C. Blobel

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Potential Role for ADAM15 in Pathological Neovascularization in Mice

K. Horiuchi, G. Weskamp, L. Lum, 2003, Molecular and Cellular Biology.

ADAM12 is highly expressed in carcinoma-associated stroma and is required for mouse prostate tumor progression

C. Blobel, V. Reuter, H. Scher, 2006, Oncogene.

iRhom2 controls the substrate selectivity of stimulated ADAM17-dependent ectodomain shedding

C. Blobel, T. Mak, D. Mcilwain, 2013, Proceedings of the National Academy of Sciences.

Deletions in the cytoplasmic domain of iRhom1 and iRhom2 promote shedding of the TNF receptor by the protease ADAM17

G. Nolan, N. Aghaeepour, C. Blobel, 2015, Science Signaling.

In search of partners: linking extracellular proteases to substrates

Christopher M. Overall, C. Blobel, C. Overall, 2007, Nature Reviews Molecular Cell Biology.

Analysis of the Conditions That Affect the Selective Processing of Endogenous Notch1 by ADAM10 and ADAM17

C. Blobel, J. Lora, R. Alabi, 2021, International journal of molecular sciences.

Intriguing Roles for Endothelial ADAM10/Notch Signaling in the Development of Organ-Specific Vascular Beds.

C. Blobel, R. Alabi, Gregory Farber, 2018, Physiological reviews.

ADAM10-Dependent Signaling Through Notch1 and Notch4 Controls Development of Organ-Specific Vascular Beds.

G. Weskamp, C. Blobel, S. Monette, 2016, Circulation research.

Epidermal ADAM17 is dispensable for Notch activation

C. Blobel, P. Saftig, M. Vooijs, 2013, The Journal of investigative dermatology.

Deletion of Adam10 in endothelial cells leads to defects in organ-specific vascular structures.

K. Manova, C. Blobel, B. de Strooper, 2011, Blood.

Macrocyclic θ-defensins suppress tumor necrosis factor-α (TNF-α) shedding by inhibition of TNF-α–converting enzyme

C. Blobel, M. Selsted, A. Ouellette, 2018, The Journal of Biological Chemistry.

Metalloprotease-Disintegrin MDC9: Intracellular Maturation and Catalytic Activity*

G. Weskamp, C. Blobel, H. Erdjument-Bromage, 1999, The Journal of Biological Chemistry.

Epidermal ADAM17 maintains the skin barrier by regulating EGFR ligand–dependent terminal keratinocyte differentiation

K. Horiuchi, C. Blobel, D. Threadgill, 2012, The Journal of experimental medicine.

A protective Langerhans cell–keratinocyte axis that is dysfunctional in photosensitivity

C. Blobel, E. Pamer, P. Izmirly, 2018, Science Translational Medicine.

Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion.

C. Blobel, J. White, P. Primakoff, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Blood-Induced Arthropathy in Hemophilia: Mechanisms and Heterogeneity

C. Blobel, J. Salmon, E. Dicarlo, 2015, Seminars in Thrombosis & Hemostasis.

Roles of Metalloprotease-Disintegrins in Cell-Cell Interactions, in Neurogenesis, and in the Cleavage of TNFα

C. Blobel, 1999 .

Evidence for a Role of a Tumor Necrosis Factor-α (TNF-α)-converting Enzyme-like Protease in Shedding of TRANCE, a TNF Family Member Involved in Osteoclastogenesis and Dendritic Cell Survival*

L. Lum, C. Blobel, H. Erdjument-Bromage, 1999, The Journal of Biological Chemistry.

A Novel Regulatory Role for Stromal-derived Factor-1 Signaling in Bone Morphogenic Protein-2 Osteogenic Differentiation of Mesenchymal C2C12 Cells*

B. Frenkel, C. Blobel, O. Boachie-Adjei, 2007, Journal of Biological Chemistry.

Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival.

L. Lum, C. Blobel, H. Erdjument-Bromage, 1999, The Journal of biological chemistry.

Biochemical and Pharmacological Criteria Define Two Shedding Activities for TRANCE/OPGL That Are Distinct from the Tumor Necrosis Factor α Convertase*

L. Lum, C. Blobel, J. Schlöndorff, 2001, The Journal of Biological Chemistry.

Characterization of the catalytic properties of the membrane-anchored metalloproteinase ADAM9 in cell-based assays.

