Tim Schulte
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View article: Development of DARPin T cell engagers for specific targeting of tumor-associated HLA/peptide complexes
Development of DARPin T cell engagers for specific targeting of tumor-associated HLA/peptide complexes Open
The balance between affinity and specificity in T cell receptor (TCR)-dependent targeting of HLA-restricted tumor-associated antigens presents a significant challenge for immunotherapy development. T cell engagers that circumvent these lim…
View article: Development of DARPin T cell engagers for specific targeting of tumor-associated HLA/peptide complexes
Development of DARPin T cell engagers for specific targeting of tumor-associated HLA/peptide complexes Open
The compromise between affinity and specificity in TCR-dependent targeting of HLA-restricted tumor-associated antigens presents a significant challenge in developing efficacious immunotherapies. As such, T cell engagers which circumvent th…
View article: Nanobodies counteract the toxicity of an amyloidogenic light chain by stabilizing a partially open dimeric conformation
Nanobodies counteract the toxicity of an amyloidogenic light chain by stabilizing a partially open dimeric conformation Open
Broggini L, Barzago MM, Speranzini V, Schulte T, Sonzini F, Giono M, Romeo M, Milani P, Caminito S, Mazzini G, Rognoni P, Merlini G, Pappone C, Anastasia L, Nuvolone M, Palladini G, Diomede L, Ricagno S. Nanobodies counteract the toxicity …
View article: Nanobodies counteract the toxicity of an amyloidogenic light chain by stabilizing a partially open dimeric conformation
Nanobodies counteract the toxicity of an amyloidogenic light chain by stabilizing a partially open dimeric conformation Open
Broggini L, Barzago MM, Speranzini V, Schulte T, Sonzini F, Giono M, Romeo M, Milani P, Caminito S, Mazzini G, Rognoni P, Merlini G, Pappone C, Anastasia L, Nuvolone M, Palladini G, Diomede L, Ricagno S. Nanobodies counteract the toxicity …
View article: Helical superstructures between amyloid and collagen VI in heart-derived fibrils from a patient with Light Chain Amyloidosis.
Helical superstructures between amyloid and collagen VI in heart-derived fibrils from a patient with Light Chain Amyloidosis. Open
Systemic light chain (LC) amyloidosis (AL) is a disease where organs are damaged by an overload of a misfolded patient-specific antibody-derived LC, secreted by an abnormal B cell clone. The high LC concentration in the blood leads to amyl…
View article: The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with chemokine CXCL12
The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with chemokine CXCL12 Open
Chemokines engage in heterodimeric interactions to activate or dampen their cognate receptors in inflammatory conditions. The chemokine CXCL12 forms with the alarmin HMGB1 a patho-physiologically relevant heterocomplex (HMGB1●CXCL12), whos…
View article: Caprin-1 binding to the critical stress granule protein G3BP1 is influenced by pH
Caprin-1 binding to the critical stress granule protein G3BP1 is influenced by pH Open
G3BP is the central node within stress-induced protein–RNA interaction networks known as stress granules (SGs). The SG-associated proteins Caprin-1 and USP10 bind mutually exclusively to the NTF2 domain of G3BP1, promoting and inhibiting S…
View article: The Cryo-EM structure of renal amyloid fibril suggests structurally homogeneous multiorgan aggregation in AL amyloidosis
The Cryo-EM structure of renal amyloid fibril suggests structurally homogeneous multiorgan aggregation in AL amyloidosis Open
Immunoglobulin light chain amyloidosis (AL) is caused by the aberrant production of amyloidogenic light chains (LC) that accumulate as amyloid deposits in vital organs. Distinct LC sequences in each patient yield distinct amyloid structure…
View article: AA-amyloidosis in cats (Felis catus) housed in shelters
AA-amyloidosis in cats (Felis catus) housed in shelters Open
Systemic AA-amyloidosis is a protein-misfolding disease characterized by fibril deposition of serum amyloid-A protein (SAA) in several organs in humans and many animal species. Fibril deposits originate from abnormally high serum levels of…
View article: Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains
Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains Open
Russo R, Romeo M, Schulte T, Maritan M, Oberti L, Barzago MM, Barbiroli A, Pappone C, Anastasia L, Palladini G, Diomede L, Ricagno S. Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains. Int J Mol Sci. 2022 Jan 16;2…
View article: Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains
Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains Open
