The consequence of ATP synthase dimer angle on mitochondrial morphology studied by cryo-electron tomography
Biochem J. 2024 Jan 2:BCJ20230450. doi: 10.1042/BCJ20230450. Online ahead of print.ABSTRACTMitochondrial ATP synthases form rows of dimers, which induce membrane curvature to give cristae their characteristic lamellar or tubular morphology. The angle formed between the central stalks of ATP synthase dimers varies between species. Using cryo-electron tomography and sub-tomogram averaging, we determined the structure of the ATP synthase dimer from the nematode worm C. elegans and show that the dimer angle differs from previously determined structures. The consequences of this species-specific difference at the dimer interfac...
Source: The Biochemical Journal - January 2, 2024 Category: Biochemistry Authors: Emma Buzzard Mathew McLaren Piotr Bragoszewski Andrea Brancaccio Holly Ford Bertram Daum Patricia Kuwabara Ian Collinson Vicki Gold Source Type: research
Non-crosslinking advanced glycation end products affect prohormone processing
Biochem J. 2023 Dec 19:BCJ20230321. doi: 10.1042/BCJ20230321. Online ahead of print.ABSTRACTAdvanced glycation end products (AGEs) are non-enzymatic post-translational modifications of amino acids. and are associated with diabetic complications. One proposed pathomechanism is the impaired processing of AGE-modified proteins or peptides including prohormones. Two approaches were applied to investigate whether substrate modification with AGEs affects the processing of substrates like prohormones to the active hormones. First, we employed solid phase peptide synthesis to generate unmodified as well as AGE-modified protease su...
Source: The Biochemical Journal - December 19, 2023 Category: Biochemistry Authors: Sebastian Brings Walter Mier Barbro Beijer Elisabeth Kliemank Stephan Herzig Julia Szendroedi Peter Nawroth Thomas Fleming Source Type: research
Non-crosslinking advanced glycation end products affect prohormone processing
Biochem J. 2023 Dec 19:BCJ20230321. doi: 10.1042/BCJ20230321. Online ahead of print.ABSTRACTAdvanced glycation end products (AGEs) are non-enzymatic post-translational modifications of amino acids. and are associated with diabetic complications. One proposed pathomechanism is the impaired processing of AGE-modified proteins or peptides including prohormones. Two approaches were applied to investigate whether substrate modification with AGEs affects the processing of substrates like prohormones to the active hormones. First, we employed solid phase peptide synthesis to generate unmodified as well as AGE-modified protease su...
Source: The Biochemical Journal - December 19, 2023 Category: Biochemistry Authors: Sebastian Brings Walter Mier Barbro Beijer Elisabeth Kliemank Stephan Herzig Julia Szendroedi Peter Nawroth Thomas Fleming Source Type: research
Non-crosslinking advanced glycation end products affect prohormone processing
Biochem J. 2023 Dec 19:BCJ20230321. doi: 10.1042/BCJ20230321. Online ahead of print.ABSTRACTAdvanced glycation end products (AGEs) are non-enzymatic post-translational modifications of amino acids. and are associated with diabetic complications. One proposed pathomechanism is the impaired processing of AGE-modified proteins or peptides including prohormones. Two approaches were applied to investigate whether substrate modification with AGEs affects the processing of substrates like prohormones to the active hormones. First, we employed solid phase peptide synthesis to generate unmodified as well as AGE-modified protease su...
Source: The Biochemical Journal - December 19, 2023 Category: Biochemistry Authors: Sebastian Brings Walter Mier Barbro Beijer Elisabeth Kliemank Stephan Herzig Julia Szendroedi Peter Nawroth Thomas Fleming Source Type: research
Non-crosslinking advanced glycation end products affect prohormone processing
Biochem J. 2023 Dec 19:BCJ20230321. doi: 10.1042/BCJ20230321. Online ahead of print.ABSTRACTAdvanced glycation end products (AGEs) are non-enzymatic post-translational modifications of amino acids. and are associated with diabetic complications. One proposed pathomechanism is the impaired processing of AGE-modified proteins or peptides including prohormones. Two approaches were applied to investigate whether substrate modification with AGEs affects the processing of substrates like prohormones to the active hormones. First, we employed solid phase peptide synthesis to generate unmodified as well as AGE-modified protease su...