G. Weskamp, C. Blobel, K. Reiss, 2017, The Biochemical journal.

Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs).

C. Blobel, J. Becherer, Carl P. Blobel, 2003, Current topics in developmental biology.

ADAM10 and ADAM17 promote SARS‐CoV‐2 cell entry and spike protein‐mediated lung cell fusion

C. Blobel, A. Pichlmair, O. Gokce, 2022, EMBO reports.

Cell Surface Colony-Stimulating Factor 1 Can Be Cleaved by TNF-α Converting Enzyme or Endocytosed in a Clathrin-Dependent Manner1

K. Horiuchi, C. Blobel, Y. Toyama, 2007, The Journal of Immunology.

Stimulated Shedding of Vascular Cell Adhesion Molecule 1 (VCAM-1) Is Mediated by Tumor Necrosis Factor-α-converting Enzyme (ADAM 17)*

C. Blobel, P. Dempsey, E. Raines, 2003, Journal of Biological Chemistry.

Blood-induced bone loss in murine hemophilic arthropathy is prevented by blocking the iRhom2/ADAM17/TNF-α pathway.

C. Blobel, T. Mak, D. Mcilwain, 2018, Blood.

Loss of the Metalloprotease ADAM9 Leads to Cone-Rod Dystrophy in Humans and Retinal Degeneration in Mice

Colin A. Johnson, S. Jacobson, Rebecca K. Chance, 2009, American journal of human genetics.

Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence

C. Blobel, J. White, P. Primakoff, 1990, The Journal of cell biology.

The pseudoprotease iRhom1 controls ectodomain shedding of membrane proteins in the nervous system

N. Plesnila, C. Blobel, M. Simons, 2021, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

MyD88 signaling in nonhematopoietic cells protects mice against induced colitis by regulating specific EGF receptor ligands

C. Blobel, B. Beutler, Xiaohong Li, 2010, Proceedings of the National Academy of Sciences.

3D trumps 2D when studying endothelial cells.

C. Blobel, 2010, Blood.

Intravitreal injection of TIMP3 or the EGFR inhibitor erlotinib offers protection from oxygen-induced retinopathy in mice.

G. Weskamp, C. Blobel, R. Khokha, 2013, Investigative ophthalmology & visual science.

ADAM17 stabilizes its interacting partner inactive Rhomboid 2 (iRhom2) but not inactive Rhomboid 1 (iRhom1)

G. Weskamp, C. Blobel, T. Mak, 2020, The Journal of Biological Chemistry.

Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin.

L. Lum, C. Blobel, Carl P. Blobel, 1997, Developmental biology.

iRhom2 Regulation of TACE Controls TNF-Mediated Protection Against Listeria and Responses to LPS

C. Blobel, T. Mak, R. Khokha, 2012, Science.

Glomerular endothelial cell maturation depends on ADAM10, a key regulator of Notch signaling

C. Blobel, Raphael Kopan, C. Meyer-Schwesinger, 2018, Angiogenesis.

iRhom2 regulates CSF1R cell surface expression and non‐steady state myelopoiesis in mice

C. Blobel, T. Mak, M. Merad, 2016, European journal of immunology.

iRHOM2 is a critical pathogenic mediator of inflammatory arthritis.

K. Horiuchi, C. Blobel, T. Mak, 2013, The Journal of clinical investigation.

VEGF-A Stimulates ADAM17-Dependent Shedding of VEGFR2 and Crosstalk Between VEGFR2 and ERK Signaling

S. Rafii, K. Horiuchi, G. Weskamp, 2008, Circulation research.

TACE (ADAM17) inhibits Schwann cell myelination

K. Horiuchi, C. Blobel, L. Wrabetz, 2011, Nature Neuroscience.

Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta.

C. Blobel, J. Schlöndorff, K. Nelson, 1999, The Biochemical journal.

iRhoms 1 and 2 are essential upstream regulators of ADAM17-dependent EGFR signaling

G. Weskamp, C. Blobel, T. Mak, 2015, Proceedings of the National Academy of Sciences.

Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1).

