Person
ISNI: 
0000 0000 8164 7076
https://isni.org/isni/0000000081647076
Name: 
Iacobus Rothman
James E. Rothman
James E. Rothman (nobelprisvinner i medisin)
James Edward Rothman
James Rothman (American biologist)
James Rothman (amerikanischer Biochemiker)
James Rothman (biologiste américain)
James Rothman (Biologo statunitense)
James Rothman (biomédico e investigador científico estadounidense)
Rothman, J. E.
Rothman, James
Rothman, James E.
Rothman, James Edward
Джеймс Ротман
Джэймс Ротман
Ротман, Джеймс (американский биолог)
ג'יימס רותמן
جيمس روثمان
جیمز رتھمین
جیمز روثمن
जेम्स रॉथमैन
জেমস ই রথম্যান
ஜேம்ஸ் ரோத்மன்
제임스로스먼
ジェームズ・ロスマン
詹姆斯·罗斯曼
Dates: 
1950-
Creation class: 
article
cre
Language material
txt
Creation role: 
author
editor
redactor
Related names: 
Koninklijke Nederlandse Akademie van Wetenschappen (Amsterdam)
Warren, Graham (1948-)
Warren, Graham (co-author)
Warren, Graham S.
Titles: 
ADP-ribosylation factor and coatomer couple fusion to vesicle budding.
ADP-ribosylation factor and phosphatidic acid levels in Golgi membranes during budding of coatomer-coated vesicles.
ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein.
Alternative zippering as an on-off switch for SNARE-mediated fusion.
amino terminus of ADP-ribosylation factor (ARF) is a critical determinant of ARF activities and is a potent and specific inhibitor of protein transport., The
Anterograde flow of cargo across the golgi stack potentially mediated via bidirectional "percolating" COPI vesicles.
Arrangement of Subunits in 20 S Particles Consisting of NSF, SNAPs, and SNARE Complexes
Asymmetrical distribution of phospholipids in the membrane of Bacillus megaterium.
ATP catalyzes the sequestration of clathrin during enzymatic uncoating.
ATPase core of a clathrin uncoating protein., The
Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway
"BFA bodies": a subcompartment of the endoplasmic reticulum.
Bidirectional transport by distinct populations of COPI-coated vesicles.
Bimodal interaction of coatomer with the p24 family of putative cargo receptors.
Binding of an N-ethylmaleimide-sensitive fusion protein to Golgi membranes requires both a soluble protein(s) and an integral membrane receptor.
binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein., The
Binding of coatomer to Golgi membranes requires ADP-ribosylation factor.
Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses.
Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi.
Brefeldin A, a drug that blocks secretion, prevents the assembly of non-clathrin-coated buds on Golgi cisternae.
Budding from Golgi membranes requires the coatomer complex of non-clathrin coat proteins.
Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin.
capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack., The
Cell-based assays using primary endothelial cells to study multiple steps in inflammation.
Cell biology. An unfolding story of protein translocation.
Characterization of protein transport between successive compartments of the Golgi apparatus: asymmetric properties of donor and acceptor activities in a cell-free system.
Clamping Mechanism Involved in SNARE-Dependent Exocytosis, A
Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors.
Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol.
Coated vesicles transport newly synthesized membrane glycoproteins from endoplasmic reticulum to plasma membrane in two successive stages.
'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles.
Coatomer-rich endoplasmic reticulum.
Compartmental specificity of cellular membrane fusion encoded in SNARE proteins.
Compartmentation of asparagine-linked oligosaccharide processing in the Golgi apparatus.
Complexin activates and clamps SNAREpins by a common mechanism involving an intermediate energetic state.
Complexin cross-links prefusion SNAREs into a zigzag array.
Components responsible for transport between successive Golgi cisternae are highly conserved in evolution.
Concerted Auto-regulation in Yeast Endosomal t-SNAREs
Conformational change of chaperone Hsc70 upon binding to a decapeptide: a circular dichroism study.
conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion., A
Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs.