Russo R, Romeo M, Schulte T, Maritan M, Oberti L, Barzago MM, Barbiroli A, Pappone C, Anastasia L, Palladini G, Diomede L, Ricagno S. Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains. Int J Mol Sci. 2022 Jan 16;2…
View article: Cryo-EM structure of<i>ex vivo</i>fibrils associated with extreme AA amyloidosis prevalence in a cat shelter
Cryo-EM structure of<i>ex vivo</i>fibrils associated with extreme AA amyloidosis prevalence in a cat shelter Open
AA amyloidosis is a systemic disease characterized by deposition of misfolded serum amyloid A protein (SAA) into cross-β amyloid in multiple organs in humans and animals. AA amyloidosis occurs at high SAA serum levels during chronic inflam…
View article: AA-amyloidosis in cats (<i>Felis catus</i>) housed in shelters
AA-amyloidosis in cats (<i>Felis catus</i>) housed in shelters Open
Systemic AA-amyloidosis is a protein-misfolding disease that is characterized by fibril deposition of serum amyloid-A protein (SAA) in several organs in humans and many animal species. Fibril deposits originate from abnormally high serum l…
View article: Micrographs of ex vivo AA amyloid from renal tissue of a short hair cat deceased in a shelter
Micrographs of ex vivo AA amyloid from renal tissue of a short hair cat deceased in a shelter Open
EMPIAR, the Electron Microscopy Public Image Archive centered at EMBL-EBI, is a public resource for raw electron microscopy images related to EMDB, contains micrographs, particle sets and tilt-series.
View article: Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains
Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains Open
Light chain amyloidosis (AL) is caused by the aberrant overproduction of immunoglobulin light chains (LCs). The resulting abnormally high LC concentrations in blood lead to deposit formation in the heart and other target organs. Organ dama…
View article: Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains
Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains Open
Light chain amyloidosis (AL) is caused by the aberrant overproduction of immunoglobulin light chains (LCs). The resulting abnormally high LC concentrations in blood lead to deposit formation in the heart and other target organs. Organ dama…
View article: Caprin-1 binding to the critical stress granule protein G3BP1 is regulated by pH
Caprin-1 binding to the critical stress granule protein G3BP1 is regulated by pH Open
G3BP is the central hub within the protein-RNA interaction network of stress-induced bio-molecular condensates known as stress granules (SG). The SG-associated proteins Caprin-1 and USP10 exhibit mutually exclusive binding to the structure…
View article: An alpaca nanobody neutralizes SARS-CoV-2 by blocking receptor interaction
An alpaca nanobody neutralizes SARS-CoV-2 by blocking receptor interaction Open
SARS-CoV-2 enters host cells through an interaction between the spike glycoprotein and the angiotensin converting enzyme 2 (ACE2) receptor. Directly preventing this interaction presents an attractive possibility for suppressing SARS-CoV-2 …
View article: An alpaca nanobody neutralizes SARS-CoV-2 by blocking receptor interaction
An alpaca nanobody neutralizes SARS-CoV-2 by blocking receptor interaction Open
SARS-CoV-2 is the etiologic agent of COVID-19, currently causing a devastating pandemic for which pharmacological interventions are urgently needed. The virus enters host cells through an interaction between the spike glycoprotein and the …
View article: Phosphorylation of G3BP1-S149 does not influence stress granule assembly
Phosphorylation of G3BP1-S149 does not influence stress granule assembly Open
Tourrière et al. (2003. J. Cell Biol. https://doi.org/10.1083/jcb.200212128) reported that G3BP1-S149 dephosphorylation promotes stress granule formation. We show that constructs used to establish this conclusion contain additional mutatio…
View article: Revisiting G3BP-S149 phosphorylation and its impact on stress granule assembly
Revisiting G3BP-S149 phosphorylation and its impact on stress granule assembly Open
Stress granules (SGs) are cytoplasmic, non-membranous RNA/protein structures that assemble in response to environmental stress. G3BP is a critical SG-nucleating protein, and its ability to regulate SGs has been reported to be regulated by …
View article: Biofilm formation – what we can learn from recent developments
Biofilm formation – what we can learn from recent developments Open
Although biofilms have been observed early in the history of microbial research, their impact has only recently been fully recognized. Biofilm infections, which contribute to up to 80% of human microbial infections, are associated with com…