C. Blobel, D. Greaves, P. Dempsey, 2001, The Journal of biological chemistry.

The metalloprotease ADAM10 (a disintegrin and metalloprotease 10) undergoes rapid, postlysis autocatalytic degradation

C. Blobel, P. Noy, M. Tomlinson, 2018, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

ADAM10 is a principal 'sheddase' of the low-affinity immunoglobulin E receptor CD23

S. Umland, G. Weskamp, C. Blobel, 2006, Nature Immunology.

Evaluation of the contribution of different ADAMs to tumor necrosis factor alpha (TNFalpha) shedding and of the function of the TNFalpha ectodomain in ensuring selective stimulated shedding by the TNFalpha convertase (TACE/ADAM17).

C. Blobel, D. Hartmann, P. Saftig, 2004, The Journal of biological chemistry.

Correction to Epidermal ADAM17 maintains the skin barrier by regulating EGFR ligand-dependent terminal keratinocyte differentiation [The Journal of Experimental Medicine, 209, 6, (2012) 1105-1119]

K. Horiuchi, C. Blobel, D. Threadgill, 2012 .

The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs

P. Slocombe, C. Blobel, W. English, 2002, FEBS letters.

Cloning and Initial Characterization of Mouse Meltrin β and Analysis of the Expression of Four MetalloproteaseDisintegrins in Bone Cells*

G. Weskamp, L. Lum, R. Baron, 1998, The Journal of Biological Chemistry.

A family of cellular proteins related to snake venom disintegrins.

G. Weskamp, C. Blobel, Carl P. Blobel, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Functional and biochemical characterization of ADAMs and their predicted role in protein ectodomain shedding

C. Blobel, Carl P. Blobel, 2002, Inflammation Research.

The Threshold Effect: Lipopolysaccharide-Induced Inflammatory Responses in Primary Macrophages Are Differentially Regulated in an iRhom2-Dependent Manner

C. Blobel, G. Dixit, T. Maretzky, 2021, Frontiers in Cellular and Infection Microbiology.

Substrate‐selective protein ectodomain shedding by ADAM17 and iRhom2 depends on their juxtamembrane and transmembrane domains

H. Weinstein, C. Blobel, T. Mak, 2020, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

The xenoestrogens biphenol‐A and nonylphenol differentially regulate metalloprotease‐mediated shedding of EGFR ligands

C. Blobel, T. Mak, Xia Li, 2018, Journal of cellular physiology.

Ectodomain Shedding of FLT3 Ligand Is Mediated by TNF-α Converting Enzyme1

K. Horiuchi, C. Blobel, Y. Toyama, 2009, The Journal of Immunology.

Cutting Edge: TNF-α-Converting Enzyme (TACE/ADAM17) Inactivation in Mouse Myeloid Cells Prevents Lethality from Endotoxin Shock1

K. Horiuchi, C. Blobel, Y. Okada, 2007, The Journal of Immunology.

Metalloproteases regulate T‐cell proliferation and effector function via LAG‐3

C. Blobel, R. Black, D. Hartmann, 2007, The EMBO journal.

ADAM28, mouse form

C. Blobel, 2004 .

ADAMs and ADAMTSs☆

C. Blobel, S. Apte, 2020, Reference Module in Biomedical Sciences.

ADAMs and ADAMTSs

C. Blobel, S. Apte, 2020, Reference Module in Biomedical Sciences.

Intracellular maturation and localization of the tumour necrosis factor α convertase ( TACE )

C. Blobel, J. Schlöndorff, J. Becherer, 2022 .

ADAMs: key components in EGFR signalling and development

C. Blobel, Carl P. Blobel, 2005, Nature Reviews Molecular Cell Biology.

A sensitive method to monitor ectodomain shedding of ligands of the epidermal growth factor receptor.