Countercurrent distribution of two distinct SNARE complexes mediating transport within the Golgi stack.
Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors.
debate about transport in the Golgi--two sides of the same coin?, The
Differential use of endoplasmic reticulum membrane for phagocytosis in J774 macrophages
Dissection of a single round of vesicular transport: sequential intermediates for intercisternal movement in the Golgi stack.
Dissociation of clathrin coats coupled to the hydrolysis of ATP: role of an uncoating ATPase.
Distinct Domains of Complexins Bind SNARE Complexes and Clamp Fusion in Vitro.
Distinct SNARE complexes mediating membrane fusion in Golgi transport based on combinatorial specificity.
Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport.
Dynamic transport of SNARE proteins in the Golgi apparatus.
Early and late functions associated with the Golgi apparatus reside in distinct compartments.
En bloc incorporation of coatomer subunits during the assembly of COP-coated vesicles
Energetics and dynamics of SNAREpin folding across lipid bilayers.
Enzymatic dissociation of clathrin cages in a two-stage process.
Enzymatic recycling of clathrin from coated vesicles.
enzyme that removes clathrin coats: purification of an uncoating ATPase., An
ERS-24, a mammalian v-SNARE implicated in vesicle traffic between the ER and the Golgi.
Exclusion of golgi residents from transport vesicles budding from Golgi cisternae in intact cells.
Fatty acyl-coenzyme A is required for budding of transport vesicles from Golgi cisternae.
Fatty acylation promotes fusion of transport vesicles with Golgi cisternae.
Felix Hoppe-Seyler Lecture 1996. Mechanisms of intracellular protein transport.
Flotillin-1 is essential for PKC-triggered endocytosis and membrane microdomain localization of DAT.
Functional architecture of an intracellular membrane t-SNARE.
Functional mapping of disease susceptibility loci using cell biology
Fusion and protein-mediated phospholipid exchange studied with single bilayer phosphatidylcholine vesicles of different density.
Fusion of cells by flipped SNAREs.
fusion protein required for vesicle-mediated transport in both mammalian cells and yeast., A
future of Golgi research., The
Glucosidase II, a glycoprotein of the endoplasmic reticulum membrane. Proteolytic cleavage into enzymatically active fragments.
glycoprotein that is transported between successive compartments of the Golgi in a cell-free system resides in stacks of cisternae., The
Glycosylation of a membrane protein is restricted to the growing polypeptide chain but is not necessary for insertion as a transmembrane protein.
goldi, The
Golgi apparatus, coated vesicles, and the sorting problem., The
Golgi apparatus: roles for distinct 'cis' and 'trans' compartments., The
golgi apparatus: two organelles in tandem., The
GTP and Methionine Bristles
Hybrid molecules and their use for optically detecting changes in cellular microenvironments
Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles.
i-SNAREs: inhibitory SNAREs that fine-tune the specificity of membrane fusion.
Imaging single membrane fusion events mediated by SNARE proteins.
Implications of the SNARE hypothesis for intracellular membrane topology and dynamics.
Induction of cellular immunity by immunization with novel hybrid peptides complexed to heat shock protein 70
Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes
Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF.
integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding, An
Intercompartmental transport in the Golgi complex is a dissociative process: facile transfer of membrane protein between two Golgi populations.
interview with the Kavli prize winners. Interview by Claudia Wiedemann., An
Intracellular Bacteria Encode Inhibitory SNARE-Like Proteins
Intracellular membrane fusion.
Involvement of GTP-binding "G" proteins in transport through the Golgi stack.
Journeys through the Golgi--taking stock in a new era.
KNAW Heineken lectures 2000
Lasker Basic Medical Research Award. The machinery and principles of vesicle transport in the cell.
Length of the Flexible SNAREp in Juxtamembrane Region Is a Critical Determinant of SNARE-Dependent Fusion, The
length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion., The
Lipidic Antagonists to SNARE-mediated Fusion
Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation
machinery and principles of vesicle transport in the cell, The
Mechanisms of intracellular protein transport.
