromuscular Synaptogenesis in Agrin-Deficient Mutant Mice
Medha Gautam;Peter G Noakes;Lisa Moscoso;Fabio Rupp.
The syntaxin family of vesicular transport receptors
Mark K. Bennett;JoséE. Garcia-Arrarás;Lisa A. Elferink;Karen Peterson.
The molecular machinery for secretion is conserved from yeast to neurons.
Mark K. Bennett;Richard H. Scheller.
Proceedings of the National Academy of Sciences of the United States of America (1993)
Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex.
Kira M. S. Misura;Richard H. Scheller;William I. Weis.
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