K. Horiuchi, G. Weskamp, C. Blobel, 2006, Methods in molecular biology.

Structure, function and evolutionary relationship of proteins containing a disintegrin domain

C. Blobel, J. White, Carl P. Blobel, 1992, Current Biology.

ADAM 10 is a principal ‘ sheddase ’ of the low-affinity immunoglobulin E receptor CD 23

S. Umland, G. Weskamp, C. Blobel, 2006 .

ADAM9 Is Involved in Pathological Retinal Neovascularization (cid:1)

P. Campochiaro, C. Blobel, S. Chavala, 2009 .

The Cytoplasmic Domain of A Disintegrin and Metalloproteinase 10 (ADAM10) Regulates Its Constitutive Activity but Is Dispensable for Stimulated ADAM10-dependent Shedding*

C. Blobel, K. Reiss, N. Speck, 2015, The Journal of Biological Chemistry.

TNF-alpha-converting enzyme (TACE/ADAM17) inactivation in mouse myeloid cells prevents lethality from endotoxin shock

K. Horiuchi, C. Blobel, Y. Okada, 2007 .

Evidence for cadherin-11 cleavage in the synovium and partial characterization of its mechanism

C. Blobel, G. Watts, M. Brenner, 2015, Arthritis Research & Therapy.

iRhoms in the brain – a new frontier?

C. Blobel, B. O’Hara, S. Lichtenthaler, 2015, Cell cycle.

Adam Meets Eph: An ADAM Substrate Recognition Module Acts as a Molecular Switch for Ephrin Cleavage In trans

C. Blobel, E. Nievergall, P. W. Janes, 2005, Cell.

Identification of Molecular Determinants in iRhoms1 and 2 That Contribute to the Substrate Selectivity of Stimulated ADAM17

C. Blobel, Xia Li, J. M. Perez-Aguilar, 2022, International journal of molecular sciences.

Remarkable roles of proteolysis on and beyond the cell surface.

C. Blobel, Carl P. Blobel, 2000, Current opinion in cell biology.

iRhom2 promotes lupus nephritis through TNF-α and EGFR signaling

C. Blobel, T. Mak, L. Donlin, 2021 .

Biochemical and pharmacological criteria define two shedding activities for TRANCE/OPGL that are distinct from the tumor necrosis factor alpha convertase.

L. Lum, C. Blobel, J. Schlöndorff, 2001, The Journal of biological chemistry.

With blood in the joint – what happens next? Could activation of a pro‐inflammatory signalling axis leading to iRhom2/TNFα‐convertase‐dependent release of TNFα contribute to haemophilic arthropathy?

C. Blobel, C. Haxaire, 2014, Haemophilia : the official journal of the World Federation of Hemophilia.

ADAM10 Regulates Endothelial Permeability and T-Cell Transmigration by Proteolysis of Vascular Endothelial Cadherin

C. Blobel, P. Saftig, K. Reiss, 2008, Circulation research.

Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands

G. Weskamp, C. Blobel, D. Hartmann, 2004, The Journal of cell biology.

A potential fusion peptide and an integrin ligand domain in a protein active in sperm–egg fusion

T. Wolfsberg, C. Blobel, C. Turck, 1992, Nature.

Notch-RBP-J Signaling Regulates IRF8 to Promote Inflammatory Macrophage Polarization

C. Blobel, Yueming Li, L. Ivashkiv, 2012, Nature Immunology.

Phytochemicals Perturb Membranes and Promiscuously Alter Protein Function

Helgi I. Ingólfsson, Jon T. Sack, Katherine C. Hall, 2014, ACS chemical biology.

Identification of metalloprotease/disintegrins in Xenopus laevis testis with a potential role in fertilization.

G. Weskamp, C. Blobel, H. Cai, 1997, Developmental biology.

Tumor Necrosis Factor-α Converting Enzyme/ADAM 17 Mediates MUC1 Shedding*

C. Blobel, A. Thathiah, D. Carson, 2003, The Journal of Biological Chemistry.

Tumor necrosis factor-alpha converting enzyme/ADAM 17 mediates MUC1 shedding.