Megavesicles implicated in the rapid transport of intracisternal aggregates across the Golgi stack.
Membrane assembly in vitro: synthesis, glycosylation, and asymmetric insertion of a transmembrane protein.
Membrane assembly: synthesis and intracellular processing of the vesicular stomatitis viral glycoprotein.
Membrane fusion: grappling with SNARE and SM proteins.
molecular basis of mesomorphic phase transitions in phospholipid systems., The
Molecular machinery mediating vesicle budding, docking and fusion.
Molecular mass, stoichiometry, and assembly of 20 S particles.
Molecular mechanism for the interaction of phospholipid with cholesterol.
Movement of proteins through the Golgi stack: A molecular dissection of vesicular transport.
Multiple cytosolic components promote intra-Golgi protein transport. Resolution of a protein acting at a late stage, prior to membrane fusion.
Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25
multisubunit particle implicated in membrane fusion., A
N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion.
Neurotransmission: harnessing fusion machinery at the synapse.
new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack., A
novel 115-kD peripheral membrane protein is required for intercisternal transport in the Golgi stack., A
novel prefusion complex formed during protein transport between Golgi cisternae in a cell-free system., A
Patterns of synaptic activity in neural networks recorded by light emission from synaptolucins.
Peptide binding and release by proteins implicated as catalysts of protein assembly.
Peptide-binding specificity of the molecular chaperone BiP.
planar organization of lecithin-cholesterol bilayers., The
Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells.
Positive cooperativity in the functioning of molecular chaperone GroEL.
possible docking and fusion particle for synaptic transmission., A
PRIM: proximity imaging of green fluorescent protein-tagged polypeptides.
protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion., A
Protein Determinants of SNARE-Mediated Lipid Mixing
protein machinery of vesicle budding and fusion., The
Protein sorting by selective retention in the endoplasmic reticulum and Golgi stack.
Protein sorting by transport vesicles.
Protein Trafficking in Neurodegenerative Diseases
Proteins involved in vesicular transport and membrane fusion.
Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack.
Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport.
Purification of coated vesicles by agarose gel electrophoresis.
Purification of three related peripheral membrane proteins needed for vesicular transport.
Putative fusogenic activity of NSF is restricted to a lipid mixture whose coalescence is also triggered by other factors
Rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles, A
Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain.
Rapid transmembrane movement of newly synthesized phospholipids during membrane assembly.
rate of bulk flow from the endoplasmic reticulum to the cell surface., The
rate of bulk flow from the Golgi to the plasma membrane., The
Receptor-mediated Uptake of Antigen/Heat Shock Protein Complexes Results in Major Histocompatibility Complex Class I Antigen Presentation via Two Distinct Processing Pathways
reconstitution of intracellular protein transport in cell-free systems., The
Reconstitution of steps in the constitutive secretory pathway in permeabilized cells. Secretion of glycosylated tripeptide and truncated sphingomyelin.
Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine.
Regulation of membrane fusion by the membrane-proximal coil of the t-SNARE during zippering of SNAREpins.
Regulation of protein secretion through controlled aggregation in the endoplasmic reticulum.
Release of clathrin from coated vesicles dependent upon a nucleoside triphosphate and a cytosol fraction.
Removal of Rab GTP-binding proteins from Golgi membranes by GDP dissociation inhibitor inhibits inter-cisternal transport in the Golgi stacks.
resident Golgi protein is excluded from peri-Golgi vesicles in NRK cells, A
Retention of membrane proteins by the endoplasmic reticulum.
role for clathrin light chains in the recognition of clathrin cages by 'uncoating ATPase'., A
role for GTP-binding proteins in vesicular transport through the Golgi complex., A
Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack.
Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments.
Selective activation of cognate SNAREpins by Sec1/Munc18 proteins.