Source: The Biochemical Journal - December 19, 2023 Category: Biochemistry Authors: Sebastian Brings Walter Mier Barbro Beijer Elisabeth Kliemank Stephan Herzig Julia Szendroedi Peter Nawroth Thomas Fleming Source Type: research
Non-crosslinking advanced glycation end products affect prohormone processing
Biochem J. 2023 Dec 19:BCJ20230321. doi: 10.1042/BCJ20230321. Online ahead of print.ABSTRACTAdvanced glycation end products (AGEs) are non-enzymatic post-translational modifications of amino acids. and are associated with diabetic complications. One proposed pathomechanism is the impaired processing of AGE-modified proteins or peptides including prohormones. Two approaches were applied to investigate whether substrate modification with AGEs affects the processing of substrates like prohormones to the active hormones. First, we employed solid phase peptide synthesis to generate unmodified as well as AGE-modified protease su...
Source: The Biochemical Journal - December 19, 2023 Category: Biochemistry Authors: Sebastian Brings Walter Mier Barbro Beijer Elisabeth Kliemank Stephan Herzig Julia Szendroedi Peter Nawroth Thomas Fleming Source Type: research
Non-crosslinking advanced glycation end products affect prohormone processing
Biochem J. 2023 Dec 19:BCJ20230321. doi: 10.1042/BCJ20230321. Online ahead of print.ABSTRACTAdvanced glycation end products (AGEs) are non-enzymatic post-translational modifications of amino acids. and are associated with diabetic complications. One proposed pathomechanism is the impaired processing of AGE-modified proteins or peptides including prohormones. Two approaches were applied to investigate whether substrate modification with AGEs affects the processing of substrates like prohormones to the active hormones. First, we employed solid phase peptide synthesis to generate unmodified as well as AGE-modified protease su...
Source: The Biochemical Journal - December 19, 2023 Category: Biochemistry Authors: Sebastian Brings Walter Mier Barbro Beijer Elisabeth Kliemank Stephan Herzig Julia Szendroedi Peter Nawroth Thomas Fleming Source Type: research
Non-crosslinking advanced glycation end products affect prohormone processing
Biochem J. 2023 Dec 19:BCJ20230321. doi: 10.1042/BCJ20230321. Online ahead of print.ABSTRACTAdvanced glycation end products (AGEs) are non-enzymatic post-translational modifications of amino acids. and are associated with diabetic complications. One proposed pathomechanism is the impaired processing of AGE-modified proteins or peptides including prohormones. Two approaches were applied to investigate whether substrate modification with AGEs affects the processing of substrates like prohormones to the active hormones. First, we employed solid phase peptide synthesis to generate unmodified as well as AGE-modified protease su...
Source: The Biochemical Journal - December 19, 2023 Category: Biochemistry Authors: Sebastian Brings Walter Mier Barbro Beijer Elisabeth Kliemank Stephan Herzig Julia Szendroedi Peter Nawroth Thomas Fleming Source Type: research
Non-crosslinking advanced glycation end products affect prohormone processing
Biochem J. 2023 Dec 19:BCJ20230321. doi: 10.1042/BCJ20230321. Online ahead of print.ABSTRACTAdvanced glycation end products (AGEs) are non-enzymatic post-translational modifications of amino acids. and are associated with diabetic complications. One proposed pathomechanism is the impaired processing of AGE-modified proteins or peptides including prohormones. Two approaches were applied to investigate whether substrate modification with AGEs affects the processing of substrates like prohormones to the active hormones. First, we employed solid phase peptide synthesis to generate unmodified as well as AGE-modified protease su...
Source: The Biochemical Journal - December 19, 2023 Category: Biochemistry Authors: Sebastian Brings Walter Mier Barbro Beijer Elisabeth Kliemank Stephan Herzig Julia Szendroedi Peter Nawroth Thomas Fleming Source Type: research
Non-crosslinking advanced glycation end products affect prohormone processing
Biochem J. 2023 Dec 19:BCJ20230321. doi: 10.1042/BCJ20230321. Online ahead of print.ABSTRACTAdvanced glycation end products (AGEs) are non-enzymatic post-translational modifications of amino acids. and are associated with diabetic complications. One proposed pathomechanism is the impaired processing of AGE-modified proteins or peptides including prohormones. Two approaches were applied to investigate whether substrate modification with AGEs affects the processing of substrates like prohormones to the active hormones. First, we employed solid phase peptide synthesis to generate unmodified as well as AGE-modified protease su...