C. Blobel, A. Thathiah, D. Carson, 2003, The Journal of biological chemistry.

Pathological Neovascularization Is Reduced by Inactivation of ADAM17 in Endothelial Cells but Not in Pericytes

K. Horiuchi, G. Weskamp, C. Blobel, 2010, Circulation research.

A transforming Src mutant increases the bioavailability of EGFR ligands via stimulation of the cell-surface metalloproteinase ADAM17

C. Blobel, W. Zhou, T. Maretzky, 2011, Oncogene.

L1 Is Sequentially Processed by Two Differently Activated Metalloproteases and Presenilin/γ-Secretase and Regulates Neural Cell Adhesion, Cell Migration, and Neurite Outgrowth

C. Blobel, P. Altevogt, S. Rose-John, 2005, Molecular and Cellular Biology.

Proteolytic Processing of Delta-like 1 by ADAM Proteases*

C. Blobel, A. Sehara-Fujisawa, Emilia Dyczynska, 2007, Journal of Biological Chemistry.

ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor alpha, L-selectin, and tumor necrosis factor alpha.

K. Horiuchi, C. Blobel, D. Conrad, 2009, Molecular biology of the cell.

ADAM17 Controls Endochondral Ossification by Regulating Terminal Differentiation of Chondrocytes

Katherine C. Hall, C. Blobel, A. Boskey, 2013, Molecular and Cellular Biology.

Ectodomain shedding of EGFR ligands and TNFR1 dictates hepatocyte apoptosis during fulminant hepatitis in mice.

K. Horiuchi, C. Blobel, R. Khokha, 2010, The Journal of clinical investigation.

iRhom2 promotes lupus nephritis through TNF-&agr; and EGFR signaling

C. Blobel, T. Mak, L. Donlin, 2018, The Journal of clinical investigation.

Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE).

C. Blobel, J. Schlöndorff, J. Becherer, 2000, The Biochemical journal.

The Functional Maturation of A Disintegrin and Metalloproteinase (ADAM) 9, 10, and 17 Requires Processing at a Newly Identified Proprotein Convertase (PC) Cleavage Site*

Y. Peleg, C. Blobel, I. Sagi, 2015, The Journal of Biological Chemistry.

The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications.

T. Wolfsberg, C. Blobel, J. Bazan, 1993, Proceedings of the National Academy of Sciences of the United States of America.

MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains

G. Weskamp, C. Blobel, J. Krätzschmar, 1996, The Journal of cell biology.

ADAM12 is expressed in the tumour vasculature and mediates ectodomain shedding of several membrane-anchored endothelial proteins.

C. Blobel, P. Kronqvist, A. Kotzsch, 2013, The Biochemical journal.

Functional processing of fertilin: evidence for a critical role of proteolysis in sperm maturation and activation.

C. Blobel, 2000, Reviews of reproduction.

AM67, a Secretory Component of the Guinea Pig Sperm Acrosomal Matrix, Is Related to Mouse Sperm Protein sp56 and the Complement Component 4-binding Proteins*

C. Blobel, V. Winfrey, G. Olson, 1997, The Journal of Biological Chemistry.

Critical function for ADAM9 in mouse prostate cancer.

C. Blobel, V. Reuter, H. Scher, 2005, Cancer research.

Interaction of the Metalloprotease Disintegrins MDC9 and MDC15 with Two SH3 Domain-containing Proteins, Endophilin I and SH3PX1*

C. Blobel, R. Maciewicz, K. Nelson, 1999, The Journal of Biological Chemistry.

Migration of growth factor-stimulated epithelial and endothelial cells depends on EGFR transactivation by ADAM17.

S. Rafii, C. Blobel, K. Reiss, 2011, Nature communications.

ADAM8 is a negative regulator of retinal neovascularization and of the growth of heterotopically injected tumor cells in mice

G. Weskamp, C. Blobel, S. Swendeman, 2010, Journal of Molecular Medicine.

The disintegrin/metalloproteinase Adam10 is essential for epidermal integrity and Notch-mediated signaling

C. Blobel, B. de Strooper, R. Lüllmann-Rauch, 2011, Development.

Src stimulates fibroblast growth factor receptor-2 shedding by an ADAM15 splice variant linked to breast cancer.

C. Blobel, C. Overall, D. Edwards, 2009, Cancer research.

Stromal fibroblast-specific expression of ADAM-9 modulates proliferation and apoptosis in melanoma cells in vitro and in vivo.