Sequence characteristics of functional siRNAs
Sequential intermediates in the pathway of intercompartmental transport in a cell-free system.
Signal-peptide recognition. GTP and methionine bristles.
SNAP family of NSF attachment proteins includes a brain-specific isoform.
SNAP-mediated protein-protein interactions essential for neurotransmitter release.
SNAP receptors implicated in vesicle targeting and fusion.
SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast.
SNARE required for retrograde transport to the endoplasmic reticulum., A
SNAREpin/Munc18 promotes adhesion and fusion of large vesicles to giant membranes
SNAREpins are functionally resistant to disruption by NSF and alphaSNAP.
SNAREpins: minimal machinery for membrane fusion.
SNAREs can promote complete fusion and hemifusion as alternative outcomes.
Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAP receptor complex in Golgi membranes.
Sorting determinants in the transmembrane domain of p24 proteins.
specificity of SNARE-dependent fusion is encoded in the SNARE motif, The
Stepwise assembly of functionally active transport vesicles.
Synchronised transmembrane insertion and glycosylation of a nascent membrane protein.
t-SNARE of the endocytic pathway must be activated for fusion., A
Throttles and dampers: Controlling the engine of membrane fusion
Topological restriction of SNARE-dependent membrane fusion.
TRANSBILAYER ASYMMETRY AND ITS MAINTENANCE IN BIOLOGICAL MEMBRANES
Transbilayer distribution and movement of cholesterol and phospholipid in the membrane of influenza virus.
Transbilayer phospholipid asymmetry and its maintenance in the membrane of influenza virus.
Transient activity of Golgi-like membranes as donors of vesicular stomatitis viral glycoprotein in vitro.
Transport between Golgi cisternae.
Transport-coupled oligosaccharide processing in a cell-free system.
Transport of newly synthesized vesicular stomatitis viral glycoprotein to purified Golgi membranes.
Transport of protein between cytoplasmic membranes of fused cells: correspondence to processes reconstituted in a cell-free system.
Transport of the membrane glycoprotein of vesicular stomatitis virus to the cell surface in two stages by clathrin-coated vesicles.
Transport of the vesicular stomatitis glycoprotein to trans Golgi membranes in a cell-free system.
Transport of vesicular stomatitis virus glycoprotein in a cell-free extract.
Two classes of binding sites for uncoating protein in clathrin triskelions.
Two distinct populations of ARF bound to Golgi membranes.
Uncoating ATPase is a member of the 70 kilodalton family of stress proteins.
use of pHluorins for optical measurements of presynaptic activity., The
v-SNARE implicated in intra-Golgi transport., A
Vesicle fusion following receptor-mediated endocytosis requires a protein active in Golgi transport.
Vesicles on strings: Morphological evidence for processive transport within the Golgi stack
Vesicular transport between the endoplasmic reticulum and the Golgi stack requires the NEM-sensitive fusion protein.
Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins.
Yeast and mammals utilize similar cytosolic components to drive protein transport through the Golgi complex.
yeast SEC17 gene product is functionally equivalent to mammalian alpha-SNAP protein., The
Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi transport
zeta-COP, a subunit of coatomer, is required for COP-coated vesicle assembly.
Contributed to or performed: 
ADVANCES IN SECOND MESSENGER AND PHOSPHOPROTEIN RESEARCH
BIOLOGICAL CHEMISTRY HOPPE SEYLER
NATURE -LONDON-
NATURE MEDICINE
PROTEIN SCIENCE
Notes: 
Reconstitution of intracellular transport, c1992 t.p. (James E. Rothman)
The Golgi, c2011 ECIP t.p. (James Rothman, Yale University)
The Nobel Prize Web site, July 3, 2019 James E. Rothman Facts (James E. Rothman; Nobel Prize in Physiology or Medicine 2013; b. 3 November 1950, Haverhill, MA; Affiliation at the time of the award: Yale University, New Haven, CT)
Sources: 
VIAF NUKAT SUDOC WKD
NLS
NTA
ZETO