James E. Rothman

ORCID: 0000-0003-4822-4161
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Cellular transport and secretion
  • Lipid Membrane Structure and Behavior
  • Endoplasmic Reticulum Stress and Disease
  • Retinal Development and Disorders
  • Biotin and Related Studies
  • Neuroscience and Neuropharmacology Research
  • Pancreatic function and diabetes
  • Erythrocyte Function and Pathophysiology
  • Biochemical and Structural Characterization
  • Advanced Fluorescence Microscopy Techniques
  • Heat shock proteins research
  • Photosynthetic Processes and Mechanisms
  • Calcium signaling and nucleotide metabolism
  • Glycosylation and Glycoproteins Research
  • Protein Structure and Dynamics
  • Microtubule and mitosis dynamics
  • Lysosomal Storage Disorders Research
  • Advanced Electron Microscopy Techniques and Applications
  • Fungal and yeast genetics research
  • Photoreceptor and optogenetics research
  • Supramolecular Self-Assembly in Materials
  • RNA and protein synthesis mechanisms
  • Advanced biosensing and bioanalysis techniques
  • RNA Interference and Gene Delivery
  • Toxin Mechanisms and Immunotoxins

Yale University
2016-2025

Heidelberg (Poland)
2020-2023

Dr Gray's Hospital
2023

La Jolla Alcohol Research
2018-2023

FC Barcelona
2023

Roth and Rau (Germany)
1992-2019

University College London
2017-2018

National Hospital for Neurology and Neurosurgery
2018

Edwards (United Kingdom)
2018

University of New Haven
2011

Two members of the hsp70 family, termed hsc70 and BiP, have been implicated in promoting protein folding assembly processes cytoplasm lumen endoplasmic reticulum, respectively. Short hydrophilic (8 to 25 residues) synthetic peptides now tested as possible mimics polypeptide chain substrates help define an enzymatic basis for these activities. Both BiP specific peptide binding sites. Peptide elicits hydrolysis adenosine triphosphate, with subsequent release bound peptide.

10.1126/science.2756425 article EN Science 1989-07-28

Three new and likely related components of the cellular fusion machinery have been purified from bovine brain cytosol, termed α-SNAP (35 kd), β-SNAP (36 γ-SNAP (39 kd). Transport between cisternae Golgi complex measured in vitro requires SNAP activity during membrane stage, each is capable binding general protein NSF to membranes. The SNAP-NSF-membrane may be an early stage assembly a proposed multisubunit "fusion machine" on target membrane. transport factor also found yeast. Yeast cytosol...

10.1016/0092-8674(90)90482-t article EN cc-by-nc-nd Cell 1990-05-01

N-Ethylmaleimide (NEM) inhibits protein transport between successive compartments of the Golgi stack in a cell-free system. After inactivation membranes by NEM, can be rescued adding back an appropriately prepared cytosol fraction. This complementation assay has allowed us to purify NEM-sensitive factor, which we term NSF. The factor is tetramer 76-kDa subunits, and appears act catalytically, one leading metabolism numerous vesicles.

10.1073/pnas.85.21.7852 article EN Proceedings of the National Academy of Sciences 1988-11-01

Uncoating ATPase, an abundant 70,000-mol-wt polypeptide mediating the ATP-dependent dissociation of clathrin from coated vesicles and empty cages, has been purified to virtual homogeneity calf brain cytosol. protein is present in cells amounts roughly stoichiometric with clathrin. This enzyme isolated as a mixture monomers dimers, both forms being active. ATP can support protein-facilitated at micromolar levels; all other ribotriphosphates well deoxy-ATP are inactive. The that released cages...

10.1083/jcb.99.2.723 article EN The Journal of Cell Biology 1984-08-01

Heat shock proteins (HSPs) derived from tumors or virally infected cells can stimulate antigen-specific CD8+ T cell responses in vitro and vivo. Although this antigenicity is known to arise HSP-associated peptides presented the immune system by major histocompatibility complex (MHC) class I molecules, biology underlying presentation process remains poorly understood. Here we show that HSP 70 binds surface of antigen presenting a mechanism with characteristics saturable receptor system. After...

10.1084/jem.191.11.1957 article EN The Journal of Experimental Medicine 1999-06-06

Dissecting SNARE Zippering The complex is critical for vesicle fusion, notably during release of neurotransmitters at synapses. Understanding the biophysics assembly has been object several structural studies, and yet much remains to be understood about mechanisms. Now, Gao et al. (p. 1340 , published online 16 August; see Perspective by Rizo ) describe results cell-free experiments using optical tweezers elucidate disassembly complex. Direct observations intermediates revealed multiple...

10.1126/science.1224492 article EN Science 2012-08-17

The NEM-sensitive fusion protein, NSF, together with SNAPs (soluble NSF attachment proteins) and the SNAREs (SNAP receptors), is thought to be generally used for of transport vesicles their target membranes. a homotrimer whose polypeptide subunits are made up three distinct domains: an amino-terminal domain (N) two homologous ATP-binding domains (D1 D2). Mutants were produced in which either order or composition altered. These mutants could not support intra-Golgi transport, but they...

10.1083/jcb.126.4.945 article EN The Journal of Cell Biology 1994-08-15
Coming Soon ...