C. Blobel, J. Landsberg, J. Fox, 2012, The Journal of investigative dermatology.

Different ADAMs have distinct influences on Kit ligand processing: phorbol-ester-stimulated ectodomain shedding of Kitl1 by ADAM17 is reduced by ADAM19

K. Horiuchi, C. Blobel, Y. Toyama, 2007, Journal of Cell Science.

Metalloprotease‐disintegrin ADAM8: Expression analysis and targeted deletion in mice

K. Horiuchi, K. Manova, C. Blobel, 2005, Developmental dynamics : an official publication of the American Association of Anatomists.

COMPONENTS IN EGFR SIGNALLING AND DEVELOPMENT

C. Blobel, 2004 .

Catalytic Properties of ADAM19*

C. Blobel, H. Erdjument-Bromage, P. Tempst, 2003, Journal of Biological Chemistry.

Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28.

C. Blobel, R. Maciewicz, L. Howard, 2000, The Biochemical journal.

Cloning and characterization of ADAM 28 : evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM 28

C. Blobel, R. Maciewicz, L. Howard, 2022 .

The Disintegrin/Metalloproteinase ADAM10 Is Essential for the Establishment of the Brain Cortex

G. Weskamp, C. Blobel, B. de Strooper, 2010, The Journal of Neuroscience.

ADAM17 is regulated by a rapid and reversible mechanism that controls access to its catalytic site

C. Blobel, R. Khokha, P. Saftig, 2010, Journal of Cell Science.

Lack of ADAM15 in mice is associated with increased osteoblast function and bone mass

R. Chiusaroli, R. Baron, C. Blobel, 2011, Biological chemistry.

The role of protease activity in ErbB biology.

C. Blobel, M. Freeman, G. Carpenter, 2009, Experimental cell research.

Targeted truncation of the ADAM17 cytoplasmic domain in mice results in protein destabilization and a hypomorphic phenotype

G. Weskamp, C. Blobel, J. Lora, 2021, The Journal of biological chemistry.

Interleukin-1 Stimulates ADAM17 through a Mechanism Independent of its Cytoplasmic Domain or Phosphorylation at Threonine 735

Katherine C. Hall, C. Blobel, 2012, PloS one.

Shedding of the Mer Tyrosine Kinase Receptor Is Mediated by ADAM17 Protein through a Pathway Involving Reactive Oxygen Species, Protein Kinase Cδ, and p38 Mitogen-activated Protein Kinase (MAPK)*

C. Blobel, T. Vaisar, I. Tabas, 2011, The Journal of Biological Chemistry.

Role of iRhoms 1 and 2 in Endochondral Ossification

G. Weskamp, C. Blobel, T. Mak, 2020, International journal of molecular sciences.

The waved with open eyelids (woe) Locus Is a Hypomorphic Mouse Mutation in Adam17

C. Blobel, C. Zeiss, B. Chang, 2010, Genetics.

Of Il-17 and G-csf Increased Granulopoiesis via Dysregulation Promoter Leads to Osteoporosis and Sox9 Conditional Inactivation of Tace by a Blobel and Yoshiaki Toyama

K. Horiuchi, C. Blobel, Y. Okada, 2022 .

Ectodomain shedding of the EGF‐receptor ligand epigen is mediated by ADAM17

C. Blobel, Umut Şahin, 2007, FEBS letters.

Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding.

C. Blobel, J. Schlöndorff, J. Schlondorff, 1999, Journal of cell science.

Essential Role for ADAM19 in Cardiovascular Morphogenesis

K. Horiuchi, G. Weskamp, R. Chiusaroli, 2004, Molecular and Cellular Biology.

Metalloprotease-Disintegrins: Links to Cell Adhesion and Cleavage of TNFα and Notch

C. Blobel, Carl P. Blobel, 1997, Cell.

Between VEGFR2 and ERK Signaling VEGF-A Stimulates ADAM17-Dependent Shedding of VEGFR2 and Crosstalk

S. Rafii, K. Horiuchi, G. Weskamp, 2008 .

Evidence for Regulation of the Tumor Necrosis Factor α-Convertase (TACE) by Protein-tyrosine Phosphatase PTPH1*

