Results 191 to 200 of about 18,838 (278)

Interfollicular Plasmacytosis and Hyperplastic Germinal Centers in Idiopathic Multicentric Castleman Disease, Idiopathic Plasmacytic Lymphadenopathy Subtype

open access: yes
American Journal of Hematology, EarlyView.
Stephanie Quon   +5 more
wiley   +1 more source

The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid. [PDF]

open access: yesAdv Sci (Weinh)
Peña-Díaz S   +12 more
europepmc   +1 more source

Proteinvermittelte Kupfer‐Redoxregulation: Rolle von Disulfidbrücken und allosterischer Modulation

open access: yesAngewandte Chemie, EarlyView.
Copper binding triggers structural changes that expose a reactive disulphide bridge, enabling intrinsic Cu(II) reduction in folded proteins. SAXS, XAS, and QM/MM simulations reveal how globular proteins such as HSA and SOD1 employ disulphide‐mediated dynamics to modulate site accessibility and control copper redox chemistry.
Rebecca Sternke‐Hoffmann   +9 more
wiley   +1 more source

The intrinsically disordered region of the human parathyroid hormone controls functional amyloid properties. [PDF]

open access: yesJ Biol Chem
Sachan S   +7 more
europepmc   +1 more source

O‐Terphenyl‐basierte Familie konjugierter Makrozyklen: Selektive Erkennung von Phenylalanin im Wasser und Interaktion mit Insulin

open access: yesAngewandte Chemie, EarlyView.
Diese Studie beschreibt die Herstellung und Eigenschaften einer neuen Familie von o‐Terphenyl‐basierten Makrozyklen, TP[n] (n = 2‐8). Der Trimer bindet Phenylalanin in Wasser sehr effizient und ist dabei zehnmal selektiver als bei anderen Aminosäuren und aromatischen Neurotransmittern.
Swapnil Ghule   +5 more
wiley   +1 more source

Structural basis for T-cell intracellular antigen-1 amyloid fibril formation revealed by cryo-electron microscopy. [PDF]

open access: yesPNAS Nexus
Inaoka D   +13 more
europepmc   +1 more source

Origin of class B J-domain proteins involved in amyloid transactions. [PDF]

open access: yesProc Natl Acad Sci U S A
Domanski P   +13 more
europepmc   +1 more source

Protein‐Driven Copper Redox Regulation: Uncovering the Role of Disulphide Bonds and Allosteric Modulation

open access: yesAngewandte Chemie International Edition, EarlyView.
Copper binding triggers structural changes that expose a reactive disulphide bridge, enabling intrinsic Cu(II) reduction in folded proteins. SAXS, XAS, and QM/MM simulations reveal how globular proteins such as HSA and SOD1 employ disulphide‐mediated dynamics to modulate site accessibility and control copper redox chemistry.
Rebecca Sternke‐Hoffmann   +9 more
wiley   +1 more source

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