2009 - Fellow of the Mineralogical Society of America
2006 - Distinguished Scientist Award, Mineralogical Society of America
1966 - Fellow of the American Association for the Advancement of Science (AAAS)
Joseph S. Wall mainly focuses on Crystallography, Scanning transmission electron microscopy, Biophysics, Biochemistry and Fibril. The study incorporates disciplines such as Protein structure, Dimer, Fiber and Monomer in addition to Crystallography. His Scanning transmission electron microscopy study is concerned with the larger field of Electron microscope.
The various areas that Joseph S. Wall examines in his Biophysics study include Molecular biology, Nucleus, Plant cell and Agrobacterium tumefaciens. While the research belongs to areas of Biochemistry, he spends his time largely on the problem of Cell biology, intersecting his research to questions surrounding Myxococcus xanthus. His Fibril research is multidisciplinary, incorporating elements of Peptide sequence, Recombinant DNA and Peptide.
The scientist’s investigation covers issues in Scanning transmission electron microscopy, Crystallography, Biophysics, Electron microscope and Biochemistry. Joseph S. Wall works mostly in the field of Scanning transmission electron microscopy, limiting it down to topics relating to Ribosomal RNA and, in certain cases, Ribosomal protein and Ribosome, as a part of the same area of interest. His Crystallography study integrates concerns from other disciplines, such as Protein structure, Dimer, Protein subunit and Molecular mass.
As a part of the same scientific family, Joseph S. Wall mostly works in the field of Dimer, focusing on Stereochemistry and, on occasion, Trimer. In the subject of general Biophysics, his work in Fibril is often linked to Amyloid fibril and Tau protein, thereby combining diverse domains of study. His study in Electron microscope is interdisciplinary in nature, drawing from both Transmission electron microscopy and Scanning electron microscope.
Biophysics, Crystallography, Fibril, Protein structure and Self-assembly are his primary areas of study. His research in Biophysics intersects with topics in Scanning transmission electron microscopy, Protein subunit and Biochemistry. Scanning transmission electron microscopy and Membrane are frequently intertwined in his study.
His Crystallography study also includes fields such as
His primary areas of investigation include Fibril, Crystallography, Biophysics, Protein structure and Peptide sequence. In his study, Electron microscope, Microscopy, Molecular model and Dimer is strongly linked to Protein aggregation, which falls under the umbrella field of Crystallography. His Biophysics research incorporates themes from Scanning transmission electron microscopy, Protein subunit, Peptide and Amyloidosis.
Scanning transmission electron microscopy and Transmembrane protein are two areas of study in which Joseph S. Wall engages in interdisciplinary research. Protein structure is a subfield of Biochemistry that he studies. His Peptide sequence research includes elements of Fiber diffraction, Extracellular and Sequence.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils
Hilal A. Lashuel;Benjamin M. Petre;Joseph Wall;Martha Simon.
Journal of Molecular Biology (2002)
Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril
Marielle Aulikki Wälti;Francesco Ravotti;Hiromi Arai;Charles G. Glabe.
Proceedings of the National Academy of Sciences of the United States of America (2016)
Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils
Michael T. Colvin;Robert Silvers;Qing Zhe Ni;Thach V. Can.
Journal of the American Chemical Society (2016)
Relative Nucleophilic Reactivities of Amino Groups and Mercaptide Ions in Addition Reactions with α,β-Unsaturated Compounds1,2
Mendel Friedman;J. F. Cavins;J. S. Wall.
Journal of the American Chemical Society (1965)
A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
J D Trent;E Nimmesgern;J S Wall;F U Hartl.
ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replication.
Iris A. Mastrangelo;Paul V. C. Hough;Joseph S. Wall;Mark Dodson.
Molecular basis for insulin fibril assembly.
Magdalena I. Ivanova;Stuart A. Sievers;Michael R. Sawaya;Joseph S. Wall.
Proceedings of the National Academy of Sciences of the United States of America (2009)
Microtubule-associated protein 1C from brain is a two-headed cytosolic dynein
Richard B. Vallee;Joseph S. Wall;Bryce Mark Paschal;Howard S. Shpetner.
Structure of the herpes simplex virus capsid : molecular composition of the pentons and the triplexes
William W. Newcomb;Benes L. Trus;Frank P. Booy;Alasdair C. Steven.
Journal of Molecular Biology (1993)
DNA looping and Sp1 multimer links: a mechanism for transcriptional synergism and enhancement.
Iris A. Mastrangelo;Albert J. Courey;Joseph S. Wall;Stephen P. Jackson.
Proceedings of the National Academy of Sciences of the United States of America (1991)
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