C. Blobel, Yufang Zheng, J. Schlöndorff, 2002, The Journal of Biological Chemistry.

Mice Lacking the Metalloprotease-Disintegrin MDC9 (ADAM9) Have No Evident Major Abnormalities during Development or Adult Life

G. Weskamp, T. Brodie, T. Ludwig, 2002, Molecular and Cellular Biology.

Evidence for a Critical Role of the Tumor Necrosis Factor α Convertase (TACE) in Ectodomain Shedding of the p75 Neurotrophin Receptor (p75NTR)*

G. Weskamp, L. Lum, C. Blobel, 2004, Journal of Biological Chemistry.

Neuronal Brain-derived Neurotrophic Factor Is Synthesized in Excess, with Levels Regulated by Sortilin-mediated Trafficking and Lysosomal Degradation

C. Blobel, P. Saftig, B. Hempstead, 2011, The Journal of Biological Chemistry.

Correction for Substrate Selectivity of Epidermal Growth Factor-Receptor Ligand Sheddases and their Regulation by Phorbol Esters and Calcium Influx

K. Horiuchi, C. Blobel, Y. Toyama, 2006, Molecular biology of the cell.

ADAM10 controls the differentiation of the coronary arterial endothelium

C. Blobel, S. Blanchard, S. Monette, 2018, Angiogenesis.

Neural crest-specific and general expression of distinct metalloprotease-disintegrins in early Xenopus laevis development.

C. Blobel, H. Cai, G. Hunnicutt, 1998, Developmental biology.

Chapter 2 STUDIES FROM ADAM KNOCKOUT MICE

C. Blobel, Keisuke Hoiruchi, 2006 .

Evaluation of the Contribution of Different ADAMs to Tumor Necrosis Factor α (TNFα) Shedding and of the Function of the TNFα Ectodomain in Ensuring Selective Stimulated Shedding by the TNFα Convertase (TACE/ADAM17)*

C. Blobel, D. Hartmann, P. Saftig, 2004, Journal of Biological Chemistry.

Studies from ADAM Knockout Mice

C. Blobel, Keisuke Hoiruchi, 2005 .

Intracellular Maturation of the Mouse Metalloprotease Disintegrin MDC15*

L. Lum, C. Blobel, Martha S. Reid, 1998, The Journal of Biological Chemistry.

ADAMs Regulate Cell–Cell Interactions by Controlling the Function of the EGF-Receptor, TNF α and Notch

C. Blobel, 2016 .

Shedding of Collagen XVII/BP180 in Skin Depends on Both ADAM10 and ADAM9*

C. Blobel, Claus-Werner Franzke, L. Bruckner-Tuderman, 2009, The Journal of Biological Chemistry.

Characterization of the catalytic activity of the membrane-anchored metalloproteinase ADAM15 in cell-based assays.

C. Blobel, C. Overall, U. Hassiepen, 2009, The Biochemical journal.

Evaluation of the contributions of ADAMs 9, 12, 15, 17, and 19 to heart development and ectodomain shedding of neuregulins beta1 and beta2.

K. Horiuchi, K. Manova, C. Blobel, 2005, Developmental biology.

ADAM12: a potential target for the treatment of chronic wounds

C. Blobel, O. Stojadinović, M. Tomic-Canic, 2008, Journal of Molecular Medicine.

ADAM10 controls the differentiation of the coronary arterial endothelium

C. Blobel, S. Blanchard, S. Monette, 2018, Angiogenesis.

Stimulation of Platelet-derived Growth Factor Receptor β (PDGFRβ) Activates ADAM17 and Promotes Metalloproteinase-dependent Cross-talk between the PDGFRβ and Epidermal Growth Factor Receptor (EGFR) Signaling Pathways*

C. Blobel, P. Saftig, S. Swendeman, 2010, The Journal of Biological Chemistry.

Apexin, an acrosomal pentaxin.