Source: The Biochemical Journal - December 19, 2023 Category: Biochemistry Authors: Sebastian Brings Walter Mier Barbro Beijer Elisabeth Kliemank Stephan Herzig Julia Szendroedi Peter Nawroth Thomas Fleming Source Type: research
Non-crosslinking advanced glycation end products affect prohormone processing
Biochem J. 2023 Dec 19:BCJ20230321. doi: 10.1042/BCJ20230321. Online ahead of print.ABSTRACTAdvanced glycation end products (AGEs) are non-enzymatic post-translational modifications of amino acids. and are associated with diabetic complications. One proposed pathomechanism is the impaired processing of AGE-modified proteins or peptides including prohormones. Two approaches were applied to investigate whether substrate modification with AGEs affects the processing of substrates like prohormones to the active hormones. First, we employed solid phase peptide synthesis to generate unmodified as well as AGE-modified protease su...
Source: The Biochemical Journal - December 19, 2023 Category: Biochemistry Authors: Sebastian Brings Walter Mier Barbro Beijer Elisabeth Kliemank Stephan Herzig Julia Szendroedi Peter Nawroth Thomas Fleming Source Type: research
Correction: Mechanism of sphingosine 1-phosphate clearance from blood
Biochem J. 2023 Dec 20;480(24):2059-2060. doi: 10.1042/BCJ20190730_COR.NO ABSTRACTPMID:38108461 | DOI:10.1042/BCJ20190730_COR (Source: The Biochemical Journal)
Source: The Biochemical Journal - December 18, 2023 Category: Biochemistry Authors: Yugesh Kharel Tao Huang Anita Salamon Thurl E Harris Webster L Santos Kevin R Lynch Source Type: research
Correction: Mechanism of sphingosine 1-phosphate clearance from blood
Biochem J. 2023 Dec 20;480(24):2059-2060. doi: 10.1042/BCJ20190730_COR.NO ABSTRACTPMID:38108461 | DOI:10.1042/BCJ20190730_COR (Source: The Biochemical Journal)
Source: The Biochemical Journal - December 18, 2023 Category: Biochemistry Authors: Yugesh Kharel Tao Huang Anita Salamon Thurl E Harris Webster L Santos Kevin R Lynch Source Type: research
Into the fold: advances in understanding aPKC membrane dynamics
Biochem J. 2023 Dec 20;480(24):2037-2044. doi: 10.1042/BCJ20230390.ABSTRACTAtypical protein kinase Cs (aPKCs) are part of the PKC family of protein kinases and are atypical because they don't respond to the canonical PKC activators diacylglycerol (DAG) and Ca2+. They are central to the organization of polarized cells and are deregulated in several cancers. aPKC recruitment to the plasma membrane compartment is crucial to their encounter with substrates associated with polarizing functions. However, in contrast with other PKCs, the mechanism by which atypical PKCs are recruited there has remained elusive until recently. Her...
Source: The Biochemical Journal - December 15, 2023 Category: Biochemistry Authors: Mathias Cobbaut Peter J Parker Neil Q McDonald Source Type: research
Into the fold: advances in understanding aPKC membrane dynamics
Biochem J. 2023 Dec 20;480(24):2037-2044. doi: 10.1042/BCJ20230390.ABSTRACTAtypical protein kinase Cs (aPKCs) are part of the PKC family of protein kinases and are atypical because they don't respond to the canonical PKC activators diacylglycerol (DAG) and Ca2+. They are central to the organization of polarized cells and are deregulated in several cancers. aPKC recruitment to the plasma membrane compartment is crucial to their encounter with substrates associated with polarizing functions. However, in contrast with other PKCs, the mechanism by which atypical PKCs are recruited there has remained elusive until recently. Her...
Source: The Biochemical Journal - December 15, 2023 Category: Biochemistry Authors: Mathias Cobbaut Peter J Parker Neil Q McDonald Source Type: research