C. Blobel, M. Reid, 1994, The Journal of biological chemistry.

Endothelial deletion of ADAM10, a key regulator of Notch signaling, causes impaired decidualization and reduced fertility in female mice

C. Blobel, D. James, D. Dufort, 2020, Angiogenesis.

Impaired Trafficking and Activation of Tumor Necrosis Factor-α-converting Enzyme in Cell Mutants Defective in Protein Ectodomain Shedding*

C. Blobel, J. Baselga, A. Pandiella, 2003, Journal of Biological Chemistry.

Glomerular endothelial cell maturation depends on ADAM10, a key regulator of Notch signaling

C. Blobel, Raphael Kopan, C. Meyer-Schwesinger, 2018, Angiogenesis.

Metargidin, a Membrane-anchored Metalloprotease-Disintegrin Protein with an RGD Integrin Binding Sequence (*)

L. Lum, C. Blobel, J. Krätzschmar, 1996, The Journal of Biological Chemistry.

TNF-α-converting enzyme/a disintegrin and metalloprotease-17 mediates mechanotransduction in murine tracheal epithelial cells.

K. Horiuchi, C. Blobel, J. Drazen, 2011, American journal of respiratory cell and molecular biology.

Homeostatic effects of the metalloproteinase disintegrin ADAM15 in degenerative cartilage remodeling.

T. Brodie, C. Blobel, T. Aigner, 2005, Arthritis and rheumatism.

Potential Role for ADAM15 in Pathological Neovascularization in Mice

K. Horiuchi, G. Weskamp, L. Lum, 2003, Molecular and Cellular Biology.

Structural modeling defines transmembrane residues in ADAM17 that are crucial for Rhbdf2–ADAM17-dependent proteolysis

H. Weinstein, G. Weskamp, C. Blobel, 2017, Journal of Cell Science.

Characterization of oxygen-induced retinopathy in mice carrying an inactivating point mutation in the catalytic site of ADAM15.

C. Blobel, V. Guaiquil, T. Maretzky, 2014, Investigative ophthalmology & visual science.

ADAM9 Is Involved in Pathological Retinal Neovascularization

P. Campochiaro, C. Blobel, S. Chavala, 2009, Molecular and Cellular Biology.

Endothelial deletion of ADAM10, a key regulator of Notch signaling, causes impaired decidualization and reduced fertility in female mice

C. Blobel, D. James, D. Dufort, 2020, Angiogenesis.

The interferon-rich skin environment regulates Langerhans cell ADAM17 to promote photosensitivity in lupus

C. Blobel, P. Lipsky, I. Rogatsky, 2021, bioRxiv.

Catalytic activity of ADAM28

C. Blobel, R. Maciewicz, Yufang Zheng, 2001, FEBS letters.

Lack of ADAM10 in endothelial cells affects osteoclasts at the chondro‐osseus junction

Katherine C. Hall, G. Weskamp, C. Blobel, 2014, Journal of Orthopaedic Research.

Analysis of the function of ADAM17 in iRhom2-curly-bare (cub) and Tylosis with Oesophageal Cancer (TOC) mutant mice.

G. Weskamp, C. Blobel, S. Monette, 2023, Journal of cell science.

Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNF alpha and Notch.

C. Blobel, 1997, Cell.

Identification of Molecular Determinants in iRhoms1 and 2 That Contribute to the Substrate Selectivity of Stimulated ADAM17

C. Blobel, Xia Li, J. M. Perez-Aguilar, 2022, International journal of molecular sciences.

Conditional Inactivation of TACE by a Sox9 Promoter Leads to Osteoporosis and Increased Granulopoiesis via Dysregulation of IL-17 and G-CSF1

K. Horiuchi, C. Blobel, Y. Okada, 2009, The Journal of Immunology.

Characterization of the catalytic properties of the membrane-anchored metalloproteinase ADAM9 in cell-based assays.

G. Weskamp, C. Blobel, K. Reiss, 2017, The Biochemical journal.

Tumor Necrosis Factor- Converting Enzyme/ADAM 17 Mediates MUC1 Shedding*

C. Blobel, A. Thathiah, D. Carson, 2003 .

Src stimulates fibroblast growth factor receptor-2 shedding by an ADAM15 splice variant linked to breast cancer.

C. Blobel, C. Overall, D. Edwards, 2009, Cancer research.